Abstract
Six mouse monoclonal antibodies directed against respiratory syncytial virus proteins were produced. Each was characterized by immunoprecipitation and indirect immunofluorescence. One was directed against the nucleocapsid protein, NP 44, 2 were directed against a 37,000-dalton protein, 2 were directed against the major envelope glycoprotein, GP 90, and 1 was directed against the 70,000-dalton envelope protein, VP 70. Indirect immunofluorescence stain patterns of infected human laryngeal carcinoma HEp-2 cells defined GP 90 and VP 70 as viral proteins expressed on the cell surface. NP 44 and the 37,000-dalton protein were detected as intracytoplasmic inclusions. One of the anti-GP 90 antibodies neutralized virus only in the presence of complement but did not inhibit cell-cell fusion. The anti-VP 70 antibody neutralized virus without complement and inhibited cell-cell fusion of previously infected HEp-2 cell, thus identifying VP 70 as the fusion protein.