Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion.

ABSTRACT: To achieve efficient binding and subsequent fusion, most enveloped viruses encode between one and five proteins¹. For many viruses, the clustering of fusion proteins-and their distribution on virus particles-is crucial for fusion activity^2,3. Poxviruses, the most complex mammalian viruses, dedicate 15 proteins to binding and membrane fusion⁴. However, the spatial organization of these proteins and how this influences fusion activity is unknown. Here, we show that the membrane of vaccinia virus is organized into distinct functional domains that are critical for the efficiency of membrane fusion. Using super-resolution microscopy and single-particle analysis, we found that the fusion machinery of vaccinia virus resides exclusively in clusters at virion tips.

SUBMITTER: Gray RDM 

PROVIDER: S-EPMC7617052 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature