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

ABSTRACT: 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 ?2,3-linked sialic acid motif (SA2,3Gal) in avian, equine, and canine species; the ?2,6-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 Neu5Ac?2-6Gal?, human-origin viruses could bind glycans with Neu5Ac?2-8Neu5Ac?2-8Neu5Ac and Neu5Gc?2-6Gal?1-4GlcNAc substructures; Gal? and GlcNAc? terminal substructures, without sialic acid branches, were associated with the binding of human-, swine-, and avian-origin viruses; sulfated Neu5Ac?2-3 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.

SUBMITTER: Zhao N 

PROVIDER: S-EPMC4623813 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature