Clathrin Potentiates Vaccinia-Induced Actin Polymerization to Facilitate Viral Spread

Ashley C. Humphries; Mark Dodding; David J. Barry; Lucy M. Collinson; Charlotte H. Durkin; Michael Way

doi:10.1016/j.chom.2012.08.002

Clathrin Potentiates Vaccinia-Induced Actin Polymerization to Facilitate Viral Spread

Ashley C. Humphries, Mark Dodding, David J. Barry, Lucy M. Collinson, Charlotte H. Durkin, Michael Way

London Research Institute

Research output: Contribution to journal › Article › peer-review

43 Citations (Scopus)

Abstract

During their egress, newly assembled vaccinia virus particles fuse with the plasma membrane and enhance their spread by inducing Arp2/3-dependent actin polymerization. Investigating the events surrounding vaccinia virus fusion, we discovered that vaccinia transiently recruits clathrin in a manner dependent on the clathrin adaptor AP-2. The recruitment of clathrin to vaccinia dramatically enhances the ability of the virus to induce actin-based motility. We demonstrate that clathrin promotes clustering of the virus actin tail nucleator A36 and host N-WASP, which activates actin nucleation through the Arp2/3 complex. Increased clustering enhances N-WASP stability, leading to more efficient actin tail initiation and sustained actin polymerization. Our observations uncover an unexpected role for clathrin during virus spread and have important implications for the regulation of actin polymerization.

Original language	English
Pages (from-to)	346-359
Number of pages	14
Journal	Cell Host and Microbe
Volume	12
Issue number	3
DOIs	https://doi.org/10.1016/j.chom.2012.08.002
Publication status	Published - 13 Sept 2012

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title = "Clathrin Potentiates Vaccinia-Induced Actin Polymerization to Facilitate Viral Spread",

abstract = "During their egress, newly assembled vaccinia virus particles fuse with the plasma membrane and enhance their spread by inducing Arp2/3-dependent actin polymerization. Investigating the events surrounding vaccinia virus fusion, we discovered that vaccinia transiently recruits clathrin in a manner dependent on the clathrin adaptor AP-2. The recruitment of clathrin to vaccinia dramatically enhances the ability of the virus to induce actin-based motility. We demonstrate that clathrin promotes clustering of the virus actin tail nucleator A36 and host N-WASP, which activates actin nucleation through the Arp2/3 complex. Increased clustering enhances N-WASP stability, leading to more efficient actin tail initiation and sustained actin polymerization. Our observations uncover an unexpected role for clathrin during virus spread and have important implications for the regulation of actin polymerization.",

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T1 - Clathrin Potentiates Vaccinia-Induced Actin Polymerization to Facilitate Viral Spread

AU - Humphries, Ashley C.

AU - Dodding, Mark

AU - Barry, David J.

AU - Collinson, Lucy M.

AU - Durkin, Charlotte H.

AU - Way, Michael

PY - 2012/9/13

Y1 - 2012/9/13

N2 - During their egress, newly assembled vaccinia virus particles fuse with the plasma membrane and enhance their spread by inducing Arp2/3-dependent actin polymerization. Investigating the events surrounding vaccinia virus fusion, we discovered that vaccinia transiently recruits clathrin in a manner dependent on the clathrin adaptor AP-2. The recruitment of clathrin to vaccinia dramatically enhances the ability of the virus to induce actin-based motility. We demonstrate that clathrin promotes clustering of the virus actin tail nucleator A36 and host N-WASP, which activates actin nucleation through the Arp2/3 complex. Increased clustering enhances N-WASP stability, leading to more efficient actin tail initiation and sustained actin polymerization. Our observations uncover an unexpected role for clathrin during virus spread and have important implications for the regulation of actin polymerization.

AB - During their egress, newly assembled vaccinia virus particles fuse with the plasma membrane and enhance their spread by inducing Arp2/3-dependent actin polymerization. Investigating the events surrounding vaccinia virus fusion, we discovered that vaccinia transiently recruits clathrin in a manner dependent on the clathrin adaptor AP-2. The recruitment of clathrin to vaccinia dramatically enhances the ability of the virus to induce actin-based motility. We demonstrate that clathrin promotes clustering of the virus actin tail nucleator A36 and host N-WASP, which activates actin nucleation through the Arp2/3 complex. Increased clustering enhances N-WASP stability, leading to more efficient actin tail initiation and sustained actin polymerization. Our observations uncover an unexpected role for clathrin during virus spread and have important implications for the regulation of actin polymerization.

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DO - 10.1016/j.chom.2012.08.002

M3 - Article

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VL - 12

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JO - Cell Host and Microbe

JF - Cell Host and Microbe

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ER -

Clathrin Potentiates Vaccinia-Induced Actin Polymerization to Facilitate Viral Spread

Abstract

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