JVI Accepts, published online ahead of print on 9 January 2008

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J. Virol. doi:10.1128/JVI.02477-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Crystal Structure of Unliganded Influenza B Virus Hemagglutinin

Qinghua Wang^*, Feng Cheng, Mingyang Lu, Xia Tian, and Jianpeng Ma

Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, BCM-125, Houston, TX 77030; Department of Structural Biology and Computational Biology, University of Virginia, Charlottesville, VA 22908; Department of Bioengineering, Rice University, 6100 Main Street, Houston, TX 77005

^* To whom correspondence should be addressed. Email: qinghuaw{at}bcm.tmc.edu.

Here we report the crystal structure of hemagglutinin (HA) from influenza B/HK/8/73 virus determined to 2.8 Å. At a sequence identity of 25% to influenza A virus HAs, B/HK HA shares a similar overall structure and domain organization. More than two dozen of amino acid substitutions have been identified on influenza B virus HAs to cause antigenicity alteration in site-specific mutants, monoclonal antibody-escape mutants or field isolates. Mapping these substitutions on the structure of B/HK HA reveals four major epitopes, the 120-loop, 150-loop, 160-loop and 190-helix, that are located close in space to form a large, continuous antigenic site. Moreover, a systematic comparison of known HA structures across the entire influenza virus family reveals evolutionarily conserved ionizable residues at all regions along chain and subunit interface. These ionizable residues are likely the structural basis for the pH-dependence and sensitivity to ionic strength of influenza HA and HEF proteins.

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