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Parvovirus glycan interactions.

Lin-Ya Huang1, Sujata Halder1, Mavis Agbandje-McKenna1

  • 1Department of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL, 32610, USA.

Current Opinion in Virology
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Summary
This summary is machine-generated.

Parvoviruses use cell surface glycans like sialic acid for attachment. Despite diverse sequences, their similar capsid structures bind these essential receptors, influencing infection outcomes.

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Area of Science:

  • Virology
  • Structural Biology
  • Glycobiology

Background:

  • Parvoviridae family viruses use glycan receptors for cell attachment.
  • These interactions influence viral transduction efficiency and pathogenicity.
  • Understanding glycan-host interactions is crucial for parvovirus research.

Purpose of the Study:

  • To review the glycan receptors utilized by Parvoviridae.
  • To identify capsid binding footprints for these receptors.
  • To discuss the overlap between binding sites and viral tropism, transduction, and pathogenicity.

Main Methods:

  • Literature review of Parvoviridae studies focusing on glycan interactions.
  • Analysis of structural data on parvovirus capsids and their binding sites.
  • Comparative analysis of glycan receptor usage across different parvovirus genera.

Main Results:

  • Most parvoviruses bind negatively charged glycans, including sialic acid and heparan sulfate.
  • High structural homology in parvovirus capsids facilitates common glycan binding regions.
  • Sequence diversity within these common footprints allows for varied glycan binding specificity.

Conclusions:

  • Parvovirus glycan receptor binding is conserved despite sequence diversity.
  • Capsid structure dictates common binding sites, while sequence variation refines specificity.
  • Glycan receptor interactions are key determinants of parvovirus tropism and pathogenesis.