The sweet spot: defining virus-sialic acid interactions.

Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101190261 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1740-1534 (Electronic) Linking ISSN: 17401526 NLM ISO Abbreviation: Nat Rev Microbiol Subsets: MEDLINE

Original Publication: London, UK : Nature Pub. Group, c2003-

N-Acetylneuraminic Acid/*metabolism ; Polysaccharides/*metabolism ; Receptors, Cell Surface/*metabolism ; Virus Diseases/*virology ; Viruses/*metabolism; Animals ; Binding Sites ; Host-Pathogen Interactions ; Humans ; Receptors, Virus/metabolism ; Species Specificity ; Virus Attachment

Viral infections are initiated by attachment of the virus to host cell surface receptors, including sialic acid-containing glycans. It is now possible to rapidly identify specific glycan receptors using glycan array screening, to define atomic-level structures of virus-glycan complexes and to alter the glycan-binding site to determine the function of glycan engagement in viral disease. This Review highlights general principles of virus-glycan interactions and provides specific examples of sialic acid binding by viruses with stalk-like attachment proteins, including influenza virus, reovirus, adenovirus and rotavirus. Understanding virus-glycan interactions is essential to combating viral infections and designing improved viral vectors for therapeutic applications.

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R01 AI76983 United States AI NIAID NIH HHS; R01 AI076983 United States AI NIAID NIH HHS; R01 AI038296 United States AI NIAID NIH HHS; R37 AI038296 United States AI NIAID NIH HHS; R37 AI38296 United States AI NIAID NIH HHS

0 (Polysaccharides)
0 (Receptors, Cell Surface)
0 (Receptors, Virus)
GZP2782OP0 (N-Acetylneuraminic Acid)

Date Created: 20140930 Date Completed: 20150121 Latest Revision: 20211021

20250114

PMC4791167

10.1038/nrmicro3346

25263223