Abstract
Serial "blind" passages in human rhabdomyosarcoma (RD) cells of prototype viruses from each of the six immunotypes of the group B coxsackieviruses (CB) resulted in the isolation of intratypic variants of CB1, CB3, CB5, and CB6. Each variant virus strain acquired the capacity to agglutinate human erythrocytes and produce small plaques on HeLa cells, although their serological specificity remained unchanged. An alteration in VP1 mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis was noted for CB3-RD. The CB3-RD variant was plaque purified on RD cells and studied for receptor interactions on both HeLa and RD cells. An attachment restriction appeared to exist for prototype CB3 on RD cells, whereas CB3-RD attached well to both cells. In attachment interference assays, HeLa cells saturated with CB3-RD blocked the attachment of CB3. In contrast, saturation of cells with CB1 (which shares a common receptor with parental CB3) failed to block the attachment of CB3-RD. This unidirectional receptor blockade suggested that a second site for the attachment of virions to receptors was acquired by the CB3-RD variant. Thus, more than one virus receptor specificity may be operative in the selection of host range virus mutants. The implications of this phenomenon as they may relate to pathogenesis are discussed.