Crystal Structure of Unliganded Influenza B Virus Hemagglutinin

@article{citeulike:2428519, abstract = {Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 A. 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 amino acid substitutions on influenza B virus HAs have been identified 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, the 150 loop, the 160 loop, and the 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 the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins. 10.1128/JVI.02477-07}, author = {Wang, Qinghua and Cheng, Feng and Lu, Mingyang and Tian, Xia and Ma, Jianpeng }, citeulike-article-id = {2428519}, doi = {http://dx.doi.org/10.1128/JVI.02477-07}, journal = {J. Virol.}, keywords = {influenza, structure, virus}, month = {March}, number = {6}, pages = {3011--3020}, posted-at = {2008-02-26 06:16:03}, priority = {3}, title = {Crystal Structure of Unliganded Influenza B Virus Hemagglutinin}, url = {http://dx.doi.org/10.1128/JVI.02477-07}, volume = {82}, year = {2008} }

TY - JOUR ID - citeulike:2428519 L3 - citeulike-article-id:2428519 TI - Crystal Structure of Unliganded Influenza B Virus Hemagglutinin JF - J. Virol. VL - 82 IS - 6 SP - 3011 EP - 3020 N2 - Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 A. 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 amino acid substitutions on influenza B virus HAs have been identified 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, the 150 loop, the 160 loop, and the 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 the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins. 10.1128/JVI.02477-07 KW - influenza KW - structure KW - virus AU - Wang, Qinghua AU - Cheng, Feng AU - Lu, Mingyang AU - Tian, Xia AU - Ma, Jianpeng PY - 2008/03/15/ UR - http://dx.doi.org/10.1128/JVI.02477-07 ER -