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Extensive antigenic diversification of foot-and-mouth disease virus by amino acid substitutions outside the major antigenic site

M. E. Piccone^1,

¹ Instituto de Biología Molecular, Centro de Investigación en Ciencias Veterinarias, INTA, cc77, 1708 Moron, Buenos Aires, Argentina,
² Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain
and³ Istituto Zooprofilattico Sperimentale della Lombardia e dell'Emilia, 25125 Brescia, Italy

The antigenic sites A and C (the G-H loop and the C terminus, respectively) in VP1 of foot-and-mouth disease virus (FMDV) have been considered the immunodominant regions of the virus involved in the induction of protection. Other antigenic sites have been described but their involvement in protection has not been established. Here we report that two closely related but serologically different FMDVs (the field isolate C₃ Argentina/84 and the vaccine strain C₃ Resende Br/55) have identical A and C sites but differ at other antigenic sites. Such differences have been documented by reactivity with a panel of 28 monoclonal antibodies (MAbs). The two viruses reacted to the same extent with each of 13 MAbs which recognized epitopes within sites A or C, but reacted differently with six out of 15 MAbs that recognized other sites. Accordingly, sequencing of the entire region coding for the capsid proteins, for both viruses, revealed four amino acid substitutions at three antigenic sites other than A and C. The results suggest that identity of sites A and C may not be sufficient to induce cross-protection, and provide the first evidence of significant antigenic diversification of FMDV in the field mediated by amino acid substitutions outside sites A or C.

Present address: Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029, U.S.A.

Received 8 April 1992; accepted 26 August 1992.

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