IP Library Granted Patent US 12,391,729
Granted Patent B2
US 12,391,729 · App. 18/398,650 · Granted Aug 19, 2025

Fusion proteins, recombinant bacteria, and methods for using recombinant bacteria

Inventors: Brian Thompson (Creve Coeur, MO); Ashley Siegel (St. Louis, MO)
Assignee: Spogen Biotech Inc.
C07K14/32A01H3/00A01N37/44A01N63/10A01N63/50A23K20/147A61L2/18C02F3/342C02F3/348C09K8/62C12N1/20C12N3/00C12N15/62C12N15/75C12P21/02E21B43/16A01N63/20A23K10/18A61K39/00C02F2101/10C02F2101/30C02F2103/002C02F2103/003C02F2103/007C02F2103/06C02F2103/10C02F2103/14C02F2103/16C02F2103/26C02F2103/28C07K2319/01C07K2319/035C07K2319/40C09K2208/24
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,391,729
App. No.
18/398,650
Granted
Aug 19, 2025
Kind
B2
Abstract

Fusion proteins containing a targeting sequence, an exosporium protein, or an exosporium protein fragment that targets the fusion protein to the exosporium of a Bacillus cereus family member are provided. Recombinant Bacillus cereus family members expressing such fusion proteins are also provided. Genetically inactivated Bacillus cereus family members and recombinant Bacillus cereus family members that overexpress exosporium proteins are also provided. Seeds coated with the recombinant Bacillus cereus family members and methods for using the recombinant Bacillus cereus family members (e.g., for stimulating plant growth) are also provided. Various modifications of the recombinant Bacillus cereus family members that express the fusion proteins are further provided. Fusion proteins comprising a spore coat protein and a protein or peptide of interest, recombinant bacteria that express such fusion proteins, seeds coated with such recombinant bacteria, and methods for using such recombinant bacteria (e.g., for stimulating plant growth) are also provided.

Claims (26)

1. A plant seed coated with a Bacillus cereus superoxide dismutase or a Bacillus thuringiensis superoxide dismutase.

2. The plant seed of claim 1 , wherein the superoxide dismutase comprises superoxide dismutase 1 (SODA1) or superoxide dismutase 2 (SODA2).

3. The plant seed of claim 1 , wherein the superoxide dismutase comprises an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% identity with SEQ ID NO: 155 or 156.

4. The plant seed of claim 1 , wherein the seed is coated with a formulation comprising the superoxide dismutase and an agriculturally acceptable carrier.

5. The plant seed of claim 4 , wherein the agriculturally acceptable carrier comprises a dispersant, a surfactant, an additive, water, a thickener, an anti-caking agent, residue breakdown, a composting formulation, a granular application, diatomaceous earth, an oil, a coloring agent, a stabilizer, a preservative, a polymer, a coating, or a combination thereof.

6. The plant seed of claim 5 , wherein the agriculturally acceptable carrier comprises an additive, and the additive comprises an oil, a gum, a resin, a clay, a polyoxyethylene glycol, a terpene, a viscid organic, a fatty acid ester, a sulfated alcohol, an alkyl sulfonate, a petroleum sulfonate, an alcohol sulfate, a sodium alkyl butane diamate, a polyester of sodium thiobutane dioate, a benzene acetonitrile derivative, a proteinaceous material, or a combination thereof; the agriculturally acceptable carrier comprises a thickener, and the thickener comprises a long chain alkylsulfonate of polyethylene glycol, a polyoxyethylene oleate, or a combination thereof; the agriculturally acceptable carrier comprises a surfactant, and the surfactant comprises a heavy petroleum oil, a heavy petroleum distillate, a polyol fatty acid ester, a polyethoxylated fatty acid ester, an aryl alkyl polyoxyethylene glycol, an alkyl amine acetate, an alkyl aryl sulfonate, a polyhydric alcohol, an alkyl phosphate, or a combination thereof; or the agriculturally acceptable carrier comprises an anti-caking agent, and the anti-caking agent comprises a sodium salt, a calcium carbonate, diatomaceous earth, or a combination thereof.

7. The plant seed of claim 6 , wherein additive comprises a proteinaceous material, and the proteinaceous material comprises a milk product, wheat flour, soybean meal, blood, albumin, gelatin, alfalfa meal, yeast extract, or a combination thereof; or the anti-caking agent comprises a sodium salt, and the sodium salt comprises a sodium salt of monomethyl naphthalene sulfonate, a sodium salt of dimethyl naphthalene sulfonate, a sodium sulfite, a sodium sulfate, or a combination thereof.

8. The plant seed of claim 4 , wherein the agriculturally acceptable carrier comprises vermiculite, charcoal, sugar factory carbonation press mud, rice husk, carboxymethyl cellulose, peat, perlite, fine sand, calcium carbonate, flour, alum, a starch, talc, polyvinyl pyrrolidone, or a combination thereof.

9. The plant seed of claim 4 , wherein the seed coating formulation comprises an aqueous or oil-based solution for application to seeds or a powder or granular formulation for application to seeds.

10. The plant seed of claim 4 , wherein the formulation further comprises an agrochemical, the agrochemical comprising a fertilizer, a micronutrient fertilizer material, an insecticide, an herbicide, a plant growth amendment, a fungicide, an insecticide, a molluscicide, an algicide, a bacterial inoculant, a fungal inoculant, or a combination thereof.

11. The plant seed of claim 10 , wherein the formulation comprises a bacterial inoculant and the bacterial inoculant comprises a plant-growth promoting strain of bacteria.

12. The plant seed of claim 11 , wherein the plant-growth promoting strain of bacteria produces an insecticidal toxin, produces a fungicidal compound, produces a nematocidal compound, produces a bactericidal compound, is resistant to one or more antibiotics, comprises one or more freely replicating plasmids, binds to plant roots, colonizes plant roots, forms biofilms, solubilizes nutrients, and/or secretes organic acids.

13. The plant seed of claim 12 , wherein the insecticidal toxin comprises a Cry toxin; wherein the fungicidal compound comprises a β-1,3-glucanase, a chitosanase, a lyticase, or a combination thereof; or wherein the nematocidal compound comprises a Cry toxin.

14. The plant seed of claim 11 , wherein the plant-growth promoting strain of bacteria comprises Bacillus aryabhattai CAP53 (NRRL No. B-50819), Bacillus aryabhattai CAP56 (NRRL No. B-50817), Bacillus flexus BT054 (NRRL No. B-50816), Paracoccus kondratievae NC35 (NRRL No. B-50820), Bacillus mycoides BT155 (NRRL No. B-50921), Enterobacter cloacae CAP12 (NRRL No. B-50822), Bacillus nealsonii BOBA57 (NRRL No. NRRL B-50821), Bacillus mycoides EE118 (NRRL No. B-50918), Bacillus subtilis EE148 (NRRL No. B-50927), Alcaligenes faecalis EE107 (NRRL No. B-50920), Bacillus mycoides EE141 (NRRL NO. B-50916), Bacillus mycoides BT46-3 (NRRL No. B-50922), Bacillus cereus family member EE128 (NRRL No. B-50917), Bacillus thuringiensis BT013A (NRRL No. B-50924), Paenibacillus massiliensis BT23 (NRRL No. B-50923), Bacillus cereus family member EE349 (NRRL No. B-50928), Bacillus subtilis EE218 (NRRL No. B-50926), Bacillus megaterium EE281 (NRRL No. B-50925), Bacillus cereus family member EE-B00377 (NRRL B-67119); Bacillus pseudomycoides EE-B00366 (NRRL B-67120), Bacillus mycoides EE-B00363 (NRRL B-67121), Bacillus pumilus EE-B00143 (NRRL B-67123), or Bacillus thuringiensis EE-B00184 (NRRL B-67122), or a combination thereof.

15. The plant seed of claim 10 , wherein the agrochemical comprises a fertilizer, and the fertilizer comprises a liquid fertilizer; wherein the agrochemical comprises a micronutrient fertilizer material and the micronutrient fertilizer material comprises boric acid, a borate, a boron frit, copper sulfate, a copper frit, a copper chelate, a sodium tetraborate decahydrate, an iron sulfate, an iron oxide, iron ammonium sulfate, an iron frit, an iron chelate, a manganese sulfate, a manganese oxide, a manganese chelate, a manganese chloride, a manganese frit, a sodium molybdate, molybdic acid, a zinc sulfate, a zinc oxide, a zinc carbonate, a zinc frit, zinc phosphate, a zinc chelate, or a combination thereof; wherein the agrochemical comprises an insecticide, and the insecticide comprises an organophosphate, a carbamate, a pyrethroid, an acaricide, an alkyl phthalate, boric acid, a borate, a fluoride, sulfur, a haloaromatic substituted urea, a hydrocarbon ester, a biologically-based insecticide, or a combination thereof; wherein the agrochemical comprises an herbicide, and the herbicide comprises a chlorophenoxy compound, a nitrophenolic compound, a nitrocresolic compound, a dipyridyl compound, an acetamide, an aliphatic acid, an anilide, a benzamide, a benzoic acid, a benzoic acid derivative, anisic acid, an anisic acid derivative, a benzonitrile, benzothiadiazinone dioxide, a thiocarbamate, a carbamate, a carbanilate, chloropyridinyl, a cyclohexenone derivative, a dinitroaminobenzene derivative, a fluorodinitrotoluidine compound, isoxazolidinone, nicotinic acid, isopropylamine, an isopropylamine derivative, oxadiazolinone, a phosphate, a phthalate, a picolinic acid compound, a triazine, a triazole, a uracil, a urea derivative, endothall, sodium chlorate, or a combination thereof; wherein the agrochemical comprises a fungicide, and the fungicide comprises a substituted benzene, a thiocarbamate, an ethylene bis dithiocarbamate, a thiophthalidamide, a copper compound, an organomercury compound, an organotin compound, a cadmium compound, anilazine, benomyl, cyclohexamide, dodine, etridiazole, iprodione, metlaxyl, thiamimefon, triforine, or a combination thereof; wherein the agrochemical comprises a fungal inoculant and the fungal inoculant comprises a fungal inoculant of the family Glomeraceae, a fungal inoculant of the family Claroidoglomeraceae, a fungal inoculant of the family Gigasporaceae, a fungal inoculant of the family Acaulosporaceae, a fungal inoculant of the family Sacculosporaceae, a fungal inoculant of the family Entrophosporaceae, a fungal inoculant of the family Pacidsporaceae, a fungal inoculant of the family Diversisporaceae, a fungal inoculant of the family Paraglomeraceae, a fungal inoculant of the family Archaeosporaceae, a fungal inoculant of the family Geosiphonaceae, a fungal inoculant of the family Ambisporaceae, a fungal inoculant of the family Scutellosporaceae, a fungal inoculant of the family Dentiscultataceae, a fungal inoculant of the family Racocetraceae, a fungal inoculant of the phylum Basidiomycota, a fungal inoculant of the phylum Ascomycota, a fungal inoculant of the phylum Zygomycota, or a combination thereof; or wherein the agrochemical comprises a bacterial inoculant and the bacterial inoculant comprises a bacterial inoculant of the genus Rhizobium , a bacterial inoculant of the genus Bradyrhizobium , a bacterial inoculant of the genus Mesorhizobium , a bacterial inoculant of the genus Azorhizobium , a bacterial inoculant of the genus Allorhizobium , a bacterial inoculant of the genus Sinorhizobium , a bacterial inoculant of the genus Kluyvera , a bacterial inoculant of the genus Azotobacter , a bacterial inoculant of the genus Pseudomonas , a bacterial inoculant of the genus Azospirillium , a bacterial inoculant of the genus Bacillus , a bacterial inoculant of the genus Streptomyces , a bacterial inoculant of the genus Paenibacillus , a bacterial inoculant of the genus Paracoccus , a bacterial inoculant of the genus Enterobacter , a bacterial inoculant of the genus Alcaligenes , a bacterial inoculant of the genus Mycobacterium , a bacterial inoculant of the genus Trichoderma , a bacterial inoculant of the genus Gliocladium , a bacterial inoculant of the genus Glomus , a bacterial inoculant of the genus Klebsiella , or a combination thereof.

16. The plant seed of claim 10 , wherein the agrochemical comprises a fungicide, and the fungicide comprises aldimorph, ampropylfos, ampropylfos potassium, andoprim, anilazine, azaconazole, azoxystrobin, benalaxyl, benodanil, benomyl, benzamacril, benzamacryl-isobutyl, bialaphos, binapacryl, biphenyl, bitertanol, blasticidin-S, boscalid, bromuconazole, bupirimate, buthiobate, calcium polysulphide, capsimycin, captafol, captan, carbendazim, carvon, quinomethionate, chlobenthiazone, chlorfenazole, chloroneb, chloropicrin, chlorothalonil, chlozolinate, clozylacon, cufraneb, cymoxanil, cyproconazole, cyprodinil, cyprofuram, debacarb, dichlorophen, diclobutrazole, diclofluanid, diclomezine, dicloran, diethofencarb, dimethirimol, dimethomorph, dimoxystrobin, diniconazole, diniconazole-M, dinocap, diphenylamine, dipyrithione, ditalimfos, dithianon, dodemorph, dodine, drazoxolon, edifenphos, epoxiconazole, etaconazole, ethirimol, etridiazole, famoxadon, fenapanil, fenarimol, fenbuconazole, fenfuram, fenitropan, fenpiclonil, fenpropidin, fenpropimorph, fentin acetate, fentin hydroxide, ferbam, ferimzone, fluazinam, flumetover, fluoromide, fluquinconazole, flurprimidol, flusilazole, flusulfamide, flutolanil, flutriafol, folpet, fosetyl-aluminium, fosetyl-sodium, fthalide, fuberidazole, furalaxyl, furametpyr, furcarbonil, furconazole, furconazole-cis, furmecyclox, guazatine, hexachlorobenzene, hexaconazole, hymexazole, imazalil, imibenconazole, iminoctadine, iminoctadine albesilate, iminoctadine triacetate, iodocarb, iprobenfos (IBP), iprodione, irumamycin, isoprothiolane, isovaledione, kasugamycin, kresoxim-methyl, copper hydroxide, copper naphthenate, copper oxychloride, copper sulphate, copper oxide, oxine-copper, Bordeaux mixture, mancopper, mancozeb, maneb, meferimzone, mepanipyrim, mepronil, metconazole, methasulfocarb, methfuroxam, metiram, metomeclam, metsulfovax, mildiomycin, myclobutanil, myclozolin, nickel dimethyldithiocarbamate, nitrothal-isopropyl, nuarimol, ofurace, oxadixyl, oxamocarb, oxolinic acid, oxycarboxim, oxyfenthiin, paclobutrazole, pefurazoate, penconazole, pencycuron, phosdiphen, pimaricin, piperalin, polyoxin, polyoxorim, probenazole, prochloraz, procymidone, propamocarb, propanosine-sodium, propiconazole, propineb, prothioconazole, pyrazophos, pyrifenox, pyrimethanil, pyroquilon, pyroxyfur, quinconazole, quintozene (PCNB), sulphur and sulphur preparations, tebuconazole, tecloftalam, tecnazene, tetcyclasis, tetraconazole, thiabendazole, thicyofen, thifluzamide, thiophanate-methyl, tioxymid, tolclofos-methyl, tolylfluanid, triadimefon, triadimenol, triazbutil, triazoxide, trichlamide, tricyclazole, tridemorph, trifloxystrobin, triflumizole, triforine, uniconazole, validamycin A, vinclozolin, viniconazole, zarilamide, zineb, ziram, Dagger G, OK-8705, OK-8801, α-(1,1-dimethylethyl)-(3-(2-phenoxyethyl)-1H-1,2,4-triazole-1-ethanol, α-(2,4-dichlorophenyl)-[3-fluoro-3-propyl-1H-1,2,4-triazole-1-ethanol, α-(2,4-dichlorophenyl)-[3-methoxy-α-methyl-1H-1,2,4-triazole-1-ethanol, α-(5-methyl-1,3-dioxan-5-yl)-[3-[4-(trifluoromethyl)-phenyl]-methylene]-1H-1,2,4-triazole-1-ethanol, (E)-α-(methoxyimino)-N-methyl-2-phenoxy-phenylacetamide, 1-isopropyl{2-methyl-1-[[[1-(4-methylphenyl)-ethyl]-amino]-carbonyl]-propyl}carbamate, 1-(2,4-dichlorophenyl)-2-(1H-1,2,4-triazol-1-yl)-ethanone-O-(phenyl methyl)-oxime, 1-(2-methyl-1-naphthalenyl)-1H-pyrrole-2,5-dione, 1-(3,5-dichlorophenyl)-3-(2-propenyl)-2,5-pyrrolidindione, 1-[(diiodomethyl)-sulphonyl]-4-methyl-benzene, 1-[[2-(2,4-dichlorophenyl)-1, 3-dioxolan-2-yl]-methyl]-1H-imidazole, 1-[[2-(4-chlorophenyl)-3-phenyloxiranyl]-methyl]-1H-1,2,4-triazole, 1-[1-[2-[(2,4-dichlorophenyl)-methoxy]-phenyl]-ethenyl]-1H-imidazole, 1-methyl-5-nonyl-2-(phenylmethyl)-3-pyrrolidinole, 2′,6′-dibromo-2-methyl-4′-trifluoromethoxy-4′-trifluoro-methyl-1, 3-thiazole-carboxanilide, 2,2-dichloro-N-[1-(4-chlorophenyl)-ethyl]-1-ethyl-3-methyl-cyclopropanecarboxamide, 2,6-dichloro-5-(methylthio)-4-pyrimidinyl-thiocyanate, 2,6-dichloro-N-(4-trifluoromethylbenzyl)-benzamide, 2,6-dichloro-N-[[4-(trifluoromethyl)-phenyl]-methyl]-benzamide, 2-(2,3,3-triiodo-2-propenyl)-2H-tetrazole, 2-[(1-methylethyl)-sulphonyl]-5-(trichloromethyl)-1,3,4-thiadiazole, 2-[[6-deoxy-4-O-(4-O-methyl-β-D-glucopyranosyl)-α-D-glucopyranosyl]amino]-4-methoxy-1H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile, 2-aminobutane, 2-bromo-2-(bromomethyl)-pentanedinitrile, 2-chloro-N-(2,3-dihydro-1,1,3-trimethyl-1H-inden-4-yl)-3-pyridinecarboxamide, 2-chloro-N-(2,6-dimethylphenyl)-N-(isothiocyanatomethyl)-acetamide, 2-phenylphenol (OPP), 3,4-dichloro-1-[4-(difluoromethoxy)-phenyl]-pyrrole-2,5-dione, 3,5-dichloro-N-[cyano[(1-methyl-2-propynyl)-oxy]-methyl]-benzamide, 3-(1,1-dimethylpropyl-1-oxo-1H-indene-2-carbonitrile, 3-[2-(4-chlorophenyl)-5-ethoxy-3-isoxazolidinyl]-pyridine, 4-chloro-2-cyano-N,N-dimethyl-5-(4-methylphenyl)-1H-imidazole-1-sulphonamide, 4-methyl-tetrazolo[1,5-a]quinazolin-5 (4H)-one, 8-(1,1-dimethylethyl)-N-ethyl-N-propyl-1,4-dioxaspiro[4, 5]decane-2-methanamine, 8-hydroxyquinoline sulphate, 9H-xanthene-2-[(phenylamino)-carbonyl]-9-carboxylic hydrazide, bis-(1-methylethyl)-3-methyl-4-[(3-methylbenzoyl)-oxy]-2,5-thiophenedicarboxylate, cis-1-(4-chlorophenyl)-2-(1H-1,2,4-triazol-1-yl)-cycloheptanol, cis-4-[3-[4-(1,1-dimethylpropyl)-phenyl-2-methylpropyl]-2,6-dimethyl-morpholine hydrochloride, ethyl[(4-chlorophenyl)-azo]-cyanoacetate, potassium bicarbonate, methanetetrathiol-sodium salt, methyl 1-(2,3-dihydro-2,2-dimethyl-inden-1-yl)-1H-imidazole-5-carboxylate, methyl N-(2,6-dimethylphenyl)-N-(5-isoxazolylcarbonyl)-DL-alaninate, methyl N-(chloroacetyl)-N-(2,6-dimethylphenyl)-DL-alaninate, N-(2,3-dichloro-4-hydroxyphenyl)-1-methyl-cyclohexanecarboxamide, N-(2,6-dimethyl phenyl)-2-methoxy-N-(tetra hydro-2-oxo-3-furanyl)-acetamide, N-(2,6-dimethyl phenyl)-2-methoxy-N-(tetrahydro-2-oxo-3-thienyl)-acetamide, N-(2-chloro-4-nitrophenyl)-4-methyl-3-nitro-benzenesulphonamide, N-(4-cyclohexylphenyl)-1,4,5,6-tetrahydro-2-pyrimidinamine, N-(4-hexylphenyl)-1,4,5,6-tetrahydro-2-pyrimidinamine, N-(5-chloro-2-methylphenyl)-2-methoxy-N-(2-oxo-3-oxazolidinyl)-acetamide, N-(6-methoxy)-3-pyridinyl)-cyclopropanecarboxamide, N-[2,2,2-trichloro-1-[(chloroacetyl)-amino]-ethyl]-benzamide, N-[3-chloro-4,5-bis(2-propinyloxy)-phenyl]-N′-methoxy-methanimidamide, N-formyl-N-hydroxy-DL-alanine-sodium salt, O,O-diethyl[2-(dipropylamino)-2-oxoethyl]-ethylphosphoramidothioate, O-methyl S-phenyl phenylpropylphosphoramidothioate, S-methyl 1,2,3-benzothiadiazole-7-carbothioate, and spiro[2H]-1-benzopyrane-2,1′(3′H)-isobenzofuran]-3′-one, tetramethylthioperoxydicarbonic diamide, methyl N-(2,6-dimethylphenyl)-N-(methoxyacetyl)-DL-alaninate, 4-(2,2-difluoro-1,3-benzodioxol-4-yl)-1-H-pyrrol-3-carbonitril, or a combination thereof.

17. The plant seed of claim 10 , wherein the agrochemical comprises a bacterial inoculant of the genus Bacillus , and the bacterial inoculant of the genus Bacillus comprises Bacillus argri, Bacillus aizawai, Bacillus albolactis, Bacillus amyloliquefaciens, Bacillus cereus, Bacillus coagulans, Bacillus endoparasiticus, Bacillus endorhythmos, Bacillus kurstaki, Bacillus lacticola, Bacillus lactimorbus, Bacillus lactis, Bacillus laterosporus, Bacillus lentimorbus, Bacillus licheniformis, Bacillus megaterium, Bacillus medusa, Bacillus metiens, Bacillus natto, Bacillus nigrificans, Bacillus popillae, Bacillus pumilus, Bacillus siamensis, Bacillus sphearicus, Bacillus spp., Bacillus subtilis, Bacillus thuringiensis, Bacillus unifagellatu , or a combination thereof.

18. The plant seed of claim 10 , wherein the agrochemical comprises an herbicide, and the herbicide comprises 2,4-D, 2,4-DB, acetochlor, acifluorfen, alachlor, ametryn, atrazine, aminopyralid, benefin, bensulfuron, bensulide, bentazon, bromacil, bromoxynil, butylate, carfentrazone, chlorimuron, chlorsulfuron, clethodim, clomazone, clopyralid, cloransulam, cycloate, DCPA, desmedipham, dicamba, dichlobenil, diclofop, diclosulam, diflufenzopyr, dimethenamid, diquat, diuron, DSMA, endothall, EPTC, ethalfluralin, ethofumesate, fenoxaprop, fluazifop-P, flucarbazone, flufenacet, flumetsulam, flumiclorac, flumioxazin, fluometuron, fluroxypyr, fomesafen, foramsulfuron, glufosinate, glyphosate, halosulfuron, hexazinone, imazamethabenz, imazamox, imazapic, imazaquin, imazethapyr, isoxaben, isoxaflutole, lactofen, linuron, MCPA, MCPB, mesotrione, metolachlor-s, metribuzin, metsulfuron, molinate, MSMA, napropamide, naptalam, nicosulfuron, norflurazon, oryzalin, oxadiazon, oxyfluorfen, paraquat, pelargonic acid, pendimethalin, phenmedipham, picloram, primisulfuron, prodiamine, prometryn, pronamide, propanil, prosulfuron, pyrazon, pyrithiobac, quinclorac, quizalofop, rimsulfuron, sethoxydim, siduron, simazine, sulfentrazone, sulfometuron, sulfosulfuron, tebuthiuron, terbacil, thiazopyr, thifensulfuron, thiobencarb, tralkoxydim, triallate, triasulfuron, tribenuron, triclopyr, trifluralin, triflusulfuron, or a combination thereof.

19. The plant seed of claim 10 , wherein the formulation comprises the herbicide and the bacterial inoculum, wherein the bacterial inoculum comprises a strain of bacteria capable of degrading the herbicide.

20. The plant seed of claim 19 , wherein the strain of bacteria that is capable of degrading an herbicide comprises Bacillus cereus family member EE349 (NRRL No. B-50928), Bacillus cereus family member EE-B00377 (NRRL B-67119), Bacillus pseudomycoides EE-B00366 (NRRL B-67120), or Bacillus mycoides EE-B00363 (NRRL B-67121), or a combination thereof.

21. The plant seed of claim 19 , wherein the herbicide comprises a sulfonylurea, an aryl triazine, dicamba, a phenoxy herbicide, 2,4-D, a pyrethrin, a pyrethroid, or a combination thereof.

22. The plant seed of claim 21 , wherein the sulfonylurea comprises sulfentrazone.

23. The plant seed of claim 10 , wherein the fertilizer comprises ammonium sulfate, ammonium nitrate, ammonium sulfate nitrate, ammonium chloride, ammonium bisulfate, ammonium polysulfide, ammonium thiosulfate, aqueous ammonia, anhydrous ammonia, ammonium polyphosphate, aluminum sulfate, calcium nitrate, calcium ammonium nitrate, calcium sulfate, calcined magnesite, calcitic limestone, calcium oxide, calcium nitrate, dolomitic limestone, hydrated lime, calcium carbonate, diammonium phosphate, monoammonium phosphate, magnesium nitrate, magnesium sulfate, potassium nitrate, potassium chloride, potassium magnesium sulfate, potassium sulfate, sodium nitrates, magnesian limestone, magnesia, urea, urea-formaldehydes, urea ammonium nitrate, sulfur-coated urea, polymer-coated urea, isobutylidene diurea, langbeinite, kainite, sylvinite, kieserite, Epsom salts, elemental sulfur, marl, ground oyster shells, fish meal, oil cakes, fish manure, blood meal, rock phosphate, super phosphates, slag, bone meal, wood ash, manure, bat guano, peat moss, compost, green sand, cottonseed meal, feather meal, crab meal, fish emulsion, humic acid, or a combination thereof.

24. The plant seed of claim 4 , wherein the formulation comprises a salt of iron, manganese, boron, copper, cobalt, molybdenum, zinc, or a combination of any thereof.

25. A method for stimulating germination of a plant seed comprising:

introducing into a plant growth medium comprising a seed, or applying to a plant seed, or an area surrounding a plant seed a Bacillus cereus superoxide dismutase or a Bacillus thuringiensis superoxide dismutase.

Continuity (6)
Division 17079942 · Oct 26, 2020
Continuation 16563086 · Sep 6, 2019
Division 15842062 · Dec 14, 2017
Continuation 14857606 · Sep 17, 2015
Provisional Application 62051885 · Sep 17, 2014
Related Publication 20240199709A1 · Jun 20, 2024
References Cited (400)
US 5290914A · Wilcox et al. · 1994 [cited by applicant]
US 5348743A · Ryals et al. · 1994 [cited by applicant]
US 5466449A · Witold · 1995 [cited by applicant]
US 5503652A · Kloepper et al. · 1996 [cited by applicant]
US 5766914A · Deits · 1998 [cited by applicant]
US 5776448A · Suslow et al. · 1998 [cited by applicant]
US 5858962A · Blackburn et al. · 1999 [cited by applicant]
US 5958104A · Nonomura et al. · 1999 [cited by applicant]
US 6110372A · Perriello · 2000 [cited by applicant]
US 6184440B1 · Shoseyov et al. · 2001 [cited by applicant]
US 6232270B1 · Branly et al. · 2001 [cited by applicant]
US 6309440B1 · Yamashita · 2001 [cited by applicant]
US 6323023B1 · Shoseyov et al. · 2001 [cited by applicant]
US 6333302B1 · Beer et al. · 2001 [cited by applicant]
US 6548743B1 · Sheen et al. · 2003 [cited by applicant]
US 6630340B2 · Wilting et al. · 2003 [cited by applicant]
US 7393678B2 · Triplett et al. · 2008 [cited by applicant]
US 7417181B2 · Wang et al. · 2008 [cited by applicant]
US 7432097B2 · Short et al. · 2008 [cited by applicant]
US 7504120B2 · Steer et al. · 2009 [cited by applicant]
US 7615681B2 · Georges et al. · 2009 [cited by applicant]
US 7919678B2 · Mironov · 2011 [cited by applicant]
US 7960148B2 · Steer et al. · 2011 [cited by applicant]
US 8030064B2 · Lee et al. · 2011 [cited by applicant]
US 8080404B1 · Turetsky et al. · 2011 [cited by applicant]
US 8097769B2 · Sarria-Millan et al. · 2012 [cited by applicant]
US 8105613B2 · Flick-Smith et al. · 2012 [cited by applicant]
US 8114659B2 · Rawson et al. · 2012 [cited by applicant]
US 8383366B2 · Ferrari et al. · 2013 [cited by applicant]
US 8461419B2 · He et al. · 2013 [cited by applicant]
US 8614078B2 · Lin et al. · 2013 [cited by applicant]
US 8673311B2 · Cutting et al. · 2014 [cited by applicant]
US 9068194B2 · Unkefer et al. · 2015 [cited by applicant]
US 9125419B2 · Asolkar et al. · 2015 [cited by applicant]
US 9132175B2 · Stewart et al. · 2015 [cited by applicant]
US 9133251B2 · Stewart et al. · 2015 [cited by applicant]
US 9392796B2 · Thompson et al. · 2016 [cited by applicant]
US 9476058B2 · Lim · 2016 [cited by applicant]
US 9540633B2 · Brinch-Pedersen et al. · 2017 [cited by applicant]
US 9573980B2 · Thompson et al. · 2017 [cited by applicant]
US 9713632B2 · van der Weerden · 2017 [cited by applicant]
US 9826743B2 · Curtis et al. · 2017 [cited by applicant]
US 9845342B2 · Thompson et al. · 2017 [cited by applicant]
US 9850289B2 · Thompson et al. · 2017 [cited by applicant]
US 9956277B2 · Stewart et al. · 2018 [cited by applicant]
US 10081790B2 · Stewart et al. · 2018 [cited by applicant]
US 10092009B2 · Thompson et al. · 2018 [cited by applicant]
US 10173938B2 · Rosas Gajardo et al. · 2019 [cited by applicant]
US 10349660B2 · Thompson et al. · 2019 [cited by applicant]
US 10407472B2 · Thompson et al. · 2019 [cited by applicant]
US 10448647B2 · Curtis et al. · 2019 [cited by applicant]
US 10555532B2 · Thompson et al. · 2020 [cited by applicant]
US 10555534B2 · Thompson et al. · 2020 [cited by applicant]
US 10667522B2 · Curtis et al. · 2020 [cited by applicant]
US 10779542B2 · Thompson et al. · 2020 [cited by applicant]
US 10836800B2 · Thompson et al. · 2020 [cited by applicant]
US 10851027B2 · Adam · 2020 [cited by applicant]
US 11124460B2 · Thompson et al. · 2021 [cited by applicant]
US 11134681B2 · Thompson et al. · 2021 [cited by applicant]
US 11406107B2 · Curtis et al. · 2022 [cited by applicant]
US 11882829B2 · Thompson et al. · 2024 [cited by applicant]
US 11905315B2 · Thompson et al. · 2024 [cited by applicant]
US 12031164B2 · Thompson et al. · 2024 [cited by applicant]
US 20030026797A1 · Beudeker · 2003 [cited by applicant]
US 20030167506A1 · Multani et al. · 2003 [cited by applicant]
US 20030228679A1 · Smith et al. · 2003 [cited by applicant]
US 20040077090A1 · Short · 2004 [cited by applicant]
US 20050232947A1 · Cutting · 2005 [cited by applicant]
US 20070184018A1 · Lahm et al. · 2007 [cited by applicant]
US 20080233175A1 · Steer et al. · 2008 [cited by applicant]
US 20080248953A1 · Smith et al. · 2008 [cited by applicant]
US 20090099079A1 · Emalfarb et al. · 2009 [cited by applicant]
US 20090192040A1 · Grobler · 2009 [cited by applicant]
US 20100055244A1 · Henriques et al. · 2010 [cited by applicant]
US 20100071093A1 · Sarria-Millan · 2010 [cited by applicant]
US 20100205690A1 · Blasing et al. · 2010 [cited by applicant]
US 20100233124A1 · Stewart et al. · 2010 [cited by applicant]
US 20100291100A1 · Macinga · 2010 [cited by applicant]
US 20110281316A1 · Stewart et al. · 2011 [cited by applicant]
US 20110321197A1 · Schon et al. · 2011 [cited by applicant]
US 20120227134A1 · Schon et al. · 2012 [cited by applicant]
US 20120259101A1 · Tan et al. · 2012 [cited by applicant]
US 20120266327A1 · Sanz Molinero et al. · 2012 [cited by applicant]
US 20130216653A1 · Perkins et al. · 2013 [cited by applicant]
US 20130345056A1 · Sada · 2013 [cited by applicant]
US 20140031576A1 · Toriumi · 2014 [cited by applicant]
US 20140259225A1 · Frank et al. · 2014 [cited by applicant]
US 20140274691A1 · Thompson · 2014 [cited by examiner]
US 20140274707A1 · Thompson et al. · 2014 [cited by applicant]
US 20140294883A1 · Poobalane et al. · 2014 [cited by applicant]
US 20140342905A1 · Bullis et al. · 2014 [cited by applicant]
US 20150274605A1 · Waldron et al. · 2015 [cited by applicant]
US 20150296785A1 · Sawada et al. · 2015 [cited by applicant]
US 20160031948A1 · Thompson et al. · 2016 [cited by applicant]
US 20160051656A1 · Stewart et al. · 2016 [cited by applicant]
US 20160053222A1 · Stewart et al. · 2016 [cited by applicant]
US 20160236996A1 · Chaudhry · 2016 [cited by applicant]
US 20160262402A1 · Thompson et al. · 2016 [cited by applicant]
US 20160278384A1 · Jabs · 2016 [cited by examiner]
US 20160316761A1 · Thompson et al. · 2016 [cited by applicant]
US 20160340658A1 · Lessl et al. · 2016 [cited by applicant]
US 20170135353A1 · Thompson et al. · 2017 [cited by applicant]
US 20170283472A1 · Curtis et al. · 2017 [cited by applicant]
US 20170290339A1 · Curtis et al. · 2017 [cited by applicant]
US 20170295797A1 · Curtis et al. · 2017 [cited by applicant]
US 20170295798A1 · Curtis et al. · 2017 [cited by applicant]
US 20170318808A1 · Curtis et al. · 2017 [cited by applicant]
US 20170347664A1 · Thompson et al. · 2017 [cited by applicant]
US 20170356002A1 · Thompson et al. · 2017 [cited by applicant]
US 20180250377A1 · Stewart et al. · 2018 [cited by applicant]
US 20190116801A1 · Thompson et al. · 2019 [cited by applicant]
US 20200029573A1 · Riggs · 2020 [cited by applicant]
US 20200216828A1 · Thompson et al. · 2020 [cited by applicant]
US 20220055961A1 · Thompson et al. · 2022 [cited by applicant]
US 20220135492A1 · Thompson et al. · 2022 [cited by applicant]
US 20230069595A1 · Curtis et al. · 2023 [cited by applicant]
US 20230134066A1 · Thompson et al. · 2023 [cited by applicant]
US 20230322642A1 · Thompson et al. · 2023 [cited by applicant]
US 20240109819A1 · Thompson et al. · 2024 [cited by applicant]
US 20240132417A1 · Thompson et al. · 2024 [cited by applicant]
US 20240132418A1 · Thompson et al. · 2024 [cited by applicant]
US 20240132419A1 · Thompson et al. · 2024 [cited by applicant]
US 20240206466A1 · Thompson et al. · 2024 [cited by applicant]
CA 2146822A1 · 1995 [cited by applicant]
CN 101056536 · 2007 [cited by applicant]
CN 100347180C · 2007 [cited by applicant]
CN 101723763A · 2010 [cited by examiner]
CN 101919407A · 2010 [cited by applicant]
CN 102031231A · 2011 [cited by applicant]
CN 101481666 · 2011 [cited by applicant]
CN 103086784A · 2013 [cited by applicant]
CN 103443278A · 2013 [cited by applicant]
CN 104945164 · 2015 [cited by applicant]
EP 1359134 · 2003 [cited by applicant]
EP 0792363B1 · 2003 [cited by applicant]
EP 1465980B1 · 2010 [cited by applicant]
EP 1590466B1 · 2010 [cited by applicant]
EP 2069504B1 · 2015 [cited by applicant]
IN 801CHE2011 · 2014 [cited by applicant]
JP H10203917A · 1998 [cited by applicant]
JP 2005298409A · 2005 [cited by applicant]
JP 2007117066A · 2007 [cited by applicant]
JP 2000253870A · 2020 [cited by applicant]
KR 20030015943 · 2003 [cited by applicant]
KR 1020110102787A · 2011 [cited by applicant]
RU 2160778C1 · 2000 [cited by applicant]
RU 2313941C2 · 2008 [cited by applicant]
RU 2439148C1 · 2012 [cited by applicant]
RU 2458132C2 · 2012 [cited by applicant]
WO 9623063A1 · 1999 [cited by applicant]
WO 0200232A2 · 2002 [cited by applicant]
WO 0245513A2 · 2002 [cited by applicant]
WO 0246388A1 · 2002 [cited by applicant]
WO 03011487A1 · 2003 [cited by applicant]
WO 03066846A1 · 2003 [cited by applicant]
WO 2005028654A1 · 2005 [cited by applicant]
WO 2006012366A2 · 2006 [cited by applicant]
WO 2007078127A1 · 2007 [cited by applicant]
WO 2007086898A2 · 2007 [cited by applicant]
WO 2008017483A2 · 2008 [cited by applicant]
WO 2009037329A2 · 2009 [cited by applicant]
WO 2009056494A2 · 2009 [cited by applicant]
WO 2010046221A1 · 2010 [cited by applicant]
WO 2011106794A1 · 2011 [cited by applicant]
WO 2011121408A1 · 2011 [cited by applicant]
WO 2013090628A1 · 2013 [cited by applicant]
WO 2013110591A1 · 2013 [cited by applicant]
WO 2013116700 · 2013 [cited by applicant]
WO 2013178649A1 · 2013 [cited by applicant]
WO 2013178650A1 · 2013 [cited by applicant]
WO 2013178658A1 · 2013 [cited by applicant]
WO 2014004487A1 · 2014 [cited by applicant]
WO 2014079773A1 · 2014 [cited by applicant]
WO 2014079814A1 · 2014 [cited by applicant]
WO 2015118516A1 · 2015 [cited by applicant]
WO 2016044529 · 2016 [cited by applicant]
WO 2016044548 · 2016 [cited by applicant]
WO 2016044575 · 2016 [cited by applicant]
WO 2016044661 · 2016 [cited by applicant]
Ahemad, M., et al., “Mechanisms and Applications of Plant Growth Promoting Rhizobacteria: Current Perspective,” Journal of King Saud University—Science, 2014, pp. 1-20, vol. 26. [cited by applicant]
Anand, R., et al., “N2-Fixation and Seedling Growth Promotion of Lodgepole Pine by Endophytic Paenibacillus polymyxa,” Microbial Ecology, 2013, pp. 369-374, vol. 66, No. 2. [cited by applicant]
Bae, C., et al., Multiple Classes of Immune Related Ptoteases Associated with the Cell Death Response in Pepper Plants, Plos One, 2013, vol. 8, No. 5, e63533. [cited by applicant]
Bent, E., et al., “Alterations in Plant Growth and in Root Hormone Levels of Lodgepole Pines Inoculated with Rhizobacteria,” Canadian Journal of Microbiology, Sep. 2001, pp. 793-800, vol. 47, No. 9. [cited by applicant]
Berlemont, R., et al., “Phylogenetic Distribution of Potential Cellulases in Bacteria,” Applied and Environmental Microbiology, Mar. 2013, pp. 1545-1554, vol. 79, No. 5. [cited by applicant]
Boydston, J. A., et al., “The ExsY Protein is Required for Complete Formation of the Exosporium of Bacillus anthracis,” Journal of Bacteriology, 2006, pp. 7440-7448, vol. 188, No. 21. [cited by applicant]
Chakraborty, U., et al., “Plant Growth Promotion and Induction of Resistance in Camellia sinensis by Bacillus megaterium,” Journal of Basic Microbiology, 2006, pp. 186-195, vol. 46, No. 3. [cited by applicant]
Chapman, K. D., “Phospholipase Activity During Plant Growth and Development and in Response to Environmental Stress,” Trends in Plant Science, Nov. 1998, pp. 419-426, vol. 3, Issue 11. [cited by applicant]
Choudhary, D. K., et al., “Interactions of [cited by applicant]
Ciabattini, A., et al., “Oral Priming of Mice by Recombinant Spores of Bacillus subtilis,” Vaccine, Oct. 2004, pp. 4139-4143, vol. 22, Nos. 31-32. [cited by applicant]
Corbineau, F. and Côme, D., “Improvement of Germination of Terminalia Ivorensis Seeds,” Forest Genetic Resources Information No. 21, http://www.fao.org/docrep/006/v3030e/V3030E10.htm, 7 pages. [cited by applicant]
Da Mota, F. F., et al., “Auxin Production and Detection of the Gene Coding for the Auxin Efflux Carrier (AEC) Protein in Paenibacillus polymyxa,” Journal of Microbiology, Jun. 2008, pp. 257-264, vol. 46, No. 3. [cited by applicant]
De Freitas, J. R., et al., “Phosphate-solubilizing Rhizobacteria Enhance the Growth and Yield but not Phosphorus Uptake of Canola ( [cited by applicant]
Ding, Y., et al., “Isolation and Identification of Nitrogen-Fixing Bacilli from Plant Rhizospheres in Beijing Region,” Journal of Applied Microbiology, 2005, pp. 1271-1281, vol. 99, No. 5. [cited by applicant]
Dong, Y.-H., et al., “Identification of Quorum-Quenching N-Acyl Homoserine Lactonases from [cited by applicant]
Doronina, N. V., et al., “Emended Description of Paracoccus kondratievae,” International Journal of Systematic and Evolutionary Microbiology, Mar. 2002, pp. 679-682, vol. 52, Part 2. [cited by applicant]
Dourado, M., et al., “Biotechnological and Agronomic Potential of Endophytic Pink-Pigmented Methylotrophic [cited by applicant]
Dowd, P. E., et al., “The Emerging Roles of Phospholipase C in Plant Growth and Development,” Lipid Signaling in Plants, 2010, pp. 23-37, vol. 16. [cited by applicant]
Duc Le H., et al., “Bacterial Spores as Vaccine Vehicles,” Infection and Immunity, May 2003, pp. 2810-2818, vol. 71, No. 5. [cited by applicant]
Duc, Le H., et al., “Immunization Against Anthrax Using Bacillus subtilis Spores Expressing the Anthrax Protective Antigen,” Vaccine, Jan. 2007, pp. 346-355, vol. 25, No. 2. [cited by applicant]
English, M. M., et al., “Overexpression of hns in the Plant Growth-Promoting Bacterium Enterobacter cloacae UW5 Increases Root Colonization,” Journal of Applied Microbiology, 2009, pp. 2180-2190, vol. 108, Issue 6. [cited by applicant]
Erturk, Y., et al., “Effects of Plant Growth Promoting Rhizobacteria (PGPR) on Rooting and Root Growth of Kiwifruit ( [cited by applicant]
Faria, D. C., et al., “Endophytic Bacteria Isolated from Orchid and Their Potential to Promote Plant Growth,” World Journal of Microbiology & Biotechnology, 2013, pp. 217-221, vol. 29, No. 2. [cited by applicant]
Feng, F. et al., “Display of Human Proinsulin on the Bacillus subtilis Spore Surface for Oral Administration,” Current Microbiology, Jul. 2013, pp. 1-8, vol. 67, Issue 1. [cited by applicant]
Forage, R. G., et al., “Glycerol Fermentation in Klebsiella pneumoniae: Functions of the Coenzyme B12-Dependent Glycerol and Diol Dehydratases,” Journal of Bacteriology, Feb. 1982, pp. 413-419, vol. 149, No. 2. [cited by applicant]
Gamalero, E., et al., “Bacterial Modulation of Plant Ethylene Levels,” Plant Physiology, Sep. 2015, pp. 13-22, vol. 169, Issue 1. [cited by applicant]
Glick, B. R., “Modulation of Plant Ethylene Levels by the Bacterial Enzyme ACC Deaminase,” FEMS Microbiology Letters, Oct. 2005, pp. 1-7, vol. 251, Issue 1. [cited by applicant]
Gnanaraj, M., et al. “Isolation and Gene Expression Analysis of Phospholipase C in Response to Abiotic Stresses from [cited by applicant]
Goldberg, L. J., et al., “A Bacterial Spore Demonstrating Rapid Larvicidal Activity Against Anopheles Sergentii, Uranotaenia Unguiculata, Culex Univitattus, Aedes Aegypti and Culex Pipiens,” Mosquito News, Sep. 1977, pp… [cited by applicant]
Guerchicoff, A., et al., “Identification and Characterization of A Previously Undescribed cyt Gene in [cited by applicant]
Gujar, P. D., et al., “Effect of Phytase from Aspergillus niger on Plant Growth and Mineral Assimilation in Wheat ( [cited by applicant]
Hafeez, F. Y., et al., “PGPR: Versatile Tool to Combat Soil Borne Pathogens and Improve Plant Health,” Aspects of Applied Biology, 2011, pp. 241-245, vol. 106. [cited by applicant]
Haggag, W. M., et al., “Colonization of Peanut Roots by Biofilm-Forming Paenibacillus polymyxa Initiates Biocontrol Against Crown Rot Disease,” Journal of Applied Microbiology, 2008, pp. 961-969, vol. 104, No. 4. [cited by applicant]
Han, W. et al., “The Application of Exogenous Cellulase to Improve Soil Fertility and Plant Growth Due to Acceleration of Straw Decomposition,” Bioresource Technology, May 2010, pp. 3724-3731, vol. 101, Issue 10. [cited by applicant]
Hartati, S., et al., “Overexpression of Poplar Cellulase Accelerates Growth and Disturbs The Closing Movements of Leaves in Sengon,” Plant Physiology, 2008, pp. 552-561, vol. 147, Issue 2. [cited by applicant]
Hinton, D. M., et al., “Enterobacter cloacae is an Endophytic Symbiont of Corn”, Mycopathologia, 1995, pp. 117-125, vol. 129, No. 2. [cited by applicant]
Hoelscher, B., et al., “Removal of Toxic Contaminants from Polluted Soil and Water via Enzyme-Linked Bacillus Spores,” Poster presented at Missouri Life Sciences Week Research Poster Session, Apr. 14, 2010. [cited by applicant]
Hong, Y. et al., “Phospholipases in Plant Response to Nitrogen and Phosphorus Availability,” Springer, Phospholipases in Plant Signaling and Communication in Plants, 2013, pp. 159-180, vol. 20. [cited by applicant]
Hontzeas, N., et al., “Changes in Gene Expression in Canola Roots Induced by ACC-Deaminase-Containing Plant-Growth-Promoting Bacteria,” Molecular Plant-Microbe Interactions, Aug. 2004, pp. 865-871, vol. 17, No. 8. [cited by applicant]
Howard, G., et al., “Effects of Cellulolytic Ruminol Bacteria and of Cell Extracts on Germination of [cited by applicant]
Idriss, E. E., et al., “Extraccellular Phytase Activity of Bacillus amyloliquefaciens FZB45 Contributes to its Plant-Growth-Promoting Effect,” Microbiology, 2002, pp. 2097-2109, vol. 148. [cited by applicant]
Iniguez, A. L., et al., “Nitrogen Fixation in Wheat Provided by Klebsiella pneumoniae 342,” Molecular Plant-Microbe Interactions, Oct. 2004, pp. 1078-1085, vol. 17, No. 10. [cited by applicant]
Invitation to Pay Additional Fees and, Where Applicable, Protest Fees, issued for PCT/US2015/050795, dated Jan. 14, 2016, 8 pages. [cited by applicant]
International Search Report and Written Opinion issued for PCT/US2015/050795, dated Mar. 31, 2016, 17 pages. [cited by applicant]
International Search Report and Written Opinion issued for PCT/US2015/050807, dated Dec. 10, 2015, 12 pages. [cited by applicant]
Islam, M. R., et al., “Characterization of Plant Growth-Promoting Traits of Free-Living Diazotrophic Bacteria and Their Inoculation Effects on Growth and Nitrogen Uptake of Crop Plants,” Journal of Microbiology and Biot… [cited by applicant]
Isticato, R., et al., “Surface Display of Recombinant Proteins on Bacillus subtilis Spores,” Journal of Bacteriology, Nov. 2001, pp. 6294-6301, vol. 183, No. 21. [cited by applicant]
Iwanicki, A., et al., “A System of Vectors for Bacillus subtilis Spore Surface Display,” Microbial Cell Factories, 2014, pp. 1-9, vol. 13, No. 30. [cited by applicant]
Jackson, W. T., “Effect of Pectinase and Cellulase Preparations on the Growth and Development of Root Hairs,” Physiologia Plantarum, 2006 (first published in 1959), pp. 502-510, vol. 12. [cited by applicant]
Jeong, H., et al., “Draft Genome Sequence of the Paenibacillus polymyxa Type Strain (Atcc 842T), A Plant Growth-Promoting Bacterium,” Journal of Bacteriology, 2011, pp. 5026-5027, vol. 193, No. 18. [cited by applicant]
Singh et al., Protein Engineering Approaches in the Post-Genomic Era, Current Protein and Peptide Science 18:1-11, 2017. [cited by applicant]
Zhang et al., Propagated Perturbations from a Peripheral Mutation Show Interaction Supporting WW Domain Thermostability, Structure 26:1474-1485, 2018. [cited by applicant]
Aakre, et al. Inhibition of Bacillus cereus phospholipase C by univalent anions. The Biochemical Journal 203, 799-801, (1982). [cited by applicant]
Goldfine, et al. “Nonspecific phospholipase C of Listeria monocytogenes: activity on phospholipids in Triton X-100-mixed micelles and in biological membranes”. J Bacteriol 175, 4298-4306, (1993). [cited by applicant]
Huang, et al. “Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH”. Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics 1864(6), 697-705, (2016). [cited by applicant]
Monturiol-Gross, et al. “Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase”. FEBS Open Bio, vol. 11(12), pp. 3262-3275, (2021). [cited by applicant]
Otnaess. “The hydrolysis of sphingomyelin by phospholipase C from Bacillus cereus”. FEBS Letters 114, 202-204, (1980). [cited by applicant]
Pomerantsev, et al. “Phosphatidylcholine-specific phospholipase C and sphingomyelinase activities in bacteria of the Bacillus cereus group”. Infect Immun. (2003); 71(11): 6591-606. [cited by applicant]
Tan, et al. “Cloning, overexpression, refolding, and purification of the nonspecific phospholipase C from Bacillus cereus”. Protein Expr Purif 10, 365-372, (1997). [cited by applicant]
Zuckert, et al. “Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog”. Infect I… [cited by applicant]
Canadian Office Action regarding Canadian App. No. 2,961,641 dated Oct. 10, 2023. [cited by applicant]
Saile et al., Bacillus anthracis multiplication, persistence, and genetic exchange in the rhizosphere of grass plants, Appl. Environ. Microbiol., 72(5):3168-3174, 2006. [cited by applicant]
Inaoka, T., et al., “SodA and Manganese Are Essential for Resistance to Oxidative Stress in Growing and Sporulating Cells of [cited by applicant]
Wang, Y., et al., “Two distinct manganese-containing superoxide dismutase genes in [cited by applicant]
Wang, W., et al., “Comparative Proteomic Analysis of Rice Seedlings in Response to Inoculation with Bacillus cereus,” Letters in Applied Microbiology, 2012, pp. 208-215, vol. 56, Issue 3. [cited by applicant]
Fan, L., et al., “Antisense Suppression of Phospholipase D(alpha) Retards Abscisic Acid- and Ethylene-Promoted Senescence of Postharvest [cited by applicant]
Glass, M., et al., “Endo-(beta)-1,4-Glucanases Impact Plant Cell Wall Development by Influencing Cellulose Crystallization,” Journal of Integrative Plant Biology, Apr. 2015, pp. 396-410, vol. 57, Issue 4. [cited by applicant]
Hong, Y., et al., “Phospholipase D(alpha)3 Is Involved in the Hyperormotic Response in [cited by applicant]
Li, M., et al., Overexpression of Patatin-Related Phospholipase Alll(delta) Altered Plant Growth and Increased Seed Oil Content in Camelina, Plant Biotechnology Journal, 2015, pp. 766-778, vol. 13. [cited by applicant]
Shani, Z., et al., “Growth Enhancement of Transgenic Poplar Plants by Overexpression of [cited by applicant]
Zhuang, X., et al., “New Advances in Plant Growth-Promoting Rhizobacteria for Bioremediation,” Environmental International, 2007, pp. 406-413, vol. 33. [cited by applicant]
Nissinen, R., et al., “ [cited by applicant]
Priest, F. G., et al., “Population Structure and Evolution of the Bacillus cereus Group,” Journal of Bacteriology, Dec. 2004, pp. 7959-7970, vol. 186, No. 23. [cited by applicant]
Mikayama, T., et al., “Molecular Cloning and Functional Expression of a cDNA Encoding Glycosylation-Inhibiting Factor,” Proceeding of the National Academy of Science of the United States of America, Nov. 1993, pp. 10056… [cited by applicant]
Rudinger, J., “Characteristics of the Amino Acids as Components of a Peptide Hormone Sequence,” Peptide Hormones, Biology Council, Jun. 1976, pp. 5-7. [cited by applicant]
UniProtKB Accession No. P23903.1, Glucan endo-1,3-beta-glucosidase A1, 1991, 2 pages. [cited by applicant]
UniProtKB Accession No. O52864, Phosphatidyl-degrading Phospholipase C, 1998, 1 page. [cited by applicant]
Sadowski, M. I., et al., “The Sequence-Structure Relationship and Protein Function Prediction,” Current Opinion in Structural Biology, 2009, pp. 357-362, vol. 19, No. 3. [cited by applicant]
Seffernick, J. L., et al., “Melamine Deaminase and Atrazine Chlorohydrolase: 98 Percent Identical but Functionally Different,” Journal of Bacteriology, Apr. 2001, pp. 2405-2410, vol. 183, No. 8. [cited by applicant]
Sloma, A., et al., “Cloning and Characterization of the Gene for an Additional Extracellular Serine Protease of Bacillus subtilis,” Journal of Bacteriology, Nov. 1991, pp. 6889-6895, vol. 173, No. 21. [cited by applicant]
Sousa, S., et al., “The ARO4 Gene of Candida albicans Encodes A Tyrosine-Sensitive DAHP Synthase: Evolution, Functional Conservation and Phenotype of Aro3p-, Aro4p-Deficient Mutants,” Microbiology, 2002, pp. 1291-1303, … [cited by applicant]
Tang, S., et al., “Identification of Dehalobacter Reductive Dehalogenases that Catalyse Dechlorination of Chloroform, 1, 1, 1-Trichloroethane and 1, 1-Dichloroethane,” Philosophical Transactions of The Royal Society, 20… [cited by applicant]
Thallinger, B., et al., “Antimicrobial Enzymes: An Emerging Strategy to Fight Microbes and Microbial Biofilms,” Biotechnology Journal, 2013, pp. 97-109, vol. 8, No. 1. [cited by applicant]
Valbuzzi, A., et al., “A Novel Member of the Subtilisin-like Protease Family from Bacillus subtilis,” Microbiology, 1999, pp. 3121-3127, vol. 145, Part 11. [cited by applicant]
Peng, Q., et al., “The Regulation of Exosporium-Related Genes in Bacillus thuringiensis,” Scientific Reports, 2016, pp. 1-12, vol. 6, No. 19005. [cited by applicant]
Tian, W., et al., “How Well is Enzyme Function Conserved as a Function of Pairwise Sequence Identity?,” Journal of Molecular Biology, 2003, pp. 863-882, vol. 333, No. 4. [cited by applicant]
Dunne, C., et al., “Overproduction of an Inducible Extracellular Serine Protease Improves Biological Control of Pythium ultimum by Stenotrophomonas maltophilia Strain W81,” Microbiology, 2000, pp. 2069-2078, vol. 146, P… [cited by applicant]
Khan, N., et al., “Antifungal Activity of [cited by applicant]
Van Pouderoyen, G., et al., “Structural Insights Into the Processivity of Endopolygalacturonase I from Aspergillus niger,” FEBS Letters, 2003, pp. 462-466, vol. 554, No. 3. [cited by applicant]
Yen, Y.-H., et al., “An Antifungal Protease Produced by Pseudomonas aeruginosa M-1001 with Shrimp and Crab Shell Powder as a Carbon Source,” Enzyme and Microbial Technology, 2006, pp. 311-317, vol. 39. [cited by applicant]
Hachisuka, Y., et al., “Exosporia and Appendages of Spores of [cited by applicant]
Benfield, et al., “Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Proteins Variants” (2007) vol. 460, No. 1, pp. 41-47. [cited by applicant]
Cheng, “Purification and Characterization of a Thermostable β-Mannanase from Bacillus Subtilis BE-91: Potential Application in Inflammatory Diseases” BioMed Research International (2016) vol. 2016, Article ID 6380147, p… [cited by applicant]
Emi, et al., “Crystallization and Some Properties of Mannanase” Agricultural and Biological Chemistry (1972) vol. 36, No. 6, pp. 991-1001. [cited by applicant]
Haldenwang , W.G., “The Sigma Factors of Bacillus Subtilis” Microbiological Reviews, vol. 59, No. 1 (Mar. 1995), pp. 1-30. [cited by applicant]
Jetiyanon, K., et al., “Film Coating of Seeds with Bacillus Cereus RS87 Spores for Early Plant Growth Enhancement”, Canadian Journal of Microbiology (2008) vol. 54, pp. 861-867. [cited by applicant]
Li, et al., “Structure Prediction and Enzymatic Properties of Phytase PhyS”, Advances in Enzyme Research (2019) vol. 7, pp. 57-65. [cited by applicant]
Bailey-Smith, K., et al. “The ExsA Protein of Bacillus Cereus is Required for Assembly of Coat and Exosporium onto the Spore Surface”, Journal of Bacteriology, Jun. 2005, vol. 187, No. 11, pp. 3800-3806. [cited by applicant]
Shah, S., et al., “Isolation and Characterization of ACC Deaminase Genes From Two Different Plant Growth-Promoting Rhizobacteria” Canadian Journal of Microbiology (1998) vol. 44, pp. 833-843. [cited by applicant]
Quan, et al., “Purification and Properties of a Phytase from Candida Krusei WZ-001”, Journal of Bioscience (2002) vol. 94, No. 5, pp. 419-425. [cited by applicant]
Henriques and Moran, Structure, assembly, and function of the spore surface layers, Annu. Rev. Microbiol. 61:555-88, 2007. [cited by applicant]
Bewley, Breaking down the walls—a role for endo-beta-mannanase in release from seed dormancy?, Trends in Plant Science 2(12):464-469, 1997. [cited by applicant]
Yang, et al., A novel beta-mannanase with high specific activity from Bacillus circulans CGMCC1554: gene cloning, expression and enzymatic characterization, Applied Biochemistry and Biotechnology 159(11):85-94, 2008. [cited by applicant]
Nguyen et al., Bacillus subtilis spores expressing the VP28 antigen: a potential oral treatment to protect Litopenaeus vannamei against white spot syndrome, FEMS Microbiology Letters 358(2): 202-208, 2014. [cited by applicant]
Crane et al., Bacterial Nitric Oxide Synthases, Annual Review in Biochemistry 79:445-470, 2010. [cited by applicant]
Leviatov et al., Involvement of Endomannanase in the Control of Seed Germination under Low Temperature Conditions, Annals of Botany, 1(76): 1-6, 1995. [cited by applicant]
Barbe et al., From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later, Microbiology 155(6):1758-1775, 2009. [cited by applicant]
Bressuire-Isoard et al., Sporulation temperature reveals a requirement for CotE in the assembly of both the coat and the exosporium layers of Bacillus cereus spores, Applied and Environmental Microbiology 82(1):232-243,… [cited by applicant]
GenBank Accession No. NP_389608, dated Feb. 12, 2021. [cited by applicant]
Geng et al., A novel serine protease, Sep1, from Bacillus firmus DS-1 has nematicidal activity and degrades multiple intestinal-associated nematode proteins, Scientific Reports 6(1): 2016. [cited by applicant]
UniProt Accession No. W7KRH1, dated Apr. 16, 2014. [cited by applicant]
UniProt Accession No. A0A380XNG8, dated Nov. 7, 2018. [cited by applicant]
Takekawa, et al. “Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa”, Journal of Bacteriology 173 (21), 6820-6825, (1991). [cited by applicant]
GenBank Accession No. P33378, dated Feb. 22, 2023. [cited by applicant]
U.S. Appl. No. 17/932,994, filed Sep. 16, 2022, Thompson et al. [cited by applicant]
U.S. Appl. No. 17/852,607, filed Jun. 29, 2022, Curtis et al. [cited by applicant]
U.S. Appl. No. 17/459,019, filed Aug. 27, 2021, Thompson et al. [cited by applicant]
U.S. Appl. No. 17/459,031, filed Aug. 27, 2021, Thompson et al. [cited by applicant]
U.S. Appl. No. 18/302,458, filed Apr. 18, 2023, Thompson et al. [cited by applicant]
U.S. Appl. No. 18/461,008, filed Sep. 5, 2023, Curtis et al. [cited by applicant]
U.S. Appl. No. 18/476,256, filed Sep. 27, 2023, Thompson et al. [cited by applicant]
U.S. Appl. No. 18/476,259, filed Sep. 23, 2023, Thompson et al. [cited by applicant]
U.S. Appl. No. 18/476,264, filed Sep. 27, 2023, Thompson et al. [cited by applicant]
U.S. Appl. No. 18/476,270, filed Sep. 27, 2023, Thompson et al. [cited by applicant]
Johnson M. J., et al., “ExsY and CotY are Required for the Correct Assembly of the Exosporium and Spore Coat of Bacillus cereus,” Journal of Bacteriology, 2006, pp. 7905-7913, vol. 188, No. 22. [cited by applicant]
Karakurt, H., et al., “Effects of indol-3-butyric acid (IBA), Plant Growth Promoting Rhizobacteria (PGPR) and Carbohydrates on Rooting of Hardwood Cutting of MM106 Apple Rootstock,” African Journal of Agricultural Resea… [cited by applicant]
Karigar, C., et al., “ Role of Microbial Enzymes in the Bioremediation of Pollutants: A Review,” SAGE—Hindawi Access to Research Enzyme Research, vol. 2011, Article ID 805187, 11 pages. [cited by applicant]
Khan, Z., et al., “A Plant Growth Promoting Rhizobacterium, Paenibacillus polymyxa Strain GBR-1, Suppresses Root-Knot Nematode,” Bioresource Technology, May 2008, pp. 3016-3023, vol. 99, No. 8. [cited by applicant]
Kim, J. F., et al., “Genome Sequence of the Polymyxin-Producing Plant-Probiotic Rhizobacterium Paenibacillus polymyxa E681,” Journal of Bacteriology, 2010, pp. 6103-6104, vol. 192, No. 22. [cited by applicant]
Kim, J. H., et al., “Bacterial Surface Display of GFP(uv) on Bacillus subtilis Spores,” Journal of Microbiology and Biotechnology, Apr. 2007, pp. 677-680, vol. 17, No. 4. [cited by applicant]
Kim, J. H., et al., “Spore-Displayed Streptavidin: A Live Diagnostic Tool in Biotechnology,” Biochemical and Biophysical Research Communications, May 2005, pp. 210-214, vol. 331, No. 1. [cited by applicant]
Kishore, G. K., et al., “Phylloplane Bacteria Increase Seedling Emergence, Growth and Yield of Field-Grown Groundnut ( [cited by applicant]
Kong, Z., et al., “Effects of 1-Aminocyclopropane-1-Carboxylate (ACC) Deaminase-Overproducing Sinorhizobium meliloti on Plant Growth and Copper Tolerance of Medicago lupulina,” Plant and Soil, Jun. 2015, pp. 383-398, vo… [cited by applicant]
Lamsal, K., et al., “Application of Rhizobacteria for Plant Growth Promotion Effect and Biocontrol of Anthracnose Caused by Colletotrichum acutatum on Pepper,” Mycobiology, Dec. 2012, pp. 244-251, vol. 40, No. 4. [cited by applicant]
Lee, S., et al., “Growth Promotion of Xanthium italicum by Application of Rhizobacterial Isolates of Bacillus aryabhattai in Microcosm Soil,” Journal of Microbiology, Feb. 2012, pp. 45-49, vol. 50, No. 1. [cited by applicant]
Leite, H. A., et al., “Bacillus subtilis and Enterobacter cloacae Endophytes from Healthy [cited by applicant]
Leski, T. A., et al., “Identification and Classification of bcl Genes and Proteins of Bacillus cereus Group Organisms and Their Application in Bacillus anthracis Detection and Fingerprinting,” Applied and Environmental … [cited by applicant]
Leveau, J. H. J., et al., “Utilization of the Plant Hormone Indole-3-Acetic Acid for Growth by Pseydomonas putida Strain 1290,” Applied and Environmental Microbiology, May 2005, pp. 2365-2371, vol. 71, No. 5. [cited by applicant]
Li, J., et al., “An ACC Deaminase Minus Mutant of Enterobacter cloacae UW4 No Longer Promotes Root Elongation,” Current Microbiology, Aug. 2000, pp. 101-105, vol. 41, No. 2. [cited by applicant]
Li, W., et al., “Cloning of the Thermostable Cellulose Gene from the Newly Isolated Bacillus subtillus and its Expression in [cited by applicant]
Liu, J. L., et al., “Effects of Two Plant Growth-Promoting Rhizobacteria Containing 1-Aminocyclopropane-1-Carboxylate Deaminase on Oat Growth in Petroleum Contaminated Soil,” International Journal of Environmental Scien… [cited by applicant]
Liu, X., et al., “Colonization of Maize and Rice Plants by Strain Bacillus megaterium C4,” Current Microbiology, 2006, pp. 186-190, vol. 52, No. 3. [cited by applicant]
Liu, Y., et al., “Study on Mechanisms of Colonization of Nitrogen-Fixing PGPB, Klebsiella pneumoniae NG14 on the Root Surface of Rice and the Formation of Biofilm,” Current Microbiology, 2011, pp. 1113-1122, vol. 62, No… [cited by applicant]
Lopez-Bucio, J., et al., “Bacillus megaterium Rhizobacteria Promote Growth and Alter Root-System Architecture Through an Auxin- and Ethylene-Independent Signaling Mechanism in [cited by applicant]
Luiz, W. B., et al., “Boosting Systemic and Secreted Antibody Responses in Mice Orally Immunized with Recombinant Bacillus subtilis Strains Following Parenteral Priming with a DNA Vaccine Encoding the Enterotoxigenic [cited by applicant]
Madmony, A., et al., “Enterobacter cloacae, An Obligatory Endophyte of Pollen Grains of Mediterranean Pines,” Folia Microbiologica (Praha), 2005, pp. 209-216, vol. 50, No. 3. [cited by applicant]
Maes, M., et al., “Experiences and Perspectives for the Use of A Paenibacillus Strain as a Plant Protectant,” Communications in Agricultural and Applied Biological Sciences, 2003, pp. 457-462, vol. 68, No. 4, Part B. [cited by applicant]
Marulanda, A., et al., “Regulation of Plasma Membrane Aquaporins by Inoculation with a Bacillus megaterium Strain in Maize ( [cited by applicant]
Mauriello, E. M., et al., “Display of Heterologous Antigens on the Bacillus subtilis Spore Coat Using CotC as a Fusion Partner,” Vaccine, Mar. 2004, pp. 1177-1187, vol. 22, Nos. 9-10. [cited by applicant]
Medie, F. M., “Genome Analyses Highlight the Different Biological Roles of Cellulases,” Nature Reviews Microbiology, Mar. 2012, pp. 227-234, vol. 10. [cited by applicant]
Meldau, D. G., et al., “A Native Plant Growth Promoting Bacterium, [cited by applicant]
Mercado, J. A., et al., “Expression of the beta-1,3-glucanase Gene bgn13.1 from Trichoderma harzianum in Strawberry Increases Tolerance to Crown Rot Diseases but Interferes with Plant Growth,” Transgenic Research, Dec. … [cited by applicant]
Negri, A., et al., “Expression and Display of Clostridium difficile Protein FliD on the Surface of Bacillus subtilis Spores,” Journal of Medical Microbiology, 2013, pp. 1379-1385, vol. 62. [cited by applicant]
Ngamau, C., “Endophytic Bacteria Associated with Bananas ( [cited by applicant]
Oh, T., et al., “Expression of Aspergillus nidulans phy Gene in Nicotiana benthamiana Produces Active Phytase with Broad Specificities,” International Journal of Molecular Sciences, 2014, pp. 15571-15591, vol. 15, No. 9. [cited by applicant]
Ortiz-Castro, R., et al., “Plant Growth Promotion by Bacillus megaterium Involves Cytokinin Signaling,” Plant Signaling & Behavior, 2008, pp. 263-265, vol. 3, Issue 4. [cited by applicant]
Paccez, J. D., et al., “Evaluation of Different Promoter Sequences and Antigen Sorting Signals on the Immunogenicity of Bacillus subtilis Vaccine Vehicles,” Vaccine, 2007, pp. 4671-4680, vol. 25, No. 24. [cited by applicant]
Paccez, J. D., et al., “Stable Episomal Expression System Under Control of a Stress Inducible Promoter Enhances the Immunogenicity of Bacillus subtilis as a Vector for Antigen Delivery,” Vaccine, 2006, pp. 2935-2943, vo… [cited by applicant]
Park, T. J., et al., “Spore Display Using Bacillus thuringiensis Exosporium Protein InhA,” Journal of Microbiology and Biotechnology, May 2009, pp. 495-501, vol. 19, No. 5. [cited by applicant]
Park, T. J., “Surface-Display of Recombinant Proteins on Bacterial Exosporium and its Biotechnological Applications,” Doctoral Thesis presented to the Department of Chemical and Biomolecular Engineering, Korea Advanced … [cited by applicant]
Peixoto, R. S., et al., “Petroleum-Degrading Enzymes: Bioremediation and New Prospects,” SAGE-Hindawi Access to Research Enzyme Research, vol. 2011, Article ID 475193, 7 pages. [cited by applicant]
Penrose, D. M., et al., “Levels of ACC and Related Compounds in Exudate and Extracts of Canola Seeds Treated with ACC Deaminase-Containing Plant Growth-Promoting Bacteria,” Canadian Journal of Microbiology, Apr. 2001, p… [cited by applicant]
Pereira, C. E., et al., “Compatibility Among Fungicide Treatments on Soybean Seeds Through Film Coating and Inoculation with Bradyrhizobium Strains,” Acta Scientiarum. Agronomy, Maringá, 2010, pp. 585-589, vol. 32, No. … [cited by applicant]
Petrov, K., et al., “High Production of 2,3-Butanediol from Glycerol by Klebsiella pneumoniae G31,” Applied Microbiology and Biotechnology, 2009, pp. 659-665, vol. 84, No. 4. [cited by applicant]
Phi, Q. T., et al., “Assessment of Root-Associated Paenibacillus polymyxa Groups on Growth Promotion and Induced Systemic Resistance in Pepper,” Journal of Microbiology and Biotechnology, Dec. 2010, pp. 1605-1613, vol. … [cited by applicant]
Phitsuwan, P., et al., “Present and Potential Applications of Cellulases in Agriculture, Biotechnology, and Bioenergy,” Folia Microbiologica, 2013, pp. 163-176, vol. 58, No. 2. [cited by applicant]
Pilar-Izquierdo, M. C., et al., “Barley Seed Coating with Free and Immobilized Alkaline Phosphatase to Improve P Uptake and Plant Growth,” Journal of Agricultural Science, 2012, pp. 691-701, vol. 150, Issue 6. [cited by applicant]
Ping, R., et al., Abstract, Journal of Northwest Forestry College, 2005, pp. 78-79, vol. 20, No. 1. [cited by applicant]
Prusty, R., et al., “The Plant Hormone Indoleacetic Acid Induces Invasive Growth in [cited by applicant]
Raddadi, N., et al., “Screening of Plant Growth Promoting Traits of Bacillus thuringiensis,” Annals of Microbiology, 2008, pp. 47-52, vol. 58, No. 1. [cited by applicant]
Rasco, D. A., et al., UniProt KB database entry Q738B1-Q7381_BACC1, Jul. 5, 2004, 6 pages (referencing Rasco, D. A., et al., “The Genome Sequence of Bacillus cereus ATCC 10987 Reveals Metabolic Adaptations and a Large P… [cited by applicant]
Rajendran, G., et al., “Enhanced Growth and Nodulation of Pigeon Pea by Co-Inoculation of Bacillus Strains with [cited by applicant]
Rajkumar, M., et al., “Effects of Inoculation of Plant-Growth Promoting Bacteria on Ni Uptake by Indian Mustard,” Bioresource Technology, 2008, pp. 3491-3498, vol. 99, No. 9. [cited by applicant]
Rao, M. A., et al., “Role of Enzymes in the Remediation of Polluted Environments,” Journal of Soil Science and Plant Nutrition, 2010, 21 pages, vol. 10, No. 3. [cited by applicant]
Reetha, S., et al., “Screening of Cellulase and Pectinase by Using Pseudomonas Fluorescens and Bacillus subtilis,” International Letters of Natural Sciences, 2014, pp. 75-80, vol. 8, No. 2. [cited by applicant]
Ryu, C. M., et al., “Bacterial Volatiles Promote Growth in [cited by applicant]
Sachdev, D. P., et al., “Isolation and Characterization of Indole Acetic Acid (IAA) Producing Klebsiella pneumoniae Strains from Rhizosphere of Wheat ( [cited by applicant]
Saleh, S., et al., “Involvement of gacS and rpoS in Enhancement of the Plant Growth-Promoting Capabilities of Enterobacter cloacae CAL2 and UW4,” Canadian Journal of Microbiology, Aug. 2001, pp. 698-705, vol. 47, No. 8. [cited by applicant]
Sales, J., et al. “Coffee ( [cited by applicant]
Selvakumar, G., et al., “Isolation and Characterization of Nonrhizobial Plant Growth Promoting Bacteria from Nodules of Kudzu ( [cited by applicant]
Sequence Listing filed in WO 2007/078127 A1 published Jul. 12, 2007, downloaded from <http://patentscope.wipo.int/search/en/detail.jsf?docld=WO2007078127&recNum=1&tab=PCTDocuments&maxRec=&office=&prevFilter=&sortOption=… [cited by applicant]
Shahid, M., et al., “Root Colonization and Growth Promotion of Sunflower ( [cited by applicant]
Shani, Z., et al., “Expression of Endo-1,4-beta-glucanase (cel1) in [cited by applicant]
Shankar, M., et al., “Root Colonization of a Rice Growth Promoting Strain of Enterobacter cloacae,” Journal of Basic Microbiology, 2011, pp. 523-530, vol. 51, No. 5. [cited by applicant]
Shao, J., et al., “Contribution of Indole-3-Acetic Acid in the Plant Growth Promotion by the Rhizospheric Strain Bacillus amyloliquefaciens SQR9,” Biology and Fertility of Soils, 2015, pp. 321-330, vol. 51, Issue 3. [cited by applicant]
Shen, M., et al., “Effect of Plant Growth-Promoting Rhizobacteria (PGPRs) on Plant Growth, Yield, and Quality of Tomato ( [cited by applicant]
Siddikee, Md. A., et al., “Halotolerant Bacteria with ACC Deaminase Activity Alleviate Salt Stress Effect in Canola Seed Germination,” Journal of the Korean Society for Applied Biological Chemistry, 2015, pp. 237-241, v… [cited by applicant]
Singh, B., et al., “Microbial Phytases in Phosphorous Acquisition and Plant Growth Promotion,” Physiology and Molecular Biology of Plants, 2011, pp. 93-103, vol. 17, Issue 2. [cited by applicant]
Singh, B., et al., “Plant Growth Promotion by an Extracellular HAP-Phytase of a Thermophilic Mold Sporotrichum thermophile,” Applied Biochemistry and Biotechnology, 2010, pp. 1267-1276, vol. 160, Issue 5. [cited by applicant]
Smirnova, I., et al., “The Effect of Inoculation by Cellulolytic Bacteria Bacillus cytaseus on Wheat Productivity,” Institute of Microbiology and Virology Ministry of Education and Science, Kazakhstan, Almaty, pp. 185-1… [cited by applicant]
Stearns, J. C., et al., “Effects of Bacterial ACC Deaminase on Brassica napus Gene Expression,” Molecular Plant-Microbe Interactions, May 2012, pp. 668-676, vol. 25, No. 5. [cited by applicant]
Steichen, C. T., et al., “Non-Uniform Assembly of the Bacillus anthracis Exosporium and a Bottle Cap Model for Spore Germination and Outgrowth,” Molecular Microbiology, Apr. 2007, pp. 359-367, vol. 64, Issue 2. [cited by applicant]
Tan, L., et al., “An Unusual Mechanism of Isopeptide Bond Formation Attaches the Collagenlike Glycoprotein BclA to the Exosporium of Bacillus anthracis,” mBio, May-Jun. 2011, 20 pages, vol. 2, No. 3. [cited by applicant]
Tan, L., et al., “An Unusual Mechanism of Isopeptide Bond Formation Attaches the Collagenlike Glycoprotein BclA to the Exosporium of Bacillus anthracis,” mBio, May-Jun. 2011, 20 pages, vol. 2, No. 3 (Retraction). [cited by applicant]
Tan, L., et al., “Sequence Motifs and Proteolytic Cleavage of the Collagen-Like Glycoprotein BclA Required for Its Attachment to the Exosporium of Bacillus anthracis,” Journal of Bacteriology, Mar. 2010, pp. 1259-1268, … [cited by applicant]
Thomas, P., et al., “Endophytic Bacteria Associated with Growing Shoot Tips of Banana ( [cited by applicant]
Thompson, B. M., “The Role of the Glycoprotein BclB in the Exosporium in the Exosporium of Bacillus Anthracis,” Doctoral Dissertation presented to the Department of Diagnostic Medicine/Pathobiology, College of Veterinar… [cited by applicant]
Thompson, B. M. et al., “A System of Efficient, Cost-Effective, and Customizable Vaccines for Use with Multiple Vaccine Candidates,” Oct. 2010 poster presentation, 1 page. [cited by applicant]
Thompson, B. M., et al., “Assembly of the BclB Glycoprotein into the Exosporium and Evidence for its Role in the Formation of the Exosporium ‘cap’ Structure in Bacillus anthracis,” Molecular Microbiology, Dec. 2012, pp.… [cited by applicant]
Thompson, B. M., et al., “Localization and Assembly of the Novel Exosporium Protein BetA of Bacillus anthracis,” Journal of Bacteriology, 2011, pp. 5098-5104, vol. 193, No. 19. [cited by applicant]
Thompson, B. M., et al., “Targeting of the BclA and BclB Proteins to the Bacillus anthracis Spore Surface,” Molecular Microbiology, 2008, pp. 421-434, vol. 70, No. 2. [cited by applicant]
Thompson, B. M., et al., “The BclB Glycoprotein of Bacillus anthracis is Involved in Exosporium Integrity,” Journal of Bacteriology, 2007, pp. 6704-6713, vol. 189, No. 18. [cited by applicant]
Thompson, B. M., et al., “The Co-Dependence of BxpB/ExsFA and BclA for Proper Incorporation into the Exosporium of Bacillus anthracis,” Molecular Microbiology, 2011, pp. 799-813, vol. 79, No. 3. [cited by applicant]
Thompson, B. M., “Amino-Terminal Sequences of the Bacillus anthracis Exosporium Proteins BclA and BclB Important for Localization and Attachment to the Spore Surface,” A Thesis presented to the Faculty of the Graduate S… [cited by applicant]
Timmusk, S., et al., “The Plant-Growth-Promoting Rhizobacterium Paenibacillus polymyxa Induces Changes in [cited by applicant]
Timmusk, S., et al., “Paenibacillus polymyxa Invades Plant Roots and Forms Biofilms,” Applied and Environmental Microbiology, Nov. 2005, pp. 7292-7300, vol. 71, No. 11. [cited by applicant]
Trivedi, P., et al., “Plant Growth Promotion Abilities and Formulation of Bacillus megaterium Strain B 388 (MTCC6521) Isolated from a Temperate Himalayan Location,” Indian Journal of Microbiology, 2008, pp. 342-347, vol… [cited by applicant]
Vendan, R. T., et al., “Diversity of Endophytic Bacteria in Ginseng and Their Potential for Plant Growth Promotion,” Journal of Microbiology, 2010, pp. 559-565, vol. 48, No. 5. [cited by applicant]
Von Der Weid, I., et al., “Diversity of Paenibacillus polymyxa Strains Isolated from the Rhizosphere of Maize Planted in Cerrado Soil,” Research in Microbiology, Jun. 2000, pp. 369-381, vol. 151, No. 5. [cited by applicant]
Walker, R., et al., “Colonization of the Developing Rhizosphere of Sugar Beet Seedlings by Potential Biocontrol Agents Applied as Seed Treatments,” Journal of Applied Microbiology, 2002, pp. 228-237, vol. 92, No. 2. [cited by applicant]
Waller, L. N., et al., “Identification of a Second Collagen-Like Glycoprotein Produced by Bacillus anthracis and Demonstration of Associated Spore-Specific Sugars,” Journal of Bacteriology, Jul. 2005, pp. 4592-4597, vol… [cited by applicant]
Wang, X., et al., “PLD: Phospholipase Ds in Plant Signaling,” Springer, Phospholipases in Plant Signaling, Signaling and Communication in Plants 20, Springer-Verlag Berlin Heidelberg 2014. [cited by applicant]
Yadav, S., et al., “Diversity and Phylogeny of Plant Growth-Promoting Bacilli from Moderately Acidic Soil,” Journal of Basic Microbiology, Feb. 2011, pp. 98-106, vol. 51, No. 1. [cited by applicant]
Yegorenkova, I. V., et al., “Paenibacillus polymyxa Rhizobacteria and Their Synthesized Exoglycans in Interaction With Wheat Roots: Colonization and Root Hair Deformation,” Current Microbiology, 2013, pp. 481-486, vol. … [cited by applicant]
Zeigler, D. R., “Bacillus thuringiensis and Bacillus cereus,” Bacillus Genetic Stock Center Catalog of Strains, 1999, Seventh Edition, vol. 2, 58 pages. [cited by applicant]
Zhou, Z., et al., “Immunogenicity of Recombinant Bacillus subtilis Spores Expressing Clonorchis sinensis Tegumental Protein,” Parasitology Research, 2008, pp. 293-297, vol. 102, Issue 2. [cited by applicant]
Zhou, Z., et al., “Oral Administration of a Bacillus subtilis Spore-Based Vaccine Expressing Clonorchis sinensis Tegumental Protein 22.3 kDa Confers Protection Against Clonorchis sinensis,” Vaccine, 2008, pp. 1817-1825,… [cited by applicant]
Zou, C., et al., “Bacillus megaterium Strain XTBG34 Promotes Plant Growth by Producing 2-pentylfuran,” Journal of Microbiology, Aug. 2010, pp. 460-466, vol. 48, No. 4. [cited by applicant]
Diaz, K., et al., “Root-Promoting Rhizobacteria in Eucalyptus globulus Cuttings,” World Journal of Microbiology and Biotechnology, 2009, pp. 867-873, vol. 25. [cited by applicant]
Egorov, M. A., et al., “Growth Stimulating Effect of a Bacilus megaterium Strain in the Greenhouse Experiment,” Vestnik of Altay State Agricultural University, 2012, pp. 46-49, vol. 89, No. 3. [cited by applicant]
Frankel, A. E., et al., “Characterization of Diphtheria Fusion Proteins Targeted to the Human Interleukin-3 Receptor,” Protein Engineering, 2000, pp. 575-581, vol. 13, No. 8. [cited by applicant]
Cited By (2)
US 12,527,323 US 12,630,484