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Divergent roles of ß- and γ-actin isoforms during spread of vaccinia virus.
Marzook, N Bishara; Latham, Sharissa L; Lynn, Helena; Mckenzie, Christopher; Chaponnier, Christine; Grau, Georges E; Newsome, Timothy P.
Afiliación
  • Marzook NB; School of Life and Environmental Sciences, The University of Sydney, Australia.
  • Latham SL; Vascular Immunology Unit, Department of Pathology, School of Medical Sciences & Marie Bashir Institute, The University of Sydney, Australia.
  • Lynn H; School of Life and Environmental Sciences, The University of Sydney, Australia.
  • Mckenzie C; School of Life and Environmental Sciences, The University of Sydney, Australia.
  • Chaponnier C; Department of Pathology-Immunology, Faculty of Medicine, University of Geneva, Switzerland.
  • Grau GE; Vascular Immunology Unit, Department of Pathology, School of Medical Sciences & Marie Bashir Institute, The University of Sydney, Australia.
  • Newsome TP; School of Life and Environmental Sciences, The University of Sydney, Australia.
Cytoskeleton (Hoboken) ; 74(4): 170-183, 2017 Apr.
Article en En | MEDLINE | ID: mdl-28218453
Actin is a major component of the cytoskeleton and is present as two isoforms in non-muscle cells: ß- and γ-cytoplasmic actin. These isoforms are strikingly conserved, differing by only four N-terminal amino acids. During spread from infected cells, vaccinia virus (VACV) particles induce localized actin nucleation that propel virus to surrounding cells and facilitate cell-to-cell spread of infection. Here we show that virus-tipped actin comets are composed of ß- and γ-actin. We employed isoform-specific siRNA knockdown to examine the role of the two isoforms in VACV-induced actin comets. Despite the high level of similarity between the actin isoforms, and their colocalization, VACV-induced actin nucleation was dependent exclusively on ß-actin. Knockdown of ß-actin led to a reduction in the release of virus from infected cells, a phenotype dependent on virus-induced Arp2/3 complex activity. We suggest that local concentrations of actin isoforms may regulate the activity of cellular actin nucleator complexes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Virus Vaccinia / Actinas / Isoformas de Proteínas Límite: Humans Idioma: En Revista: Cytoskeleton (Hoboken) Año: 2017 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Virus Vaccinia / Actinas / Isoformas de Proteínas Límite: Humans Idioma: En Revista: Cytoskeleton (Hoboken) Año: 2017 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Estados Unidos