title: Glycan Engagement by Viruses: Receptor Switches and Specificity.
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.
authors.affiliation: Interfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany; email: thilo.stehle@uni-tuebingen.de.
authors.forename: Luisa J
authors.initials: LJ
authors.lastname: Ströh
authors.affiliation: Interfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany; email: thilo.stehle@uni-tuebingen.de.|Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
authors.forename: Thilo
authors.initials: T
authors.lastname: Stehle
keywords: coronavirus; polyomavirus; reovirus; rotavirus; sialic acid; sulfated glycosaminoglycan