Three epitopes which react with haemagglutination inhibition and neutralizing antibodies have been located between amino acids 245-285 in the predicted amino acid sequence of rubella envelope glycoprotein E1.

Tween-ether treatment of rubella virus, which has no effect on the antigenic and electrophoretic properties of the two envelope glycoproteins, destroys infectivity and enhances haemagglutinating activity. Trypsin treatment alters the electrophoretic pattern of the envelope glycoproteins so that the VPI peak is no longer evident and the VPII peak is reduced. At the same time, both the properties of haemagglutination and infectivity are inactivated but the capacity to combine with neutralizing antibody is retained, which suggests that VPII may be responsible for inducing the production of neutralizing antibody.

Three epitopes have been identified on rubella virion envelope polypeptide E 1 using monoclonal antibodies. Antibodies to two of the epitopes, E 1EP1 and E 1EP2, show both haemagglutination inhibition and neutralization activities whereas antibodies to the remaining epitope, E 1EP3, show neutralizing activity only.

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Four polypeptides with molecular weights of 55 K, 47 K, 45 K, and 33 K have been resolved by polyacrylamide gel electrophoresis of immune precipitated rubella virus. The 47 K and 45 K components have similar peptide maps but different isoelectric points so that the same polypeptide may exist in more than one charged form. The 55 K and 45 K components have similar isoelectric points but different peptide maps showing that similarity of isoelectric point is not evidence of identity.