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Analysis of the Respiratory Syncytial Virus Fusion Protein Using Monoclonal and Polyclonal Antibodies

¹ Department of Medicine, The Rochester General Hospital and the University of Rochester School of Medicine and Dentistry, Rochester, New York 14621
and² Division of Molecular Virology and Immunology, Department of Microbiology, Georgetown University Schools of Medicine and Dentistry, Rockville, Maryland 20852, U.S.A.

At least four distinct epitopes are described on the respiratory syncytial virus fusion protein (VP70) using 13 monoclonal antibodies in solid-phase competitive binding studies. Two, and possibly three, fusion-inhibiting epitopes, one non-fusion-inhibiting neutralizing epitope, and one non-neutralizing epitope are described. All but the latter site demonstrated partial overlap, suggesting possible topographical proximity of these epitopes. Polyclonal rabbit sera to VP70, which neutralized virus but did not inhibit fusion of infected cells, blocked the binding of all fusion-inhibiting monoclonal antibodies to VP70 in the solid-phase assay but did not inhibit their effect in vitro. Western blot analysis of these monoclonal antibodies demonstrates that one fusion-inhibiting epitope is localized on the 48K fragment of VP70 and is resistant to denaturation by heat, 2-mercaptoethanol and SDS.

Keywords: RSV, fusion protein, epitope map

Received 9 July 1985; accepted 12 November 1985.

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