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

Citation
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
Citations number
33
Categorie Soggetti
Virology
Journal title
ISSN journal
01681702
Volume
32
Issue
1
Year of publication
1994
Pages
69 - 84
Database
ISI
SICI code
0168-1702(1994)32:1<69:AOTAPO>2.0.ZU;2-L
Abstract
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.