IP Library Granted Patent US 12,441,783
Granted Patent B2
US 12,441,783 · App. 17/418,906 · Granted Oct 14, 2025

Pathogen binding proteins

Inventors: Andreas Hougaard Laustsen (Copenhagen N, DK); Sandra Wingaard Thrane (Herlev, DK); Mads Aage Laustsen (Gentofte, DK)
Assignee: Bactolife APS
C07K16/1232A61P1/12A61P31/04A61K2039/505C07K2317/31C07K2317/569C07K2317/64C07K2317/76C07K2317/92C07K2317/94
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 12,441,783
App. No.
17/418,906
Granted
Oct 14, 2025
Kind
B2
Abstract

The present invention relates to proteins, compositions and their use, wherein said protein comprises a first peptide having a first binding specificity, a second peptide having a second binding specificity and a linker, wherein said first and said second peptides bind at least one pathogen surface component and/or at least one molecule produced by a pathogen.

Claims (63)

1. An isolated protein comprising

a first peptide;

a second peptide; and

a linker,

wherein said first and said second peptides bind at least one pathogen surface component and/or at least one molecule produced by a pathogen,

wherein:

said first peptide is a single domain antibody comprising three complementarity determining regions CDR1, CDR2 and CDR3, wherein:

CDR1 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 27,

CDR2 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 29, and

CDR3 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 31, and

said second peptide is a single domain antibody comprising three complementarity determining regions CDR1, CDR2 and CDR3, wherein:

CDR1 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 27,

CDR2 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 29, and

CDR3 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 31, and

wherein said protein comprises an amino acid sequence according to SEQ ID NO:15 or an amino acid sequence having at least 90% identity to SEQ ID NO:15; or

said first peptide is a single domain antibody comprising three complementarity determining regions CDR1, CDR2, and CDR3, wherein:

CDR1 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 28,

CDR2 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 30, and

CDR3 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 32, and

said second peptide is a single domain antibody comprising three complementarity determining regions CDR1, CDR2, and CDR3, wherein:

CDR1 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 28,

CDR2 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 30, and

CDR3 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 32, and

wherein said protein comprises an amino acid sequence according to SEQ ID NO:13 or an amino acid sequence having at least 90% identity to SEQ ID NO:13; or

said first peptide is a single domain antibody comprising an amino acid sequence according to SEQ ID NO: 5 or an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 5, wherein any sequence variance is outside the CDRs;

said second peptide is a single domain antibody comprising an amino acid sequence according to SEQ ID NO: 5 or an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 5, wherein any sequence variance is outside the CDRs; and

wherein said protein comprises an amino acid sequence according to SEQ ID NO:14 or an amino acid sequence having at least 90% identity to SEQ ID NO:14.

2. The protein according to claim 1 , wherein the linker is a GS linker.

3. The protein according to claim 2 , wherein said GS linker is of the structure (G x S) n , where x is a number between 1 and 10 and n refers to a number of repeats of the G x S sequence, where n is between 1 and 10.

4. The protein according to claim 1 , wherein said protein comprises one or more further peptides binding to at least one pathogen surface component and/or at least one molecule produced by a pathogen.

5. The protein according to claim 1 , wherein said first and said second peptides both comprise an amino acid sequence according to SEQ ID NO:10 or an amino acid sequence having at least 90% sequence identity to SEQ ID NO:10.

6. An isolated nucleic acid molecule encoding the protein according to claim 1 , a vector comprising said nucleic acid molecule, or a recombinant host cell comprising said nucleic acid molecule or vector.

7. A dietary composition comprising a protein according to claim 1 , wherein the dietary composition further comprises one or more prebiotics, probiotics, synbiotics, proteins, lipids, carbohydrates, vitamins, fibers, and/or nutrients.

8. A pharmaceutical composition comprising a protein according to claim 1 , a nucleic acid molecule encoding said protein, a vector comprising said nucleic acid molecule, and/or a recombinant host cell comprising said nucleic acid molecule or vector.

9. A method for the prevention or treatment of a pathogen induced infection associated with an internal and/or external surface of a subject, comprising administering to said subject a protein according to claim 1 , a nucleic acid molecule encoding said protein, a vector comprising said nucleic acid molecule, a recombinant host cell comprising said nucleic acid molecule or vector, and/or a pharmaceutical composition the protein, nucleic acid molecule, vector and/or recombinant host cell and further comprising one or more excipients.

10. The method according to claim 9 , wherein the infection is a gastrointestinal infection.

11. The method according to claim 9 , wherein the subject is a pig.

12. The method of claim 9 , wherein said pathogen induced infection is post-weaning diarrhea (PWD) or Edema disease.

13. An isolated protein comprising

a first peptide;

a second peptide; and

a linker,

wherein said first and said second peptides bind at least one pathogen surface component and/or at least one molecule produced by a pathogen,

wherein:

said first peptide is a single domain antibody comprising three complementarity determining regions CDR1, CDR2 and CDR3, wherein:

CDR1 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 27,

CDR2 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 29, and

CDR3 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 31, and

said second peptide is a single domain antibody comprising three complementarity determining regions CDR1, CDR2 and CDR3, wherein:

CDR1 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 27,

CDR2 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 29, and

CDR3 has an amino acid sequence comprising an amino acid sequence of SEQ ID NO: 31, and

wherein said protein comprises an amino acid sequence according to SEQ ID NO:9 or an amino acid sequence having at least 90% identity to SEQ ID NO:9.

14. The protein according to claim 13 , wherein the linker is a GS linker.

15. The protein according to claim 14 , wherein said GS linker is of the structure (G x S) n , where x is a number between 1 and 10 and n refers to a number of repeats of the G x S sequence, where n is between 1 and 10.

16. The protein according to claim 13 , wherein said protein comprises one or more further peptides binding to at least one pathogen surface component and/or at least one molecule produced by a pathogen.

17. An isolated nucleic acid molecule encoding the protein according to claim 13 , a vector comprising said nucleic acid molecule, or a recombinant host cell comprising said nucleic acid molecule or vector.

18. A dietary composition comprising a protein according to claim 13 , wherein the dietary composition further comprises one or more prebiotics, probiotics, synbiotics, proteins, lipids, carbohydrates, vitamins, fibers, and/or nutrients.

19. A pharmaceutical composition comprising a protein according to claim 13 , a nucleic acid molecule encoding said protein, a vector comprising said nucleic acid molecule, and/or a recombinant host cell comprising said nucleic acid molecule or vector.

20. A method for the prevention or treatment of a pathogen induced infection associated with an internal and/or external surface of a subject, comprising administering to said subject a protein according to claim 13 , a nucleic acid molecule encoding said protein, a vector comprising said nucleic acid molecule, a recombinant host cell comprising said nucleic acid molecule or vector, and/or a pharmaceutical composition the protein, nucleic acid molecule, vector and/or recombinant host cell and further comprising one or more excipients.

21. The method according to claim 20 , wherein the infection is a gastrointestinal infection.

22. The method according to claim 20 , wherein the subject is a pig.

23. The method of claim 20 wherein said pathogen induced infection is post-weaning diarrhea (PWD) or Edema disease.

Assignments (2)
CHANGE OF NAME Recorded Nov 13, 2025
From: BACTOLIFE APS
To: BACTOLIFE A/S
Reel/Frame 073560/0859 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 28, 2021
From: LAUSTSEN, ANDREAS HOUGAARD; THRANE, SANDRA WINGAARD; LAUSTSEN, MADS AAGE
To: BACTOLIFE APS
Reel/Frame 056999/0649 →
Priority Claims (2)
WO PCT/DK2019/050004 · Jan 7, 2019 · international
EP 19201645 · Oct 7, 2019 · regional
Continuity (1)
Related Publication 20220119505A1 · Apr 21, 2022
References Cited (63)
US 9320792B2 · Bouche et al. · 2016 [cited by applicant]
US 10202441B2 · Shoemaker · 2019 [cited by applicant]
US 10704040B2 · Tran et al. · 2020 [cited by applicant]
US 20130136744A1 · Bouche et al. · 2013 [cited by applicant]
US 20160318996A1 · Hollands et al. · 2016 [cited by applicant]
US 20170173179A1 · Sawada et al. · 2017 [cited by applicant]
EP 1558645 · 2005 [cited by applicant]
WO 198809344A1 · 1988 [cited by applicant]
WO 199215682A1 · 1992 [cited by applicant]
WO 199316185A2 · 1993 [cited by applicant]
WO 199404678A1 · 1994 [cited by applicant]
WO 199946300A1 · 1999 [cited by applicant]
WO 2020035741A2 · 2003 [cited by applicant]
WO 2005017148A1 · 2005 [cited by applicant]
WO 2005044858 · 2005 [cited by applicant]
WO 2006056306 · 2006 [cited by applicant]
WO 2006079372A1 · 2006 [cited by applicant]
WO 2006127798 · 2006 [cited by applicant]
WO 2007010040 · 2007 [cited by applicant]
WO 2007025977 · 2007 [cited by applicant]
WO 2020099922A1 · 2009 [cited by applicant]
WO 2009095235 · 2009 [cited by applicant]
WO 2009147248 · 2009 [cited by applicant]
WO 2010125187 · 2010 [cited by applicant]
WO WO2011051327A2 · 2011 [cited by examiner]
WO 2011124612 · 2011 [cited by applicant]
WO 2012025619 · 2012 [cited by applicant]
WO 2012025621A1 · 2012 [cited by applicant]
WO 2012042026A1 · 2012 [cited by applicant]
WO 2012150319A1 · 2012 [cited by applicant]
WO 2013135896A1 · 2013 [cited by applicant]
WO 202013144266A1 · 2013 [cited by applicant]
WO 2014033313A1 · 2014 [cited by applicant]
WO 2014177595A1 · 2014 [cited by applicant]
WO 2014191146A1 · 2014 [cited by applicant]
WO 2015080099A1 · 2015 [cited by applicant]
WO 2016071438A2 · 2016 [cited by applicant]
WO 2016156465A1 · 2016 [cited by applicant]
WO 2016156466A1 · 2016 [cited by applicant]
WO 2016156468A1 · 2016 [cited by applicant]
WO 2017167997A1 · 2017 [cited by applicant]
WO 2017171535A2 · 2017 [cited by applicant]
WO 2020234642 · 2020 [cited by applicant]
WO 2020254826 · 2020 [cited by applicant]
WO 2020254827 · 2020 [cited by applicant]
WO 2020254828 · 2020 [cited by applicant]
WO 2021003456A1 · 2021 [cited by applicant]
WO 2021110816A1 · 2021 [cited by applicant]
WO 2021110817A1 · 2021 [cited by applicant]
Kritas, S.K. (2018). Probiotics and Prebiotics for the Health of Pigs and Horses. In: Di Gioia, D., Biavati, B. (eds) Probiotics and Prebiotics in Animal Health and Food Safety. Springer, Cham. https://doi.org/10.1007/9… [cited by examiner]
Beirnaert E, et al. Bivalent Llama Single-Domain Antibody Fragments against Tumor Necrosis Factor Have Picomolar Potencies due to Intramolecular Interactions. Front Immunol. Jul. 31, 2017;8:867. (2017) (Year: 2017). [cited by examiner]
Alzogaray, V. et al., Single-domain llama antibodies as specific intracellular inhibitors of SpvB, the actin ADP-ribosylating toxin of [cited by applicant]
Conrath et al., Camel Single-domain Antibodies as modular Building Units in Bispecific and Bivalent Antibody Constructs, Journal of Biological Chemistry, 276(10): 7346-7350, Oct. 25, 2000. [cited by applicant]
Gonzales, L. et al., Alkaline pH is a Signal for Optimal Production and Secretion of the Heat Labile Toxin, LT in Enterotoxigenic [cited by applicant]
Harmsen, M. et al., Enhancement of toxin- and virus neutralizing capacity of single-domain antibody fragments by N-glycosylation, Appl. Microbiol. Biotechnol., 84: 1087-1094, 2009. [cited by applicant]
Harmsen, M. et al., Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy, Appl. Microbiol. Biotechnol., 72: 544-551, 2006. [cited by applicant]
Harmsen, M. et al., Properties, production, and applications of camelid single-domain antibody fragments, Applied Microbiology and Biotechnology, 77(1): 13-22, Aug. 18, 2007. [cited by applicant]
Hussack et al., Neutralization of Clostridium difficile toxin A with single domain antibodies targeting the cell receptor binding domain, Journal of Biological Chemistry, 286(11): 8961-8976, Mar. 18, 2011. [cited by applicant]
Lo, A. et al., The molecular mechanism of Shiga toxin Stx2e neutralization by a single-domain antibody targeting the cell receptor-binding domain, J. Biol. Chem. 289: 25374-25381, 2014. [cited by applicant]
Moonens, K. et al., Nanobody Mediated Inhibition of Attachment of F18 Fimbriae Expressing [cited by applicant]
Stone et al., A novel pentamer versus pentamer approach to generating neutralizers of verotoxin 1, Molecular Immunology, 44(9): 2487-2491, Jan. 17, 2007. [cited by applicant]
Van Den Broeck, W. et al., Receptor-Dependent Immune Responses in Pigs after Oral Immunization with F4 Fimbriae, Infect. Immun., 67: 520-526, 1999. [cited by applicant]
Virdi, V. et al., Orally fed seeds producing designer IgAs protect weaned piglets against enterotoxigenic [cited by applicant]