Literature DB >> 2258927

Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment specific for an influenza virus haemagglutinin and of an escape mutant of that haemagglutinin.

T Bizebard1, Y Mauguen, F Petek, P Rigolet, J J Skehel, M Knossow.   

Abstract

Preliminary crystallographic data are given for two molecules involved in the interaction between the humoral immune response and the influenza virus. These molecules are the Fab fragment of an antibody specific for the haemagglutinin of influenza virus strain X31 (Hong Kong 1/68 (H3N2)) and a mutant of X31 haemagglutinin that escapes recognition by that antibody. Crystals of the haemagglutinin are isomorphous to those of X31, whose structure is known; they diffract to 3.4 A resolution. Crystals of the Fab fragment are trigonal with space group P3(1)21 (or P3(2)21) and diffract to 2.6 A resolution. The unit cell dimensions are a = b = 98.9 A, c = 89.2 A. A native data set has been collected for both proteins.

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Year:  1990        PMID: 2258927     DOI: 10.1016/0022-2836(90)90378-Y

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Identifying antigenicity-associated sites in highly pathogenic H5N1 influenza virus hemagglutinin by using sparse learning.

Authors:  Zhipeng Cai; Mariette F Ducatez; Jialiang Yang; Tong Zhang; Li-Ping Long; Adrianus C Boon; Richard J Webby; Xiu-Feng Wan
Journal:  J Mol Biol       Date:  2012-05-17       Impact factor: 5.469

Review 2.  Advances in antiviral vaccine development.

Authors:  Barney S Graham
Journal:  Immunol Rev       Date:  2013-09       Impact factor: 12.988

  2 in total

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