tetano
Editor, Senior Moderator
Curr Opin Virol. 2014 Jul 22;7C:128-133. doi: 10.1016/j.coviro.2014.06.004. [Epub ahead of print]
Influenza virus-glycan interactions.
Air GM.
Author information
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.
PMID:
25061947
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25061947
Influenza virus-glycan interactions.
Air GM.
Author information
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.
PMID:
25061947
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25061947