title: Influenza virus-glycan interactions.
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.
authors: Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, 940 Stanton L. Young Blvd, Oklahoma City, OK 73104, USA. Electronic address: Gillian-air@ouhsc.edu.
authors: Gillian M
authors: GM
authors: Air
mesh_terms: D000818:Animals; D001717:Birds; D005936:Glucans / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000235:genetics / Q000378:metabolism*; D005585:Influenza in Birds / Q000378:metabolism* / Q000821:virology; D007251:Influenza, Human / Q000378:metabolism* / Q000821:virology; D011991:Receptors, Virus / Q000378:metabolism*
chemical_list: D005936:Glucans; D011991:Receptors, Virus