tetano
Editor, Senior Moderator
J Gen Virol. 2013 May 1. [Epub ahead of print]
Insight into structural diversity of influenza virus hemagglutinin.
Cho KJ, Lee JH, Hong KW, Kim SH, Park Y, Lee JY, Kang S, Kim S, Yang JH, Kim EK, Seok JH, Unzai S, Park SY, Saelens X, Kim CJ, Lee JY, Kang C, Oh HB, Chung MS, Kim KH.
Source
Korea University;
Abstract
Influenza virus infects host cells through membrane fusion, a process mediated by the low pH-induced conformational change of the viral surface glycoprotein hemagglutinin (HA). We determined the structures and biochemical properties of the HA proteins from A/Korea/01/2009 (KR01), a 2009 pandemic strain, and A/Thailand/CU44/2006 (CU44), a seasonal strain. The crystal structure of KR01 HA revealed a V-shaped head-to-head arrangement, which is not seen in other HA proteins including CU44 HA. We isolated a broadly neutralizing H1-specific monoclonal antibody GC0757. The KR01 HA-Fab0757 complex structure also exhibited a head-to-head arrangement of HA. Both native and Fab complex structures reveal different spatial orientation of HA1 relative to HA2, indicating that HA is flexible and dynamic at neutral pH. Further, the KR01 HA exhibited significantly lower protein stability and increased susceptibility to proteolytic cleavage compared with other HAs. Our structures provide important insight into conformational flexibility of HA.
PMID:
23636824
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23636824
Insight into structural diversity of influenza virus hemagglutinin.
Cho KJ, Lee JH, Hong KW, Kim SH, Park Y, Lee JY, Kang S, Kim S, Yang JH, Kim EK, Seok JH, Unzai S, Park SY, Saelens X, Kim CJ, Lee JY, Kang C, Oh HB, Chung MS, Kim KH.
Source
Korea University;
Abstract
Influenza virus infects host cells through membrane fusion, a process mediated by the low pH-induced conformational change of the viral surface glycoprotein hemagglutinin (HA). We determined the structures and biochemical properties of the HA proteins from A/Korea/01/2009 (KR01), a 2009 pandemic strain, and A/Thailand/CU44/2006 (CU44), a seasonal strain. The crystal structure of KR01 HA revealed a V-shaped head-to-head arrangement, which is not seen in other HA proteins including CU44 HA. We isolated a broadly neutralizing H1-specific monoclonal antibody GC0757. The KR01 HA-Fab0757 complex structure also exhibited a head-to-head arrangement of HA. Both native and Fab complex structures reveal different spatial orientation of HA1 relative to HA2, indicating that HA is flexible and dynamic at neutral pH. Further, the KR01 HA exhibited significantly lower protein stability and increased susceptibility to proteolytic cleavage compared with other HAs. Our structures provide important insight into conformational flexibility of HA.
PMID:
23636824
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23636824