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A Neutralizing Monoclonal Antibody to Respiratory Syncytial Virus which Binds to Both F₁ and F₂ Components of the Fusion Protein

¹ Department of Genetics, University of Newcastle upon Tyne, Newcastle upon Tyne, NE1 7RU, U.K.
and² Department of Virology, University of Newcastle upon Tyne, Newcastle upon Tyne, NE1 7RU, U.K.

A virus-neutralizing monoclonal antibody (1E3) specifically immunoprecipitated the 70000 mol. wt. (70K) fusion (F) protein from respiratory syncytial (RS) virus-infected HeLa cells. Western blotting analysis of polypeptides from such cells separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions revealed that 1E3 was peculiar in that it bound to both F₁ (50K) and F₂ (20K) components of the F protein. Antibody subsequently eluted from either the F₁ or the F₂ regions of immunoblots re-bound to both F₁ and F₂ regions of the SDS-PAGE blot. These results show that monoclonal antibody 1E3 reacts with an epitope which is found on both F₁ and F₂ subunits of RS virus fusion protein.

Keywords: RS virus, fusion protein, monoclonal antibody

Received 7 March 1986; accepted 7 April 1986.

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