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Cited by 9interferon and immune responsesBacteriophages and microbial interactionsDNA and Nucleic Acid Chemistry

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity

Open access
Wassarman, Douglas R., Pfaff, Patrick, Paulo, Joao A., Gygi, Steven P., Shokat, Kevan M., Kranzusch, Philip J.·2025·Science
DOI 10.1126/science.adx6053PMC PMC13044698

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Abstract

7-Deazapurines are nucleobase analogs essential for nucleic acid modifications in nearly all cellular life. In this study, we discovered a role for 7-deazapurines in protein modification within type IV cyclic oligonucleotide–based antiviral signaling system (CBASS) antiphage defense and defined functions for CBASS ancillary proteins Cap9 and Cap10 in nucleobase-protein conjugation. A structure of Cap10 revealed a transfer RNA transglycosylase family enzyme remodeled to bind a partner cGAS/DncV–like nucleotidyltransferase that is modified with an N-terminal 7-amido-7-deazaguanine (NDG) nucleobase. A structure of Cap9 explained how this QueC-like enzyme co-opts a 7-deazapurine biosynthetic reaction to install NDG. We show that Cap9, Cap10, and protein deazaguanylation are essential for host defense against phage infection. Our results define a 7-deazapurine protein modification and explain how nucleobase biosynthetic machinery has been repurposed for antiviral immunity.

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Metadata

Authors
Wassarman, D. R., Pfaff, P., Paulo, J. A., Gygi, S. P., Shokat, K. M., & Kranzusch, P. J.
Affiliations
  • Harvard University (US)
  • Howard Hughes Medical Institute (US)
  • Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Corresponding author
Kranzusch, Philip J.
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2025-09-25
Volume
389
Issue
6767
Pages
1347-1352
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.adx6053
PMC
PMC13044698
OpenAlex
W4414499149
Cited by
9
References
1
Citations by year
2026: 7 · 2025: 2
FWCI
3.31
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Science (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (submittedVersion, cc-by)
  • PubMed Central (submittedVersion, cc-by)
Funders
  • National Science Foundation (P30GM133893, DE-SC0012704)
  • U.S. Department of Energy (DE‐SC0012704, KP1607011, SC0012704., P30GM133893)
  • Parker Institute for Cancer Immunotherapy
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (214278)
  • National Institutes of Health (GM97645, 1dp2gm146250-01)
  • Office of Science (DE-SC-0012704, SC0012704, KP1607011)
  • National Institute of General Medical Sciences (1DP2GM146250, 1DP2GM146250-01, DP2 GM146250, R01GM132129, GM97645, GM132129, P30GM133893, T32GM145460)
  • Biological and Environmental Research (DE-SC0012704, KP1607011)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
  • Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords
7-deazapurines, anti-phage defense, protein modification, phage resistance, host-virus interaction

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