tailieunhanh - Báo cáo hóa học: " Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library"

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: Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library | Virology Journal BioMed Central Research Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library Angeline PC Lim Conrad EZ Chan Steven KK Wong Annie HY Chan Eng Eong Ooi and Brendon J Hanson Address Defence Medical and Environmental Research Institute DSO National Laboratories 27 Medical Dr 117510 Singapore Email Angeline PC Lim - lpeichie@ Conrad EZ Chan - cenzuo@ Steven KK Wong - wkakhuen@ Annie HY Chan - choiyi@ Eng Eong Ooi - oengeong@ Brendon J Hanson - hbrendon@ Corresponding author Open Access Published 28 October 2008 Received 29 May 2008 Accepted 28 October 2008 Virology Journal 2008 5 130 doi 1743-422X-5-130 This article is available from http content 5 1 130 2008 Lim 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_ Identification of neutralizing antibodies with specificity away from the traditional mutation prone antigenic regions against the conserved regions of hemagglutinin from H5NI influenza virus has the potential to provide a therapeutic option which can be developed ahead of time in preparation for a possible pandemic due to H5N1 viruses. In this study we used a combination of panning strategies against the hemagglutinin HA of several antigenic distinct H5N1 isolates to bias selection of Fab-phage from a naive human library away from the antigenic regions of HA toward the more conserved portions of the protein. All of the identified Fab clones which showed binding to multiple antigenically distinct HA were converted to fully human IgG and tested for their ability to neutralize