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The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies

Interfaculty Institute of Biochemistry, University of Tuebingen, 72076 Tuebingen, Baden-Wuerttemberg, Germany
Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA
Author to whom correspondence should be addressed.
Viruses 2019, 11(10), 947;
Received: 13 August 2019 / Revised: 2 October 2019 / Accepted: 9 October 2019 / Published: 14 October 2019
(This article belongs to the Special Issue Viral Entry Pathways)
Virus infections are initiated by the attachment of the viral particle to protein or carbohydrate receptors on the host cell. Sialic acid-bearing glycan structures are prominently displayed at the cell surface, and, consequently, these structures can function as receptors for a large number of diverse viruses. Structural biology research has helped to establish the molecular bases for many virus–sialic acid interactions. Due to the icosahedral 532 point group symmetry that underlies many viral capsids, the receptor binding sites are frequently arranged in a highly symmetric fashion and linked by five-fold, three-fold, or two-fold rotation axes. For the inhibition of viral attachment, one emerging strategy is based on developing multivalent sialic acid-based inhibitors that can simultaneously engage several of these binding sites, thus binding viral capsids with high avidity. In this review, we will evaluate the structures of non-enveloped virus capsid proteins bound to sialylated glycan receptors and discuss the potential of these structures for the development of potent antiviral attachment inhibitors. View Full-Text
Keywords: sialic acid; non-enveloped viruses; antiviral compounds; multivalency; inhibition sialic acid; non-enveloped viruses; antiviral compounds; multivalency; inhibition
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Rustmeier, N.H.; Strebl, M.; Stehle, T. The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies. Viruses 2019, 11, 947.

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