Literature DB >> 25061947

Influenza virus-glycan interactions.

Gillian M Air1.   

Abstract

It has been known for many years that influenza viruses bind by their hemagglutinin surface glycoprotein to sialic acid (N-acetylneuraminic acid) on the surface of the host cell, and that avian viruses most commonly bind to sialic acid linked α2-3 to galactose while most human viruses bind to sialic acid in the α2-6 configuration. Over the past few years there has been a large increase in data on this binding due to technological advances in glycan binding assays, reverse genetic systems for influenza and in X-ray crystallography. The results show some surprising changes in binding specificity that do not appear to affect the ability of the virus to infect host cells.
Copyright © 2014 Elsevier B.V. All rights reserved.

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Year:  2014        PMID: 25061947      PMCID: PMC4149921          DOI: 10.1016/j.coviro.2014.06.004

Source DB:  PubMed          Journal:  Curr Opin Virol        ISSN: 1879-6257            Impact factor:   7.090


  28 in total

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Authors:  G M Air; W G Laver
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Authors:  Trevenan Walther; Rositsa Karamanska; Renee W Y Chan; Michael C W Chan; Nan Jia; Gillian Air; Clark Hopton; Maria P Wong; Anne Dell; J S Malik Peiris; Stuart M Haslam; John M Nicholls
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7.  Guinea pig cytomegalovirus trimer complex gH/gL/gO uses PDGFRA as universal receptor for cell fusion and entry.

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