Identification of conformational neutralization sites on the fusion protein of mumps virus
| Autor: | Claes Örvell, Tanja Košutić Gulija, Maja Šantak |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Glycosylation
Molecular Sequence Data Mumps Vaccine Mumps virus Biology Antibodies Viral medicine.disease_cause Neutralization Epitope mumps virus epitopes fusion protein neutralization Antigen Virology medicine Animals Humans Treatment Failure Mice Inbred BALB C Antibodies Monoclonal Sequence Analysis DNA Antibodies Neutralizing Fusion protein Vaccination Mumps vaccine Immunology biology.protein Epitopes B-Lymphocyte Antibody Viral Fusion Proteins |
| Zdroj: | Journal of General Virology. 96:982-990 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/vir.0.000059 |
| Popis: | In spite of the success of the mumps vaccination, recent mumps outbreaks have been reported even among individuals with a history of mumps vaccination. For a better understanding of why the vaccination failed in cases of vaccinees who fell ill during recent mumps outbreaks, the immunological events during infection and/or vaccination should be better defined. In the work presented here we sought to identify new neutralization sites on the mumps virus surface glycoproteins. By using anti-mumps mAbs, three amino acid positions at residues 221, 323 and 373 in the F protein of mumps virus were shown to be located in at least two conformational neutralization epitopes. mAbs that specifically target these sites effectively neutralized mumps virus in vitro. The newly acquired glycosylation site at position 373 or loss of the existing one at position 323 was identified as the mechanism behind the escape from the specific mAbs. Based on the findings of this study, we suggest that the influence of the antigenic structure of the F protein should not be ignored in a thorough investigation of the underlying mechanism of the mumps vaccine failure or when making a strategy for development of a new vaccine. |
| Databáze: | OpenAIRE |
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