Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: Evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites

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Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus has been performed. Distinct clusters of amino acid substitutions conferring resistance to neutralization at each of the four previously defined antigenic sites (McCahon et al., 1989, J. Gen. Virol. 70, 639-645) have been identified. One site corresponds to the well-known 140-160 region of VP1, a second site is also on VP1, one site is on VP2, and the fourth site is on VP3. All of the amino acid substitutions identified are located on the surface of the virus. Despite the differences in three-dimensional structure between FMDV and other picornaviruses the neutralizing antigenic sites occur in analogous positions on the capsid surface.

Original languageEnglish
JournalVirology
Volume179
Issue number1
Pages (from-to)26-34
Number of pages9
ISSN0042-6822
DOIs
Publication statusPublished - Nov 1990

Bibliographical note

Funding Information:
This work was supported in part by the European ~ornmuni~ Biotechnology Action Programme research contract (5AP 011 Q”UK~~). J.D.A.K. was supported by an AFRC research studentship. We slso thank John McCauley for providing oligonucleotide primers, Andrew M. Q. King and Chris Bostock for encouragement and critical reading of the manuscript, and Anne Boddy and Fiona Berrie for preparatian of the manuscript. We also gratefully acknowledge the provision of the FMDV ribbon diagrams by D. Stuart and colleagues, and permission to reproduce the diagram of the picornavirus capsid protein core by 1. Hogle and Science.

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