Literature DB >> 8539243

Crystallization and preliminary X-ray diffraction studies of complexes between an influenza hemagglutinin and Fab fragments of two different monoclonal antibodies.

B Gigant1, D Fleury, T Bizebard, J J Skehel, M Knossow.   

Abstract

Fab fragments from two different monoclonal antibodies (BH151 and HC45) which bind to the same antigenic region of the influenza hemagglutinin were crystallized as complexes with the hemagglutinin. The complexes crystallize in PEG 600, pH 6.0, and PEG 2000, pH 8.5, respectively. Both crystals belong to space group P321, with very similar unit cell dimensions.

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Year:  1995        PMID： 8539243     DOI： 10.1002/prot.340230113

Source DB:  PubMed          Journal:  Proteins        ISSN： 0887-3585


  3 in total

1.  Genetic diversity of hemagglutinin gene of A(H1N1)pdm09 influenza strains isolated in Taiwan and its potential impact on HA-neutralizing epitope interaction.

Authors:  Krzysztof Łepek; Beata Pająk; Paweł Siedlecki; Marcin Niemcewicz; Janusz Kocik; Ho-Sheng Wu; Ji-Rong Yang; Krzysztof Kucharczyk; Bogusław Szewczyk
Journal:  Hum Vaccin Immunother       Date:  2014-01-09       Impact factor: 3.452

2.  Crystal structure of unliganded influenza B virus hemagglutinin.

Authors:  Qinghua Wang; Feng Cheng; Mingyang Lu; Xia Tian; Jianpeng Ma
Journal:  J Virol       Date:  2008-01-09       Impact factor: 5.103

3.  The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency.

Authors:  Simon E Hufton; Paul Risley; Christina R Ball; Diane Major; Othmar G Engelhardt; Stephen Poole
Journal:  PLoS One       Date:  2014-08-01       Impact factor: 3.240
  3 in total

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