RESUMO
Epitope specificity and protective activity of 5 types of monoclonal antibodies (MAB) to strain TM-14 of Venezuelan equine encephalomyelitis (VEE) virus were studied. The competing VEE A4 and VEE B5 MAB were shown to recognize the conformation-dependent epitope of glycoprotein E2 third site and to possess an extremely high protective activity. VEE C6 MAB were active in all the studied biological tests (hemagglutination inhibition, neutralization tests, passive defence) and were directed to glycoprotein E2 site six. Competitive radioimmunoassay demonstrated that VEE A5 MAB also interacted with E2-6 site and by the sum of characteristics detected a new epitope of this site. VEE G1 MAB specific to glycoprotein E1 were characterized by protective, but not neutralizing activity, and competed with MAB to sites E2-2 and E2-6. This means that VEE G1 MAB detect a heretofore not described epitope E1 overlapping with two E2 sites.
Assuntos
Anticorpos Monoclonais/uso terapêutico , Encefalomielite Equina Venezuelana/prevenção & controle , Epitopos/imunologia , Animais , Anticorpos Monoclonais/imunologia , Vírus da Encefalite Equina Venezuelana/imunologia , Testes de Hemaglutinação , Camundongos , Testes de Neutralização , Radioimunoensaio , Proteínas do Envelope Viral/imunologiaRESUMO
Five strains of hybrid cells producing highly active monoclonal antibodies (MCA) to Venezuelan equine encephalomyelitis (VEE) virus were generated. VEEC6 MCA had high virus-neutralizing and hemagglutinating activities attesting to their direction to the "critical" site of E2 glycoprotein. MCA VEEA5 directed to the same glycoprotein did not overlap spatially with the previous one. MCA VEEB5 and VEEA4 interacted with conformational virus determinants taking part in hemagglutination.