國家衛生研究院 NHRI:Item 3990099045/3560
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    题名: Immunological study of HA1 domain of hemagglutinin of influenza H5N1 virus
    作者: Chiu, FF;Venkatesan, N;Wu, CR;Chou, AH;Chen, HW;Lian, SP;Liu, SJ;Huang, CC;Lian, WC;Chong, P;Leng, CH
    贡献者: Vaccine Research and Development Center
    摘要: The neutralization titer of a hemagglutinin (HA)-specific neutralizing antibody against new isolates reflect both the antigenic drift and the conformation status of HA protein in these new influenza viruses. Since most antigenic sites are in the HA1 domain of HA, using HA1 domain of influenza virus as antigen is of great importance in vaccine development. In this study, we investigate different purification processes for optimizing the immunological properties of an Escherichia coli-expressed HA1 domain (rH5HA1) of influenza H5N1 virus. rH5HA1 was expressed as inclusion bodies and extracted with 6 M guanidine hydrochloride (GnHCl)/PBS buffer. The best condition for generating HA1-specific neutralization determinants is on-column oxidative refolding procedures with GSH/GSSG and l-arginine buffer. Others refolding procedures such as using high-pH buffer and/or different detergent solubilizations were found to be ineffective producing neutralization epitope recognized by a HA1-specific neutralizing monoclonal antibody that was raised against H5N1 virus.
    日期: 2009-05-22
    關聯: Biochemical and Biophysical Research Communications. 2009 May 22;383(1):27-31.
    Link to: http://dx.doi.org/10.1016/j.bbrc.2009.03.106
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0006-291X&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000265768800006
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=64949197099
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