1. Analysis of the antigenic profile of measles virus haemagglutinin in mice and humans using overlapping synthetic peptides
- Author
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Michael W. Steward, Obeid E. Obeid, and Charalambos D. Partidos
- Subjects
Cancer Research ,Antigenicity ,Paramyxoviridae ,T-Lymphocytes ,Molecular Sequence Data ,Hemagglutinins, Viral ,Mice, Inbred Strains ,Antibodies, Viral ,Epitope ,Measles virus ,Epitopes ,Mice ,Antigen ,Antibody Specificity ,Virology ,Animals ,Humans ,Amino Acid Sequence ,Antigens, Viral ,Antiserum ,B-Lymphocytes ,Mice, Inbred BALB C ,biology ,Immunogenicity ,Convalescence ,Hemagglutinin ,biology.organism_classification ,Peptide Fragments ,Infectious Diseases ,Measles - 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 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; 123–137; 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 in 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.
- Published
- 1994
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