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How a rotavirus hijacks the human protein synthesis machinery

Nature Structural Biology volume 9, pages 158–160 (2002)Cite this article

The NSP3 protein from rotaviruses recognizes a unique sequence at the 3′ end of the rotaviral mRNA. By doing so, it promotes translation of viral proteins while repressing host protein synthesis. The structure of the NSP3 protein bound to a viral 3′ end sequence reveals how this occurs and suggests how it might be possible to design a new class of antiviral drugs.

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Figure 1: The 5′ and 3′ ends of viral and eukaryotic mRNA synergistically stimulate initiation of protein synthesis.
Figure 2: NSP3 homodimer binds the viral mRNA 3′ ends and buries these nucleotides within a deep tunnel.

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Authors and Affiliations

  1. the Departments of Chemistry and Biochemistry, University of Washington, Seattle, 98102-1700, Washington, USA

    Gabriele Varani

  2. Department of Biology, ETH Zurich, Institut fur Molekularbiologie und Biophysik, ETH Honggerberg, HPK, Zurich, CH-8093, Switzerland

    Frédéric H.-T. Allain

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  1. Gabriele Varani
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  2. Frédéric H.-T. Allain
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Correspondence to Gabriele Varani or Frédéric H.-T. Allain.

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Varani, G., Allain, FT. How a rotavirus hijacks the human protein synthesis machinery. Nat Struct Mol Biol 9, 158–160 (2002). https://doi.org/10.1038/nsb0302-158

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