Structural dissection of vaccinia G9 identifies residues essential for membrane fusion and complex assembly.

ABSTRACT: Vaccinia virus, a prototypical poxvirus, utilizes a unique multi-protein entry fusion complex (EFC), comprising 11 components, to mediate membrane fusion during host cell entry. Although the crystal structure of a truncated form of the G9 protein has been determined, the functional relevance of its structural features remains poorly understood. In this study, we systematically analyzed 47 G9 mutants to identify critical functional residues. Using trans-complementation assays, co-immunoprecipitation, membrane fusion assays, and structural analysis, we identified nine key mutants, which were categorized into three functional groups. Group 1 mutants failed to interact with A16 and other EFC components, highlighting their essential roles in G9-A16 subcomplex formation. Group 2 and Group 3 muta

SUBMITTER: Chiu H-J 

PROVIDER: S-EPMC12456145 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature