The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
Identifieur interne : 000931 ( Main/Exploration ); précédent : 000930; suivant : 000932The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
Auteurs : Tony Velkov [Australie, États-Unis]Source :
- Journal of Molecular Recognition [ 0952-3499 ] ; 2013-10.
English descriptors
- Teeft :
- Accession, Adaption, Amino, Analog, Asialyl, Asialyl sugars, Assay, Assay ganglioside, Avian, Avian receptor analog lsta, Avian receptor analogs, Binding data, Binding pocket, Carbone, Consensus model, Copyright, Crystal structure, Determinant, Elisa, Gambaryan, Ganagliosides, Ganglioside, Gangliosides, Genbank, Genbank accession, Glycan, Glycans, Glycosidic linkage, Glycosylation, Glycosylation site, Govorkova, Hemagglutinin, Hemagglutinin receptors, Hydrogen bonds, John wiley sons, Krystal, Lsta, Lstc, Lugovtsev, Matrosovich, Mdck, Mutation, Receptor, Receptor binding, Receptor binding characteristics, Receptor binding data, Receptor binding pocket, Receptor probe, Receptor recognition, Recognit, Saito, Selectivity, Side chain, Side chains, Strong preference, Sulfated, Suzuki, Velkov, Viral, Virol, Virology, Virus, Virus hemagglutinin, Wang.
Abstract
The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl‐glycans, usually linked to galactose in either α2,6 or α2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg‐adapted variants. Overall, the review serves as an up‐to‐date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA. Copyright © 2013 John Wiley & Sons, Ltd.
It remains contentious whether the influenza B hemagglutinin (HA) preferentially binds to α2,6‐linked human type receptors or equally well to α2,3‐linked type avian receptors, and how or if in fact any receptor selectivity plays a role in the viruses infectivity of humans. For the first time, the present review forms a treatise that unifies the receptor binding data and provides a consensus for the modalities that determine the receptor binding selectivity of the influenza B HA.
Url:
DOI: 10.1002/jmr.2293
Affiliations:
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Le document en format XML
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<front><div type="abstract">The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl‐glycans, usually linked to galactose in either α2,6 or α2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg‐adapted variants. Overall, the review serves as an up‐to‐date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA. Copyright © 2013 John Wiley & Sons, Ltd.</div>
<div type="abstract">It remains contentious whether the influenza B hemagglutinin (HA) preferentially binds to α2,6‐linked human type receptors or equally well to α2,3‐linked type avian receptors, and how or if in fact any receptor selectivity plays a role in the viruses infectivity of humans. For the first time, the present review forms a treatise that unifies the receptor binding data and provides a consensus for the modalities that determine the receptor binding selectivity of the influenza B HA.</div>
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