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Review
. 2015:367:1-28.
doi: 10.1007/128_2013_466.

Sialic Acid Receptors of Viruses

Mikhail Matrosovich  1 , Georg Herrler, Hans Dieter Klenk
Affiliations
Review

Sialic Acid Receptors of Viruses

Mikhail Matrosovich et al. Top Curr Chem. 2015.

Abstract

Sialic acid linked to glycoproteins and gangliosides is used by many viruses as a receptor for cell entry. These viruses include important human and animal pathogens, such as influenza, parainfluenza, mumps, corona, noro, rota, and DNA tumor viruses. Attachment to sialic acid is mediated by receptor binding proteins that are constituents of viral envelopes or exposed at the surface of non-enveloped viruses. Some of these viruses are also equipped with a neuraminidase or a sialyl-O-acetyl-esterase. These receptor-destroying enzymes promote virus release from infected cells and neutralize sialic acid-containing soluble proteins interfering with cell surface binding of the virus. Variations in the receptor specificity are important determinants for host range, tissue tropism, pathogenicity, and transmissibility of these viruses.

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Figures

Fig. 1
Fig. 1
Sialic acid binding sites of the hemagglutinin (a) and the neuraminidase (b) of influenza A virus and the hemagglutinin-esterase-fusion protein of influenza C virus (c). Molecular surfaces of HA and HEF trimers and the NA tetramer are shown. Receptor-binding sites of HA, HEF and the hemadsorption site of NA are colored yellow. The catalytic sites of NA and HEF are colored green. Sialic acid moieties in the binding sites of HA and NA are shown as stick models. The figure is based on crystal structures 1MQM, 1W20, and 1FLC from Protein Data Bank
See this image and copyright information in PMC

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