Abstract
Summary Monoclonal antibodies were used to study the antigenic organization of the major inner capsid protein (VP6) of rotaviruses. This was etablished by a competitive binding assay and by determining the reactivity pattern of 8 monoclonal antibodies on 59 rotavirus specimens tested. We found that VP6 possesses at least five epitopes organized in four non-overlapping antigenic domains. Three epitopes located on three non-overlapping antigenic sites were common to all rotaviruses tested, whereas antigenic variation was observed for the two other epitopes. The significance of such variability could be explained by unclassified epitopes with random variations or a third (or even more) subgroup specificity.
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