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Structural basis for receptor specificity of influenza B virus hemagglutinin.

Authors
  • Wang, Qinghua1
  • Tian, Xia
  • Chen, Xiaorui
  • Ma, Jianpeng
  • 1 Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA. [email protected]
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
Oct 23, 2007
Volume
104
Issue
43
Pages
16874–16879
Identifiers
PMID: 17942670
Source
Medline
License
Unknown

Abstract

Receptor-binding specificity of HA, the major surface glycoprotein of influenza virus, primarily determines the host ranges that the virus can infect. Influenza type B virus almost exclusively infects humans and contributes to the annual "flu" sickness. Here we report the structures of influenza B virus HA in complex with human and avian receptor analogs, respectively. These structures provide a structural basis for the different receptor-binding properties of influenza A and B virus HA molecules and for the ability of influenza B virus HA to distinguish human and avian receptors. The structure of influenza B virus HA with avian receptor analog also reveals how mutations in the region of residues 194 to 196, which are frequently observed in egg-adapted and naturally occurring variants, directly affect the receptor binding of the resultant virus strains. Furthermore, these structures of influenza B virus HA are compared with known structures of influenza A virus HAs, which suggests the role of the residue at 222 as a key and likely a universal determinant for the different binding modes of human receptor analogs by different HA molecules.

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