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

Gray, RDM; Albrecht, D; Beerli, C; Huttunen, M; Cohen, GH; White, IJ; Burden, JJ; ... Mercer, J; + view all (2019) Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion. [Letter]. Nature Microbiology 10.1038/s41564-019-0488-4. (In press). Green open access

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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 activity2,3. 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. Repression of individual components of the fusion complex disrupts fusion-machinery polarization, consistent with the reported loss of fusion activity5. Furthermore, we show that displacement of functional fusion complexes from virion tips disrupts the formation of fusion pores and infection kinetics. Our results demonstrate how the protein architecture of poxviruses directly contributes to the efficiency of membrane fusion, and suggest that nanoscale organization may be an intrinsic property of these viruses to assure successful infection

Type: Article
Title: Nanoscale polarization of the entry fusion complex of vaccinia virus drives efficient fusion
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/s41564-019-0488-4
Publisher version: https://doi.org/10.1038/s41564-019-0488-4
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
URI: https://discovery.ucl.ac.uk/id/eprint/10077757
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