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J Gen Virol 13 (1971), 73-84; DOI 10.1099/0022-1317-13-1-73
© 1971 Society for General Microbiology

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Further Evidence for Multiple Proteins in the Foot-and-Mouth Disease Virus Particle

J. N. Burroughs, D. J. Rowlands, D. V. Sangar, P. Talbot and F. Brown

Animal Virus Research Institute, Pirbright, Surrey

Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 x 103 were clearly demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on Amberlite IRC-50.

Received 8 March 1971; accepted 1 June 1971.


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L. C. Miller, W. Blakemore, D. Sheppard, A. Atakilit, A. M. Q. King, and T. Jackson
Role of the Cytoplasmic Domain of the {beta}-Subunit of Integrin {alpha}v{beta}6 in Infection by Foot-and-Mouth Disease Virus
J. Virol., May 1, 2001; 75(9): 4158 - 4164.
[Abstract] [Full Text]




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Copyright © 1971 by the Society for General Microbiology.