Abstract
The spatial distribution of binding and fusion proteins on most viruses and the functional relevance of this organization remains largely unexplored. Employing super-resolution microscopy we define the nanoscale membrane architecture of the prototypic poxvirus, vaccinia. We show that binding and entry fusion complex (EFC) proteins are organized into distinct functional domains with fusion proteins polarized to the tips of virions. Repression of individual EFC components disrupted fusion protein polarization, correlating with a loss of fusion activity. Repression of vaccinia A27, a non-EFC protein implicated in fusion, revealed that disruption of EFC localization impacts virus fusion pore formation. We propose that the polarized distribution of EFCs is essential for poxvirus fusion efficiency.
