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Department of Medicine, The Rochester General Hospital and the University of Rochester School of Medicine and Dentistry, Rochester, New York 14621, U.S.A.
The fusion protein of respiratory syncytial virus was purified by affinity chromatography using a monoclonal antibody. Under various conditions the protein was recovered as a 145K dimer or a 70K monomer. The 70K monomer was composed of disulphide-linked fragments of 48K and 23K. Polyclonal rabbit serum produced to the dimerized fusion protein neutralized virus but did not inhibit fusion, while rabbit serum to the 2-mercaptoethanol-treated dimerized protein neutralized virus and inhibited fusion of infected cells. Only the latter serum strongly recognized the 23K fragment when studied by Western blot analysis.
Keywords: RSV, fusion protein, characterization
Received 26 July 1984;
accepted 31 October 1984.
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