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J Gen Virol 73 (1992), 621-626; DOI 10.1099/0022-1317-73-3-621
© 1992 Society for General Microbiology

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The nucleotide sequences of wild-type coxsackievirus A9 strains imply that an RGD motif in VP1 is functionally significant

Ki Ha Chang1, Carol Day2, Jackie Walker2, Timo Hyypiä3 and Glyn Stanway1

1 Department of Biology, University of Essex, Colchester CO4 3SQ
2 National Enterovirus Reference Laboratory, Epsom, Surrey KT19 8PB, U.K.
and3 Department of Virology, University of Turku, SF-20520 Turku, Finland

We have shown previously that, compared to other enteroviruses, the coxsackievirus A9 (CAV-9) prototype strain, Griggs, contains a C-terminal extension to the capsid protein VP1 and that within this extension there is an RGD (arginine-glycine-aspartic acid) motif. To determine whether these features are found in other CAV-9 strains and therefore analyse whether they are likely to be functionally important, we have determined the nucleotide sequence of the appropriate region from five strains, isolated over a 25 year period. The results indicate that there is considerable diversity between the strains and there is little correlation between nucleotide sequence identity and date of isolation. All isolates exhibit the VP1 extension and although its amino acid sequence is otherwise variable, the RGD motif is common to all. This conservation of sequence, within a region which can otherwise vary, implies that the RGD sequence must be functionally significant. The VP1 extension shows similarity to sequences found in foot-and-mouth-disease virus strains and to part of the precursor of the cellular protein, human transforming growth factor beta, and the possible significance of these observations is discussed.

Received 29 July 1991; accepted 14 November 1991.


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