The C-Terminal Repeat Domains of nsP3 from the Old World Alphaviruses Bind Directly to G3BP

  1. Gerald M. McInerneya
  1. aDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden
  2. bDepartment of Food and Environmental Sciences, University of Helsinki, Helsinki, Finland
  1. M. S. Diamond, Editor

ABSTRACT

The Old World alphaviruses block stress granule assembly by sequestration of RasGAP SH3-domain binding protein (G3BP). Here, we show that the proline-rich sequences in the hypervariable domain of nonstructural protein 3 (nsP3) of both Semliki Forest virus and Chikungunya virus were dispensable for binding to G3BP. nsP3 variants with or without this domain colocalized with G3BP. Furthermore, we show that the C-terminal repeat motifs of nsP3 were sufficient for G3BP binding.

FOOTNOTES

    • Received 14 February 2014.
    • Accepted 3 March 2014.
  • Address correspondence to Gerald M. McInerney, gerald.mcinerney{at}ki.se.

  • Published ahead of print 12 March 2014

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  1. Accepted manuscript posted online 12 March 2014, doi: 10.1128/JVI.00439-14 J. Virol. vol. 88 no. 10 5888-5893
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