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Neutralizing monoclonal antibodies raised against intact foot-and-mouth disease virus reacted with intact particles and with isolated VP1 from different strains from the same subtype. Prior treatment of the virus with either trypsin or with arginine-specific protease abolished recognition of both the virus and of VP1, suggesting the presence of a neutralization epitope in the central region of VP1 cleaved by these two enzymes. A synthetic peptide analogue of part of this region showed poor reactivity, however, with neutralizing antibody.
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