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Myristylation of picornavirus capsid protein VP4 and its structural significance

Nature volume 327, pages 482–486 (1987) Cite this article

Abstract

We have obtained evidence that poliovirus and other picornavirus particles are specifically modified by having myristic acid covalently bound to a capsid protein. The electron density map ofpoliovirus confirms the position of the myristate molecule and defines its location in the virus particle. Analogies with other myristylated proteins suggest that the myristate moiety in picornaviruses may be involved in capsid assembly or in the entry of virus into cells.

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Author notes

  1. F. Brown: To whom correspondence should be addressed.

Authors and Affiliations

  1. Department of Applied Biological Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    M. Chow

  2. Wellcome Biotechnology Ltd, Pirbright, Woking, Surrey, GU24 0NQ, UK

    J. F. E. Newman, D. J. Rowlands & F. Brown

  3. Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California, 92037, USA

    D. Filman & J. M. Hogle

  4. Department of Microbiology, Rhodes University, Grahamstown, 6140, South Africa

    J. F. E. Newman

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  1. M. Chow
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  2. J. F. E. Newman
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  3. D. Filman
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  4. J. M. Hogle
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  5. D. J. Rowlands
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Chow, M., Newman, J., Filman, D. et al. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature 327, 482–486 (1987). https://doi.org/10.1038/327482a0

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