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Structural basis of Gabija anti-phage defence and viral immune evasion.
Antine, Sadie P; Johnson, Alex G; Mooney, Sarah E; Leavitt, Azita; Mayer, Megan L; Yirmiya, Erez; Amitai, Gil; Sorek, Rotem; Kranzusch, Philip J.
Afiliación
  • Antine SP; Department of Microbiology, Harvard Medical School, Boston, MA, USA.
  • Johnson AG; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA, USA.
  • Mooney SE; Department of Microbiology, Harvard Medical School, Boston, MA, USA.
  • Leavitt A; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA, USA.
  • Mayer ML; Department of Microbiology, Harvard Medical School, Boston, MA, USA.
  • Yirmiya E; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA, USA.
  • Amitai G; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
  • Sorek R; Harvard Center for Cryo-Electron Microscopy, Harvard Medical School, Boston, MA, USA.
  • Kranzusch PJ; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
Nature ; 625(7994): 360-365, 2024 Jan.
Article en En | MEDLINE | ID: mdl-37992757
Bacteria encode hundreds of diverse defence systems that protect them from viral infection and inhibit phage propagation1-5. Gabija is one of the most prevalent anti-phage defence systems, occurring in more than 15% of all sequenced bacterial and archaeal genomes1,6,7, but the molecular basis of how Gabija defends cells from viral infection remains poorly understood. Here we use X-ray crystallography and cryo-electron microscopy (cryo-EM) to define how Gabija proteins assemble into a supramolecular complex of around 500 kDa that degrades phage DNA. Gabija protein A (GajA) is a DNA endonuclease that tetramerizes to form the core of the anti-phage defence complex. Two sets of Gabija protein B (GajB) dimers dock at opposite sides of the complex and create a 4:4 GajA-GajB assembly (hereafter, GajAB) that is essential for phage resistance in vivo. We show that a phage-encoded protein, Gabija anti-defence 1 (Gad1), directly binds to the Gabija GajAB complex and inactivates defence. A cryo-EM structure of the virally inhibited state shows that Gad1 forms an octameric web that encases the GajAB complex and inhibits DNA recognition and cleavage. Our results reveal the structural basis of assembly of the Gabija anti-phage defence complex and define a unique mechanism of viral immune evasion.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterias / Proteínas Bacterianas / Bacteriófagos / Multimerización de Proteína / Evasión Inmune Idioma: En Revista: Nature Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterias / Proteínas Bacterianas / Bacteriófagos / Multimerización de Proteína / Evasión Inmune Idioma: En Revista: Nature Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido