Structural Insight into Non-Enveloped Virus Binding to Glycosaminoglycan Receptors: A Review

Viruses are infectious agents that hijack the host cell machinery in order to replicate and generate progeny. Viral infection is initiated by attachment to host cell receptors, and typical viral receptors are cell-surface-borne molecules such as proteins or glycan structures. Sialylated glycans (gly...

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Published inViruses Vol. 13; no. 5; p. 800
Main Authors Sorin, Marie N, Kuhn, Jasmin, Stasiak, Aleksandra C, Stehle, Thilo
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 29.04.2021
MDPI
Subjects
Animals
Binding sites
Cell surface
Chondroitin sulfate
Extracellular matrix
Gag protein
glycans
Glycosaminoglycans
glycovirology
Heparan sulfate
Human papillomavirus
Humans
Life Sciences
Ligands
Molecular Conformation
non-enveloped viruses
Papilloma
Physiology
Polysaccharides
Proteins
Receptors, Virus
Review
Sialic acids
structural biology
Structure-Activity Relationship
Virus Internalization
Virus Physiological Phenomena
Viruses
glycosaminoglycans
glycovirology
viruses
non-enveloped viruses
structural biology
glycans
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Summary:Viruses are infectious agents that hijack the host cell machinery in order to replicate and generate progeny. Viral infection is initiated by attachment to host cell receptors, and typical viral receptors are cell-surface-borne molecules such as proteins or glycan structures. Sialylated glycans (glycans bearing sialic acids) and glycosaminoglycans (GAGs) represent major classes of carbohydrate receptors and have been implicated in facilitating viral entry for many viruses. As interactions between viruses and sialic acids have been extensively reviewed in the past, this review provides an overview of the current state of structural knowledge about interactions between non-enveloped human viruses and GAGs. We focus here on adeno-associated viruses, human papilloma viruses (HPVs), and polyomaviruses, as at least some structural information about the interactions of these viruses with GAGs is available. We also discuss the multivalent potential for GAG binding, highlighting the importance of charged interactions and positively charged amino acids at the binding sites, and point out challenges that remain in the field.
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PMCID: PMC8146366
These authors contributed equally.
ISSN:1999-4915
1999-4915
DOI:10.3390/v13050800