Association analyses of large-scale glycan microarray data reveal novel host-specific substructures in influenza A virus binding glycans

Influenza A viruses can infect a wide variety of animal species and, occasionally, humans. Infection occurs through the binding formed by viral surface glycoprotein hemagglutinin and certain types of glycan receptors on host cell membranes. Studies have shown that the α2,3-linked sialic acid motif (...

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Bibliographic Details
Published in:Scientific reports 2015-10, Vol.5 (1), p.15778-15778, Article 15778
Main Authors: Zhao, Nan, Martin, Brigitte E, Yang, Chun-Kai, Luo, Feng, Wan, Xiu-Feng
Format: Article
Language:English
Subjects:
Amino Acid Sequence - physiology
Animals
Birds - virology
Cell membranes
Data processing
Dogs
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
Hemagglutinins
Humans
Influenza
Influenza A
Influenza A virus - metabolism
Microarray Analysis - methods
N-Acetylneuraminic Acid - metabolism
Polysaccharides
Polysaccharides - metabolism
Receptors, Virus - metabolism
Swine
Viruses
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Summary:Influenza A viruses can infect a wide variety of animal species and, occasionally, humans. Infection occurs through the binding formed by viral surface glycoprotein hemagglutinin and certain types of glycan receptors on host cell membranes. Studies have shown that the α2,3-linked sialic acid motif (SA2,3Gal) in avian, equine, and canine species; the α2,6-linked sialic acid motif (SA2,6Gal) in humans; and SA2,3Gal and SA2,6Gal in swine are responsible for the corresponding host tropisms. However, more detailed and refined substructures that determine host tropisms are still not clear. Thus, in this study, we applied association mining on a set of glycan microarray data for 211 influenza viruses from five host groups: humans, swine, canine, migratory waterfowl, and terrestrial birds. The results suggest that besides Neu5Acα2-6Galβ, human-origin viruses could bind glycans with Neu5Acα2-8Neu5Acα2-8Neu5Ac and Neu5Gcα2-6Galβ1-4GlcNAc substructures; Galβ and GlcNAcβ terminal substructures, without sialic acid branches, were associated with the binding of human-, swine-, and avian-origin viruses; sulfated Neu5Acα2-3 substructures were associated with the binding of human- and swine-origin viruses. Finally, through three-dimensional structure characterization, we revealed that the role of glycan chain shapes is more important than that of torsion angles or of overall structural similarities in virus host tropisms.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep15778