tailieunhanh - Báo cáo sinh học: " Relationship between the loss of neutralizing antibody binding and fusion activity of the F protein of human respiratory syncytial virus"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Relationship between the loss of neutralizing antibody binding and fusion activity of the F protein of human respiratory syncytial virus | Virology Journal BioMed Central Short report Open Access Relationship between the loss of neutralizing antibody binding and fusion activity of the F protein of human respiratory syncytial virus Changbao Liu Nicole D Day Patrick J Branigan Lester L Gutshall RobertT Sarisky and Alfred M Del Vecchio Address Centocor R D Inc. 145 King of Prussia Road Radnor Pennsylvania 19087 USA Email Changbao Liu - Cliu12@ Nicole D Day - NDay2@ Patrick J Branigan - Pbraniga@ Lester L Gutshall - LGutshal@ Robert T Sarisky - RSarisky@ Alfred M Del Vecchio - Adelvecc@ Corresponding author Published 10 July 2007 Received 6 June 2007 Accepted 10 July 2007 Virology Journal 2007 4 71 doi l 743-422X-4-71 This article is available from http content 4 1 71 2007 Liu et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. 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 .

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