Oe. Obeid et al., ANALYSIS OF THE ANTIGENIC PROFILE OF MEASLES-VIRUS HEMAGGLUTININ IN MICE AND HUMANS USING OVERLAPPING SYNTHETIC PEPTIDES, Virus research, 32(1), 1994, pp. 69-84
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 r
aised in mice and late convalescent human sera. In addition the immuno
genicity of these peptides was tested in two mouse strains. Mouse anti
-MV antibodies had different fine specificity of binding to the peptid
es depending on the mouse strain. Thus in BALB/c (H-2(d)) mice, anti-M
V antibodies recognised six peptides representing residues 103-117; 12
3-237; 242-255; 293-307 and 463-477. In TO (H-2(S)) mice, anti-MV anti
bodies recognised peptides representing residues 49-72 and 463-477. Wh
en 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 infe
ctivity in vitro. The reactivity of a panel of late convalescent human
sera with the peptides was heterogeneous and the extent of the bindin
g to the peptides was related to the titre of anti-MV. However, human
sera recognized certain peptides more frequently than others, in parti
cular peptides at the carboxyl-terminus.