IP Library Granted Patent US 12,545,900
Granted Patent B2
US 12,545,900 · App. 17/270,234 · Granted Feb 10, 2026

CGAS/DNCV-like nucleotidyltransferases and uses thereof

Inventors: Aaron Whiteley (Brookline, MA); Philip J. Kranzusch (Brighton, MA); John Mekalanos (Newton, MA); James Eaglesham (Boston, MA)
Assignees: Dana-Farber Cancer Institute, Inc.; President and Fellows of Harvard College
C12N9/1241C12N1/20C12N11/06C12N15/10C12N15/1137C12N15/70C12N15/8509G01N33/5023G01N33/573G16B15/30C12N2015/8527C12N2310/14G01N2333/91245
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 12,545,900
App. No.
17/270,234
Granted
Feb 10, 2026
Kind
B2
Abstract

The present invention is based, in part, on the discovery and characterization of the CD-NTase family of proteins, as well as compositions comprising CD-NTases, methods of producing nucleotide-based second messengers using such polypeptides, and methods of screening for modulators of the structure, expression, and/or activity of such polypeptides.

Claims (15)

1 . A modified polypeptide that catalyzes production of cyclic di-purine nucleotides, wherein said polypeptide comprises an amino acid sequence having the cyclic dinucleotidyltransferase (CD-NTase) amino acid sequence of SEQ ID NO: 198 and further comprises amino acid residue S at the position corresponding to N166 of SEQ ID NO: 198.

2 . The modified polypeptide of claim 1 , wherein the cyclic di-purine nucleotides comprise cyclic-di-adenosine monophosphate (c-di-AMP).

3 . The modified polypeptide of claim 1 , further comprising a heterologous polypeptide.

4 . The modified polypeptide of claim 3 , wherein the heterologous polypeptide is selected from the group consisting of a signal peptide, a peptide tag, a dimerization domain, an oligomerization domain, an antibody, and an antibody fragment.

5 . The modified polypeptide of claim 1 , wherein the modified polypeptide is immobilized on an object selected from the group consisting of a cell, a metal, a resin, a polymer, a ceramic, a glass, a microelectrode, a graphitic particle, a bead, a gel, a plate, an array, and a capillary tube.

6 . A composition comprising the modified polypeptide of claim 1 and a pharmaceutically acceptable excipient, diluent, or carrier.

7 . An isolated nucleic acid molecule encoding the modified polypeptide of claim 1 .

8 . A vector comprising the nucleic acid molecule of claim 7 .

9 . The vector of claim 8 , wherein the vector is an expression vector.

10 . A host cell transfected with the vector of claim 9 .

11 . A method of producing a polypeptide comprising culturing the host cell of claim 10 in an appropriate culture medium to, thereby, produce the polypeptide.

12 . The method of claim 11 , wherein:

i) the host cell is a bacterial cell or a eukaryotic cell;

ii) the host cell is genetically engineered to express a selectable marker; and/or

iii) further comprising the step of isolating the polypeptide from the medium or host cell.

Assignments (4)
CORRECTIVE ASSIGNMENT TO CORRECT THE INVENTOR PHILIP J. KRANZUSCH'S FIRST NAME SPELLING PREVIOUSLY RECORDED ON REEL 62686 FRAME 477. ASSIGNOR(S) HEREBY CONFIRMS THE ASSIGNMENT. Recorded Jun 11, 2024
From: KRANZUSCH, PHILP J.; EAGLESHAM, JAMES
To: DANA-FARBER CANCER INSTITUTE, INC.
Reel/Frame 068406/0577 →
CONFIRMATORY LICENSE Recorded Nov 22, 2023
From: HARVARD UNIVERSITY
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 065664/0712 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 14, 2023
From: EAGLESHAM, JAMES; KRANZUSCH, PHILLIP J.
To: DANA-FARBER CANCER INSTITUTE, INC.
Reel/Frame 062686/0477 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 14, 2023
From: MEKALANOS, JOHN J.; WHITELEY, AARON THOMAS
To: PRESIDENT AND FELLOWS OF HARVARD COLLEGE
Reel/Frame 062686/0528 →
Continuity (3)
Provisional Application 62769163 · Nov 19, 2018
Provisional Application 62727647 · Sep 6, 2018
Related Publication 20220127586A1 · Apr 28, 2022
References Cited (26)
US 20190183917A1 · Birkus et al. · 2019 [cited by applicant]
CN 105969754A · 2016 [cited by applicant]
WO WO2017049127A1 · 2017 [cited by applicant]
WO WO2018115149A1 · 2018 [cited by applicant]
WO WO2018115140A2 · 2018 [cited by examiner]
WO WO2020051197A1 · 2020 [cited by applicant]
Rossolini et al. Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B b-lactamase showing a broad substrate profile. Biochem J. 332: 145-152. (Yea… [cited by examiner]
NCBI Blast (Nucleotide Sequence Elizabethkingia meningoseptica). https://blast.ncbi.nlm.nih.gov/Blast.cgi#alnHdr_1403377878 (Year: 2020). [cited by examiner]
NCBI Blast (Protein Sequence Elizabethkingia meningoseptica). https://blast.ncbi.nlm.nih.gov/Blast.cgi#alnHdr_WP_016200549 (Year: 2020). [cited by examiner]
Fisher Scientific (BD Difco BHI Agar). https://www.fishersci.com/shop/products/ bd-difco-dehydrated-culture-media-brain-heart-infusion-agar-3/p-4902056 (Year: 2024). [cited by examiner]
Thaller et al. Characterization and sequence of PhoC, the principal phosphate-irrepressible acid p hosp hatase of Morganella morganii. Microbiology 140: 1341-1350. (Year: 1994). [cited by examiner]
GenBank ( [cited by examiner]
Corrales et al., “Direct activation of STING in the tumor microenvironment leads to potent and systemic tumor regression and immunity,” Cell Reports, 11(7): 1018-1030 (2015). [cited by applicant]
Diner et al., “The innate immune DNA sensor cGAS produces a noncanonical cyclic dinucleotide that activates human STING,” Cell Reports, 3(5): 1355-1361 (2013). [cited by applicant]
Extended European Search Report for EP Application No. 19857772.8 dated May 10, 2022. [cited by applicant]
Govande et al., “Molecular basis of CD-NTase nucleotide selection in CBASS anti-phage defense,” Cell Reports, 35(9): 109206 (2021). [cited by applicant]
Kranzusch., “cGAS and CD-NTase enzymes: structure, mechanism, and evolution,” Current Opinion in Structural Biology, 59: 178-187 (2019). [cited by applicant]
Launer-Felty et al., “Enzymatic synthesis of cyclic dinucleotide analogs by a promiscuous cyclic-AMP-GMP synthetase and analysis of cyclic dinucleotide responsive riboswitches”, Nucleic Acids Research, 46(6): 2765-2776 … [cited by applicant]
Zhou et al., “Structure of the Human cGAS-DNA Complex Reveals Enhanced Control of Immune Surveillance,” Cell, 174(2): 300-311.e11 (2018). [cited by applicant]
Zhu et al., “Structural biochemistry of a Vibrio cholerae dinucleotide cyclase reveals cyclase activity regulation by folates,” Molecular Cell, 55(6): 931-937 (2014). [cited by applicant]
International Preliminary Report on Patentability for International Application No. PCT/US2019/049478 mailed Mar. 3, 2021. [cited by applicant]
International Search Report and Written Opinion for International Application No. PCT/US2019/049478 dated Dec. 27, 2019. [cited by applicant]
Kato et al., “Structural Basis for the Catalytic Mechanism of DncV, Bacterial Homolog of Cyclic GMP-AMP Synthase,” Structure 23(5):843-850 (2015). [cited by applicant]
Kranzusch et al., “Structure-guided reprogramming of human cGAS dinucleotide linkage specificity,” Cell 158(5):1011-1021 (2014). [cited by applicant]
Whiteley et al., “Bacterial cGAS-like enzymes synthesize diverse nucleotides signals,” Nature 567(7747):194-199 (2019). [cited by applicant]
Sadler et al., “Synthetic strategies toward carbocyclic purine-pyrimidine hybrid nucleosides.” Bioorg Med Chem. Aug. 1, 2009; 17(15): 5520-5525. [cited by applicant]