Structural basis for receptor specificity of influenza B virus hemagglutinin.

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.

authors

Wang Q,Tian X,Chen X,Ma J

doi

10.1073/pnas.0708363104

subject

Has Abstract

pub_date

2007-10-23 00:00:00

pages

16874-9

issue

43

eissn

0027-8424

issn

1091-6490

pii

0708363104

journal_volume

104

pub_type

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