tailieunhanh - Báo cáo y học: " Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học 'Respiratory Research cung cấp cho các bạn kiến thức về ngành y đề tài: " Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D. | Respiratory Research BioMed Central Research Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D Kevan L Hartshorn 1 Richard Webby2 Mitchell R White1 Tesfaldet Tecle1 Clark Pan3 Susan Boucher3 Rodney J Moreland3 Erika C Crouch4 and Ronald K Scheule3 Open Access Address 1Boston University School of Medicine Department of Medicine Boston MA USA 2Department of Infectious Diseases St Jude Children s Research Hospital Memphis TN USA 3Genzyme Corporation Framingham MA USA and 4Department of Pathology and Immunology Washington University School of Medicine St. Louis MO USA Email Kevan L Hartshorn - khartsho@ Richard Webby - Mitchell R White - mwhite@ Tesfaldet Tecle - ttecle@ Clark Pan - Susan Boucher - Rodney J Moreland - Erika C Crouch - crouch@ Ronald K Scheule - Corresponding author Published 23 September 2008 Received 22 February 2008 Accepted 23 September 2008 Respiratory Research 2008 9 65 doi 1465-9921-9-65 r r This article is available from http content 9 1 65 2008 Hartshorn 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 Background Surfactant protein D SP-D plays an important role in innate defense against influenza A viruses IAVs and other pathogens. Methods We tested antiviral activities of recombinant human SP-D against a panel of IAV strains that vary in glycosylation sites on their hemagglutinin HA . For these experiments a recombinant version of human SP-D of the Met I I Ala 160 genotype was used after it was characterized biochemically and structurally. Results