Biochemical Aspects of Variation in Foot-and-Mouth Disease Virus

Animal Virus Research Institute, Pirbright, Woking, Surrey, U.K. The biochemical basis for variation in foot-and-mouth disease virus (FMDV) has been explored by analysis of the virus RNA and the virus-induced and structural proteins of three isolates of the virus. Two of the isolates were from serot...

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Bibliographic Details
Published in:Journal of general virology 1980-01, Vol.46 (1), p.179-193
Main Authors: Robson, Kathryn J. H, Doel, T. R, Gorman, B. M, Brown, F
Format: Article
Language:English
Subjects:
Aphthovirus - analysis
Aphthovirus - classification
Capsid - analysis
Electrophoresis, Polyacrylamide Gel
Nucleic Acid Hybridization
Peptides - analysis
RNA, Viral - analysis
Serotyping
Trypsin - pharmacology
Viral Proteins - analysis
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Summary:Animal Virus Research Institute, Pirbright, Woking, Surrey, U.K. The biochemical basis for variation in foot-and-mouth disease virus (FMDV) has been explored by analysis of the virus RNA and the virus-induced and structural proteins of three isolates of the virus. Two of the isolates were from serotype A and the third was from serotype O. Hybridization studies of the RNAs showed greater than 80% homology between the two type A viruses and about 65% homology between the two type A viruses and the virus of type O. The ribonuclease T 1 maps of the three viruses gave distinct patterns typical of FMDV, but did not show that any two of the three viruses were more closely related. The virus-induced primary translation products, P88, P52 and P100 isolated from infected cells, were compared by tryptic peptide analysis. Combinations of 3 H- and 14 C-leucine-labelled polypeptides were hydrolysed with trypsin and resolved on an ion-exchange column. Much greater differences were found in P88 than in P52 or P100, indicating that the major variation occurs in the region of the genome coding for the structural proteins. Similar analysis of combinations of the structural proteins of the three viruses showed that there were differences in VP1, VP2 and VP3 and these results were supported by those obtained by PAGE analysis of the Staphylococcus aureus V8 protease cleavage products. * On leave of absence from the Queensland Institute of Medical Research, Brisbane, Australia. Received 22 June 1979; accepted 28 August 1979.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-46-1-179