The vaccinia chondroitin sulfate binding protein drives host membrane curvature to facilitate fusion

ABSTRACT: Cellular attachment of viruses determines their cell tropism and species specificity. For entry, vaccinia, the prototypic poxvirus, relies on four binding proteins and an eleven-protein entry fusion complex. The contribution of the individual virus binding proteins to virion binding orientation and membrane fusion is unclear. Here, we show that virus binding proteins guide side-on virion binding and promote curvature of the host membrane towards the virus fusion machinery to facilitate fusion. Using a membrane-bleb model system together with super-resolution and electron microscopy we find that side-bound vaccinia virions induce membrane invagination in the presence of low pH. Repression or deletion of individual binding proteins reveals that three of four contribute to binding orientation

SUBMITTER: Dr. Laura Pokorny 

PROVIDER: S-SCDT-10_1038-S44319-023-00040-2 | biostudies-other |

REPOSITORIES: biostudies-other