Strain-specific interaction of a GII.10 Norovirus with HBGAs

Abstract Noroviruses (NoVs), an important cause of gastroenteritis in humans, recognize human histo-blood group antigens (HBGAs) as receptors. The crystal structures of the protruding (P) domain of a GII.10 NoV (Vietnam 026) in complex with various HBGA oligosaccharides were elucidated. However, the...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2015-02, Vol.476, p.386-394
Main Authors: Jin, Miao, Tan, Ming, Xia, Ming, Wei, Chao, Huang, Pengwei, Wang, Leyi, Zhong, Weiming, Duan, Zhaojun, Jiang, Xi
Format: Article
Language:English
Subjects:
Acute gastroenteritis
Amino Acid Sequence
Blood Group Antigens - genetics
Blood Group Antigens - metabolism
Caliciviridae Infections - metabolism
Caliciviridae Infections - virology
Gastroenteritis - metabolism
Gastroenteritis - virology
Human histo-blood group antigens
Humans
Infectious Disease
Models, Molecular
Molecular Sequence Data
Mutagenesis
Norovirus
Norovirus - genetics
Norovirus - metabolism
Noroviruses
Oligosaccharide
Protein Binding
Protein Structure, Tertiary
Receptors, Virus - genetics
Receptors, Virus - metabolism
Saliva
Species Specificity
Viral Nonstructural Proteins - genetics
Viral Nonstructural Proteins - metabolism
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Summary:Abstract Noroviruses (NoVs), an important cause of gastroenteritis in humans, recognize human histo-blood group antigens (HBGAs) as receptors. The crystal structures of the protruding (P) domain of a GII.10 NoV (Vietnam 026) in complex with various HBGA oligosaccharides were elucidated. However, the HBGA binding profile of this virus remains unknown. In this study, we determined the saliva and oligosaccharide binding profiles of this virus and the roles of amino acids that are involved in HBGA binding. Our data showed that Vietnam 026 bound to all ABO secretor and non-secretor saliva with clear signals detected by monoclonal antibodies against H3, H1, Ley , Lea and sialyl Lea . Mutagenesis study confirmed the binding site determined by the crystallography study, in which single mutations wiped out the binding function. We also identified amino acids surrounding the central binding pocket that may participate in the binding by affecting the HBGA binding specificity of the GII.10 NoV.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2014.12.039