IP Library Granted Patent US 12,480,146
Granted Patent B2
US 12,480,146 · App. 17/785,488 · Granted Nov 25, 2025

Microbial production of mogrol and mogrosides

Inventors: Michelle N. Goettge (Cambridge, MA); Ryan N. Philippe (Orleans, CA); Ajikumar Parayil Kumaran (Cambridge, MA); Christine Nicole S. Santos (Cambridge, MA); Jason Eric Donald (Cambridge, MA); Christopher Frei (Cambridge, MA); Aaron Love (Cambridge, MA); Kaitlin Chambers (Cambridge, MA); Joyce Samson (Cambridge, MA); Christopher Toomey (Cambridge, MA)
Assignee: Manus Bio Inc.
C12P17/02C12N9/0077C12N9/14C12P5/007C12P19/18C12P19/56C12Y303/0201C12Y504/99008
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 12,480,146
App. No.
17/785,488
Granted
Nov 25, 2025
Kind
B2
Abstract

The present invention provides host cells and methods for making mogrol glycosides, including Mogroside V (Mog.V), Mogroside VI (Mog.VI), Iso-Mogroside V (Isomog.V), siamenoside, and glycosylation products that are minor products in Siraitia grosvenorii . The invention provides engineered enzymes and engineered host cells for producing mogrol glycosylation products, such as Mog.V, Mog.VI, and Isomog.V, at high purity and/or yield. The present technology further provides methods of making products containing mogrol glycosides, such as Mog.V, Mog.VI, and Isomog.V, including food products, beverages, oral care products, sweeteners, and flavoring products.

Claims (37)

1 . A method for making mogrol or mogroside, comprising:

providing a recombinant microbial host cell expressing a heterologous enzyme pathway catalyzing the conversion of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) to mogrol or mogroside, the heterologous enzyme pathway comprising:

a farnesyl diphosphate synthase (FPPS),

a squalene synthase (SQS),

a squalene epoxidase (SQE) catalyzing the formation of 2,3;22,23-dioxidosqualene from squalene,

a triterpene cyclase (TTC) catalyzing the formation of 24,25-epoxycucurbitadienol from 2,3;22,23-dioxidosqualene,

an epoxide hydrolase (EPH) catalyzing the formation of 24,25-dihydroxycucurbitadienol from 24,25-epoxycucurbitadienol, and

a cytochrome P450 enzyme catalyzing the formation of mogrol from 24,25-dihydroxycucurbitadienol;

wherein the cytochrome P450 enzyme comprises an amino acid sequence having at least 85% sequence identity with SEQ ID NO: 171; and

culturing the host cell under conditions for producing the mogrol or mogroside.

2 . The method of claim 1 , wherein the squalene epoxidase comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 39.

3 . The method of claim 1 , wherein the SQS comprises an amino acid sequence that is at least 90% identical to an amino acid sequence selected from SEQ ID NOS: 2 to 16, 166, and 167.

4 . The method of claim 1 , wherein the TTC comprises an amino acid sequence that is at least 90% identical to an amino acid sequence selected from SEQ ID NOS: 40, 191, 192, and 193.

5 . The method of claim 4 , wherein the TTC comprises an amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO: 40.

6 . The method of claim 1 , wherein the heterologous enzyme pathway comprises at least one TTC that comprises an amino acid sequence that is at least 90% identical to one of SEQ ID NO: 191, SEQ ID NO: 192, and SEQ ID NO: 193.

7 . The method of claim 1 , wherein the EPH comprises an amino acid sequence that is at least 90% identical to one of: SEQ ID NOS: 189, 58, 184, 185, 187, 188, 190, and 212.

8 . The method of claim 1 , wherein the cytochrome P450 comprises an amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO: 171.

9 . The method of claim 1 , wherein the heterologous enzyme pathway further comprises one or more uridine diphosphate-dependent glycosyltransferase (UGT) enzymes, thereby producing one or more mogrol glycosides.

10 . The method of claim 9 , wherein the one or more mogrol glycosides are selected from Mog.II-E, Mog.III, Mog.III-A1, Mog.III-A2, Mog.III, Mog.IV, Mog.IV-A, siamenoside, Mog.V, and Mog.VI.

11 . The method of claim 9 , wherein at least one uridine diphosphate dependent glycosyltransferase (UGT) enzyme comprises an amino acid sequence having at least 90% sequence identity to one of SEQ ID NO: 164, 165, 138, 204 to 211, and 213 to 218.

12 . The method of claim 11 , wherein at least one UGT enzyme further comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 146.

13 . The method of claim 11 , wherein at least one UGT enzyme further comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 202.

14 . The method of claim 11 , wherein the microbial host cell expresses at least three UGT enzymes: a first UGT enzyme catalyzing primary glycosylation at the C24 hydroxyl of mogrol, a second UGT enzyme catalyzing primary glycosylation at the C3 hydroxyl of mogrol, and a third UGT enzyme catalyzing one or more branching glycosylation reactions.

15 . The method of claim 1 , wherein the microbial host cell is a bacterium selected from Escherichia coli, Bacillus subtilis, Corynebacterium glutamicum, Rhodobacter capsulatus, Rhodobacter sphaeroides, Zymomonas mobilis, Vibrio natriegens , or Pseudomonas putida ; or is a yeast selected from Saccharomyces cerevisiae, Pichia pastoris , and Yarrowia lipolytica.

16 . The method of claim 1 , wherein the mogrol glycoside products are recovered from the extracellular media.

17 . A method for making a product comprising a mogrol glycoside, comprising:

producing a mogrol glycoside in accordance with claim 1 , and incorporating the mogrol glycoside into a product.

18 . A microbial host cell expressing a heterologous enzyme pathway catalyzing the conversion of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) to mogrol or mogroside, the heterologous enzyme pathway comprising:

a farnesyl diphosphate synthase (FPPS),

a squalene synthase (SQS),

a squalene epoxidase (SQE) catalyzing the formation of 2,3;22,23-dioxidosqualene from squalene,

a triterpene cyclase (TTC) catalyzing the formation of 24,25-epoxycucurbitadienol from 2,3;22,23-dioxidosqualene,

an epoxide hydrolase (EPH) catalyzing the formation of 24,25-dihydroxycucurbitadienol from 24,25-epoxycucurbitadienol, and

a cytochrome P450 enzyme catalyzing the formation of mogrol from 24,25-dihydroxycucurbitadienol;

wherein the cytochrome P450 enzyme comprises an amino acid sequence having at least 85% sequence identity with SEQ ID NO: 171.

19 . The method of claim 1 , wherein the microbial host cell further comprises a cytochrome P450 reductase enzyme.

20 . The method of claim 18 , wherein the microbial host cell further comprises a cytochrome P450 reductase enzyme.

Assignments (4)
SECURITY INTEREST Recorded Sep 8, 2025
From: MANUS BIO INC.; STO.PERU I LLC; STO.PERU II LLC; MANUS INTERMEDIATE INC.; MANUS INSCRIPTA, INC.
To: SYMBIOTIC CAPITAL AGENCY LLC, AS ADMINISTRATIVE AND COLLATERAL AGENT
Reel/Frame 072836/0255 →
RELEASE OF SECURITY INTEREST Recorded May 9, 2025
From: EICF AGENT LLC
To: MANUS BIO INC.
Reel/Frame 071247/0658 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Mar 5, 2025
From: GOETTGE, MICHELLE N.; PHILIPPE, RYAN N.; KUMARAN, AJIKUMAR PARAYIL; SANTOS, CHRISTINE NICOLE S.; DONALD, JASON ERIC; FREI, CHRISTOPHER; LOVE, AARON; CHAMBERS, KAITLIN; SAMSON, JOYCE; TOOMEY, CHRISTOPHER; NIEMINEN, ERIC
To: MANUS BIO INC.
Reel/Frame 070405/0979 →
SECURITY AGREEMENT Recorded Jan 5, 2023
From: MANUS BIO INC.
To: EICF AGENT LLC
Reel/Frame 062295/0756 →
Continuity (4)
Provisional Application 63075631 · Sep 8, 2020
Provisional Application 63085557 · Sep 30, 2020
Provisional Application 62948657 · Dec 16, 2019
Related Publication 20230042171A1 · Feb 9, 2023
References Cited (34)
US 10011859B2 · Liu · 2018 [cited by examiner]
US 10480015B2 · Kumaran et al. · 2019 [cited by applicant]
US 10633685B2 · Houghton-Larsen · 2020 [cited by examiner]
US 10662442B2 · Kumaran et al. · 2020 [cited by applicant]
US 10774314B2 · Donald et al. · 2020 [cited by applicant]
US 10774346B2 · Kumaran et al. · 2020 [cited by applicant]
US 11060124B2 · Patron · 2021 [cited by examiner]
US 11339412B2 · Kumaran et al. · 2022 [cited by applicant]
US 11352648B2 · Kumaran et al. · 2022 [cited by applicant]
US 20160319317A1 · Ono · 2016 [cited by applicant]
US 20180070622A1 · Van Der Hoeven et al. · 2018 [cited by applicant]
US 20180155734A1 · Guo et al. · 2018 [cited by applicant]
US 20180223264A1 · Vroom et al. · 2018 [cited by applicant]
US 20210032669A1 · Philippe · 2021 [cited by examiner]
WO WO2014086842A1 · 2014 [cited by applicant]
WO WO2016038617A1 · 2016 [cited by applicant]
WO WO2016050890A2 · 2016 [cited by applicant]
WO WO2019169027A2 · 2019 [cited by applicant]
Banerjee et al., Improving enzymes for biomass conversion: A basic research perspective. Bioenerg. Res., 2010, vol. 3: 82-92. (Year: 2010). [cited by examiner]
Broun et al., Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. Science, 1998, vol. 282: 1315-1317. (Year: 1998). [cited by examiner]
Chica et al., Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design. Curr. Opi. Biotechnol., 2005, vol. 16: 378-384. (Year: 2005). [cited by examiner]
Li et al., A structural and data-driven approach to engineering plant cytochrome P450 enzyme. Science China., 2019, vol. 62(7): 873-882. (Year: 2019). [cited by examiner]
Rahimi et al., Triterpenoid-biosynthetic UDP-glycosyltransferase from plants. Biotechnol. Advances., 2019, vol. 37: 107394, pp. 1-18. (Year: 2019). [cited by examiner]
Seffernick et al., Melamine deaminase and Atrazine chlorohydrolase: 98 percent identical but functionally different. J. Bacteriol., 2001, vol. 183 (8): 2405-2410. (Year: 2001). [cited by examiner]
Sen et al., Developments in directed evolution for enzyme functions. Appl. Biochem. Biotechnol., 2007, vol. 143: 212-223. (Year: 2007). [cited by examiner]
Qiao et al., Identification of a novel specific cucurbitadienol synthase allele in Siraitia grosvenorii correlates with high catalytic activity. Molecules, 2019, vol. 79: 49-63. (Year: 2019). [cited by examiner]
Whisstock et al., Prediction of protein function from protein sequence. Q. Rev. Biophysics., 2003, vol. 36 (3): 307-340. (Year: 2003). [cited by examiner]
Witkowski et al., Conversion of b-ketoacyl synthase to a Malonyl Decarboxylase by replacement of the active cysteine with glutamine. Biochemistry, 1999, vol. 38: 11643-11650. (Year: 1999). [cited by examiner]
Devos et al., Practical limits of function prediction. Proteins: Structure, Function, and Genetics. 2000, vol. 41: 98-107. (Year: 2000). [cited by examiner]
Badouin, et al., “The sunflower genome provides insights into oil metabolism, flowering and Asterid evolution,” Nature, 2017, vol. 546, 14 pgs. [cited by applicant]
International Search Report and Written Opinion of corresponding International Application No. PCT/US20/065285 dated May 6, 2021. 13 pages. [cited by applicant]
Genpept, “cytochrome P450 87A3-like [ [cited by applicant]
Itkin, et al., “The biosynthetic pathway of the nonsugar, high-intensity sweetener morgroside V from [cited by applicant]
Itkin, et al., Correction “The biosynthetic pathway of the nonsugar, high-intensity sweetener morgroside V from [cited by applicant]