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Implications for viral uncoating from the structure of bovine enterovirus

Nature Structural Biology volume 2, pages 224–231 (1995)Cite this article

Abstract

We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall architecture of the virion are similar to those of related picornaviruses. The external loops joining β-strands are truncated and the canyon region is partially filled by an extension of the VP3 G–H loop giving the viral capsid a relatively smooth appearance. These changes may have implications for cell attachment. In spite of these differences the virus maintains a hydrophobic pocket within VP1, occupied by a specific ‘pocket factor’ which appears to be myristic acid. These observations support the proposal that a kinetic equilibrium exists between occupied and unoccupied pocket states, with occupation inhibiting uncoating.

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Authors and Affiliations

  1. The Laboratory of Molecular Biophysics, Rex Richards Building, South Parks Road, Oxford, OX1 3QU, UK

    Michael Smyth, John Tate & David Stuart

  2. The School of Biology and Biochemistry, Queens University, Medical Biology Centre, Lisburn Road, Belfast, BT9 7BL, UK

    Elizabeth Hoey, Carol Lyons & Sam Martin

  3. The Oxford Centre for Molecular Sciences, New Chemistry Building, South Parks Road, Oxford, OX1 3QT, UK

    David Stuart

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Smyth, M., Tate, J., Hoey, E. et al. Implications for viral uncoating from the structure of bovine enterovirus. Nat Struct Mol Biol 2, 224–231 (1995). https://doi.org/10.1038/nsb0395-224

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