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The Purification of Four Respiratory Syncytial Virus Proteins and Their Evaluation as Protective Agents against Experimental Infection in BALB/c Mice

E. G. Routledge^1,

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

The fusion (F) glycoprotein, large glyco- (G) protein, phospho- (P) protein and 22K protein of respiratory syncytial (RS) virus A2 strain were purified by a combination of immunoaffinity adsorption and preparative SDS-PAGE. All four proteins elicited serum antibody in mice after repeated inoculation in adjuvant, although the magnitude of the response as measured by ELISA varied from mouse to mouse. The F protein generated neutralizing antibodies in only 50% of the mice determined to be seropositive by ELISA. The G protein also induced neutralizing antibodies but in this instance neutralization tests and ELISA titres were more closely correlated. No neutralizing activity was detected in mice immunized with the P or 22K proteins although all produced antibody detectable by ELISA. Mice immunized with either the F or the G protein were found to be protected against subsequent RS virus challenge, whether they had developed neutralizing antibody or not. Mice inoculated with the P or 22K proteins were not protected.

Keywords: respiratory syncytial virus, proteins, RSV, purification

Present address: Institut für Virologie und Immunbiologie der Universität Würzburg, Versbacher Strasse 7, D-8700 Würzburg, F.R.G.

Received 3 June 1987; accepted 8 October 1987.

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