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

被引：10

作者：

Liu, Changbao ^{[1
]}

Day, Nicole D. ^{[1
]}

Branigan, Patrick J. ^{[1
]}

Gutshall, Lester L. ^{[1
]}

Sarisky, Robert T. ^{[1
]}

Del Vecchio, Alfred M. ^{[1
]}

机构：

[1] Centocor R&D Inc, Radnor, PA 19087 USA

来源：

VIROLOGY JOURNAL | 2007年 / 4卷 / 1期

关键词：

D O I：

10.1186/1743-422X-4-71

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页数：4

共 30 条

[21] Identification of the respiratory syncytial virus proteins required for formation and passage of helper-dependent infectious particles [J].