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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

Lookup NU author(s): Dr Edward Routledge, Dr Tony Samson, Dr Ronald Scott, Dr John Anderson, Emeritus Professor Geoffrey Toms

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Abstract

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.

Publication metadata

Author(s): Routledge EG, Willcocks MM, Samson ACR, Morgan L, Scott R, Anderson JJ, Toms GL

Publication type: Article

Publication status: Published

Journal: Journal of General Virology

Year: 1988

Volume: 69

Issue: part 2

Pages: 293-303

Print publication date: 01/02/1988

ISSN (print): 0022-1317

ISSN (electronic): 1465-2099

URL: http://dx.doi.org/10.1099/0022-1317-69-2-293

DOI: 10.1099/0022-1317-69-2-293

PubMed id: 3339327

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