Interaction of cellular proteins with the poliovirus 5′ noncoding region (original) (raw)

Summary

The 5′ noncoding region (NCR) of poliovirus RNA is folded into a complex structure comprised of multiple, critically spaced, stem-loop domains. Mutations in at least one of these domains markedly affects the neurovirulence of the virus. Two proteins have been identified recently which bind and apparently mediate functions of the 5′ NCR in translation. We have demonstrated specific binding of three additional proteins in a Hela cell ribosomal salt wash that can be crosslinked to specific stem-loop segments of the 5′ NCR. These same RNA segments inhibit translation of polio RNA in vitro, presumably by competing for protein binding. The Sabin vaccine strain of polio RNA exhibits a reduced affinity of binding for specific proteins. The determinant for this reduction appears to be a single nucleotide difference at position 480 between the neuro virulent and attenuated viral strains.

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, University of California, 3205 Bio Sci II, Irvine, CA, 92717, USA
    Dr. E. Ehrenfeld
  2. Department of Cellular Viral and Molecular Biology, University of Utah School of Medicine, Utah, USA
    J. G. Gebhard

Authors

  1. Dr. E. Ehrenfeld
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  2. J. G. Gebhard
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Editors and Affiliations

  1. Department of Biology, Georgia State University, Atlanta, Georgia, USA
    Margo A. Brinton
  2. Arthropod-borne and Infectious Disease Laboratory (AIDL), Colorado State University, Fort Collins, Colorado, USA
    Charles H. Calisher
  3. Institute for Molecular Virology, University of Wisconsin, Madison, Wisconsin, USA
    Roland Rueckert

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© 1994 Springer-Verlag

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Ehrenfeld, E., Gebhard, J.G. (1994). Interaction of cellular proteins with the poliovirus 5′ noncoding region. In: Brinton, M.A., Calisher, C.H., Rueckert, R. (eds) Positive-Strand RNA Viruses. Archives of Virology Supplementum, vol 9. Springer, Vienna. https://doi.org/10.1007/978-3-7091-9326-6\_27

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