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

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 diver...

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Main Authors:	Nils H. Rustmeier, Michael Strebl, Thilo Stehle
Format:	Article
Language:	English
Published:	MDPI AG 2019-10-01
Series:	Viruses
Subjects:	sialic acid non-enveloped viruses antiviral compounds multivalency inhibition
Online Access:	https://www.mdpi.com/1999-4915/11/10/947

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spelling	doaj-7bdea2fa169144078574ae36d056367a2020-11-25T01:18:40ZengMDPI AGViruses1999-49152019-10-01111094710.3390/v11100947v11100947The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral StrategiesNils H. Rustmeier0Michael Strebl1Thilo Stehle2Interfaculty Institute of Biochemistry, University of Tuebingen, 72076 Tuebingen, Baden-Wuerttemberg, GermanyInterfaculty Institute of Biochemistry, University of Tuebingen, 72076 Tuebingen, Baden-Wuerttemberg, GermanyInterfaculty Institute of Biochemistry, University of Tuebingen, 72076 Tuebingen, Baden-Wuerttemberg, GermanyVirus 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.https://www.mdpi.com/1999-4915/11/10/947sialic acidnon-enveloped virusesantiviral compoundsmultivalencyinhibition
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Nils H. Rustmeier Michael Strebl Thilo Stehle
spellingShingle	Nils H. Rustmeier Michael Strebl Thilo Stehle The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies Viruses sialic acid non-enveloped viruses antiviral compounds multivalency inhibition
author_facet	Nils H. Rustmeier Michael Strebl Thilo Stehle
author_sort	Nils H. Rustmeier
title	The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies
title_short	The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies
title_full	The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies
title_fullStr	The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies
title_full_unstemmed	The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies
title_sort	symmetry of viral sialic acid binding sites–implications for antiviral strategies
publisher	MDPI AG
series	Viruses
issn	1999-4915
publishDate	2019-10-01
description	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.
topic	sialic acid non-enveloped viruses antiviral compounds multivalency inhibition
url	https://www.mdpi.com/1999-4915/11/10/947
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The Symmetry of Viral Sialic Acid Binding Sites–Implications for Antiviral Strategies

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