ANALYSIS OF THE ANTIGENIC PROFILE OF MEASLES-VIRUS HEMAGGLUTININ IN MICE AND HUMANS USING OVERLAPPING SYNTHETIC PEPTIDES

In this study, a panel of 55 synthetic peptides representing 92.2% of the haemagglutinin (H) glycoprotein of measles virus (MV) were used to study the antigenic profile of the H molecule of anti-MV antibodies raised in mice and late convalescent human sera. In addition the immunogenicity of these peptides was tested in two mouse strains. Mouse anti-MV antibodies had different fine specificity of binding to the peptides depending on the mouse strain. Thus in BALB/c (H-2(d)) mice, anti-MV antibodies recognised six peptides representing residues 103-117; 123-237; 242-255; 293-307 and 463-477. In TO (H-2(S)) mice, anti-MV antibodies recognised peptides representing residues 49-72 and 463-477. When the immunogenicity of the peptides was tested, 29 were immunogenic in BALB/c mice and 34 were immunogenic fn TO mice. Several of the anti-peptide antisera were found to cross-react with MV, depending on the solid phase assay system used but none were able to inhibit virus infectivity in vitro. The reactivity of a panel of late convalescent human sera with the peptides was heterogeneous and the extent of the binding to the peptides was related to the titre of anti-MV. However, human sera recognized certain peptides more frequently than others, in particular peptides at the carboxyl-terminus.