Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling

Friedrich Frischknecht, Violaine Moreau, Sabine Röttger, Stefania Gonfloni, Inge Reckmann, Giulio Superti-Furga and Michael Way ()
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Friedrich Frischknecht: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory
Violaine Moreau: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory
Sabine Röttger: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory
Stefania Gonfloni: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory
Inge Reckmann: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory
Giulio Superti-Furga: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory
Michael Way: Cell and Developmental Biology Programmes, European Molecular Biology Laboratory

Nature, 1999, vol. 401, issue 6756, 926-929

Abstract: Abstract Studies of the actin-based motility of the intracellular pathogens Listeria monocytogenes and Shigella flexneri have provided important insight into the events occurring at the leading edges of motile cells1,2,3,4,5. Like the bacteria Listeria and Shigella, vaccinia virus, a relative of the causative agent of smallpox, uses actin-based motility to spread between cells6. In contrast to Listeria or Shigella, the actin-based motility of vaccinia is dependent on an unknown phosphotyrosine protein, but the underlying mechanism remains obscure7. Here we show that phosphorylation of tyrosine 112 in the viral protein A36R by Src-family kinases is essential for the actin-based motility of vaccinia. Tyrosine phosphorylation of A36R results in a direct interaction with the adaptor protein Nck8 and the recruitment of the Ena/VASP family member N-WASP9 to the site of actin assembly. We also show that Nck and N-WASP are essential for the actin-based motility of vaccinia virus. We suggest that vaccinia virus spreads by mimicking the signalling pathways that are normally involved in actin polymerization at the plasma membrane.

Date: 1999
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DOI: 10.1038/44860

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