期刊
ANNUAL REVIEW OF VIROLOGY, VOL 1
卷 1, 期 -, 页码 285-306出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-virology-031413-085417
关键词
sialic acid; sulfated glycosaminoglycan; polyomavirus; coronavirus; reovirus; rotavirus
类别
A large number of viruses, including many human pathogens, bind cellsurface 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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