Identification of a fifth neutralizable site on type O foot-and-mouth disease virus following characterization of single and quintuple monoclonal antibody escape mutants
| Autor: | S. Farias, J. R. Crowther, A. R. Samuel, W. C. Carpenter |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
medicine.drug_class
Guinea Pigs Molecular Sequence Data Mutant Enzyme-Linked Immunosorbent Assay Monoclonal antibody Virus Neutralization Epitope Viral Proteins Aphthovirus Neutralization Tests Virology medicine Animals Amino Acid Sequence Antigens Viral biology Antibodies Monoclonal biology.organism_classification Molecular biology Polyclonal antibodies Mutation biology.protein Cattle Rabbits Foot-and-mouth disease virus Conformational epitope |
| Zdroj: | Journal of General Virology. 74:1547-1553 |
| ISSN: | 1465-2099 0022-1317 |
| Popis: | A monoclonal antibody (C3) produced against foot-and-mouth disease virus type O1Caseros was found to neutralize quadrivalent monoclonal antibody escape mutant (G67) of foot-and-mouth disease virus type O1Kaufbeuren. This mutant had been characterized at the sequence level as having distinct changes affecting four non-overlapping neutralizable sites. The C3 monoclonal antibody was used to prepare a quintuple escape mutant from the G67 and a single escape mutant from the parental O1Kaufbeuren viruses. Polyclonal post-vaccinated and infected cattle sera as well as polyclonal mouse and guinea-pig sera, which neutralized the quadrivalent mutant, no longer neutralized the quintuple mutant, indicating that a fifth site had been identified and that changing the fifth site eliminated all neutralization. The site was characterized using serological techniques and found to be conformationally dependent, trypsin-sensitive and independent of sites previously characterized by monoclonal antibodies. Amino acid sequencing comparing parental, single C3 and quintuple mutants showed that a single change from a glutamine to a histidine, at amino acid 149 in the structural protein VP1, (1D) characterized the C3 mutation. The fifth site probably represents a conformational epitope which is formed due to the interaction of the VP1 loop region with other surface amino acids. |
| Databáze: | OpenAIRE |
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