Rotavirus neutralizing protein VP7: antigenic determinants investigated by sequence analysis and peptide synthesis

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Abstract
The rotavirus neutralizing antigen, VP7, is a 37,000-MW glycoprotein which is a major component of the outer shell of the virion. The amino acid sequence of VP7 for strain S2 (human serotype 2) and Nebraska calf diarrhea virus (bovine serotype) was inferred from the nuclei acid sequence of cloned copies of genomic segment 9. Comparison of the amino acid sequences of these 2 VP7 proteins with those already determined for other rotavirus strains reveals extensive sequence conservation between serotypes with clusters of amino acid differences sited predominantly in hydrophilic domains of the protein. Six peptides were synthesized that span the hydrophilic regions of the molecule. Antisera to these peptides both recognize the respective homologous peptides in a solid-phase radioimmunoassay and bind to denatured VP7 in a Western blot. None of the antisera either recognize virus or exhibit significant neutralizing activity, indicating that these peptide sequences are not available on the surface of the virus.