Glycan Engagement by Viruses: Receptor Switches and Specificity

Annual Review of Virology
Luisa J Ströh, Thilo Stehle

Abstract

A large number of viruses, including many human pathogens, bind cell-surface glycans during the initial steps of infection. Viral glycan receptors such as glycosaminoglycans and sialic acid-containing carbohydrates are often negatively charged, but neutral glycans such as histo-blood group antigens can also function as receptors. The engagement of glycans facilitates attachment and entry and, consequently, is often a key determinant of the host range, tissue tropism, pathogenicity, and transmissibility of viruses. Here, we review current knowledge about virus-glycan interactions using representative crystal structures of viral attachment proteins in complex with glycans. We illuminate the determinants of specificity utilized by different glycan-binding viruses and explore the potential of these interactions for switching receptor specificities within or even between glycan classes. A detailed understanding of these parameters is important for the prediction of binding sites where structural information is not available, and is invaluable for the development of antiviral therapeutics.

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Related Concepts

Carbohydrate nutrients
Virus
Glycosaminoglycans
Antibodies, Neutralizing
Sialic Acid Assay
Binding Protein
Site
Antigens
Cell Surface
Binding (Molecular Function)

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