Phage anti-CBASS protein simultaneously sequesters cyclic trinucleotides and dinucleotides.
Journal
bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187
Informations de publication
Date de publication:
01 Jun 2023
01 Jun 2023
Historique:
pubmed:
3
7
2023
medline:
3
7
2023
entrez:
3
7
2023
Statut:
epublish
Résumé
CBASS is a common anti-phage immune system that uses cyclic oligonucleotide signals to activate effectors and limit phage replication. In turn, phages encode anti-CBASS (Acb) proteins. We recently uncovered a widespread phage anti-CBASS protein Acb2 that acts as a "sponge" by forming a hexamer complex with three cGAMP molecules. Here, we identified that Acb2 binds and sequesters many CBASS and cGAS-produced cyclic dinucleotides
Identifiants
pubmed: 37398474
doi: 10.1101/2023.06.01.543220
pmc: PMC10312549
pii:
doi:
Types de publication
Preprint
Langues
eng
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM127489
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI168811
Pays : United States
Déclaration de conflit d'intérêts
Declaration of interests: J.B.-D. is a scientific advisory board member of SNIPR Biome and Excision Biotherapeutics, a consultant to LeapFrog Bio, and a scientific advisory board member and co-founder of Acrigen Biosciences. The Bondy-Denomy lab received research support from Felix Biotechnology. UCSF has filed a patent application related to this work with J.B.-D. and E.H. listed as inventors.