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Relationship between the loss of neutralizing antibody binding and fusion activity of the F protein of human respiratory syncytial virus

Changbao Liu email, Nicole D Day email, Patrick J Branigan email, Lester L Gutshall email, Robert T Sarisky email and Alfred M Del Vecchio email

Centocor R&D, Inc., 145 King of Prussia Road, Radnor, Pennsylvania, 19087, USA

author email corresponding author email

Virology Journal 2007, 4:71doi:10.1186/1743-422X-4-71

Published: 10 July 2007

Abstract

To elucidate the relationship between resistance to HRSV neutralizing antibodies directed against the F protein and the fusion activity of the F protein, a recombinant approach was used to generate a panel of mutations in the major antigenic sites of the F protein. These mutant proteins were assayed for neutralizing mAb binding (ch101F, palivizumab, and MAb19), level of expression, post-translational processing, cell surface expression, and fusion activity. Functional analysis of the fusion activity of the panel of mutations revealed that the fusion activity of the F protein is tolerant to multiple changes in the site II and IV/V/VI region in contrast with the somewhat limited spectrum of changes in the F protein identified from the isolation of HRSV neutralizing antibody virus escape mutants. This finding suggests that aspects other than fusion activity may limit the spectrum of changes tolerated within the F protein that are selected for by neutralizing antibodies.


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