Nck- and N-WASP-dependent actin-based motility is conserved in divergent vertebrate poxviruses

Mark P Dodding, Michael Way

Research output: Contribution to journalArticle (Academic Journal)peer-review

40 Citations (Scopus)

Abstract

Vaccinia virus enhances its cell-to-cell spread by stimulating actin polymerization via Src- and Abl-mediated phosphorylation of the highly conserved orthopoxvirus protein A36. The Yatapoxvirus, Yaba-like disease virus (YLDV), also induces actin polymerization, although it lacks an obvious A36 ortholog. We found that the YLDV protein YL126 can functionally replace A36 to promote Nck- and N-WASP-dependent actin polymerization. At least five phosphorylated tyrosines in YL126, rather than a single residue as in A36, are able to recruit Nck to promote actin polymerization. As is the case for A36, YL126-mediated actin tail formation is enhanced by the recruitment of Grb2 via a single phosphorylated tyrosine in YL126. Furthermore, highly divergent YL126 orthologs in Yaba monkey tumor, lumpy skin disease, Shope fibroma, myxoma, and swine and squirrel poxviruses also stimulate Nck- and N-WASP-dependent actin polymerization, suggesting that actin-based motility represents a common mechanism to enhance the cell-to-cell spread of vertebrate poxviruses.

Original languageEnglish
Pages (from-to)536-50
Number of pages15
JournalCell Host & Microbe
Volume6
Issue number6
DOIs
Publication statusPublished - 17 Dec 2009

Keywords

  • Actins
  • Adaptor Proteins, Signal Transducing
  • Animals
  • Cell Line
  • Evolution, Molecular
  • Humans
  • Oncogene Proteins
  • Phosphorylation
  • Poxviridae Infections
  • Protein Binding
  • Vertebrates
  • Viral Proteins
  • Wiskott-Aldrich Syndrome Protein, Neuronal
  • Yaba monkey tumor virus
  • Journal Article
  • Research Support, Non-U.S. Gov't

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