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Interaction of alphaVbeta3 and alphaVbeta6 integrins with human parechovirus 1

Jani Seitsonen1, Petri Susi, Outi Heikkilä

  • 1Department of Biosciences, Institute of Biotechnology, PO Box 65, Viikinkaari 1, FIN-00014 University of Helsinki, Finland.

Journal of Virology
|June 18, 2010
PubMed

Insights

Human parechovirus (HPEV) infections are common in children and severe in neonates. Integrins alpha(V)beta(6) act as high-affinity receptors for HPEV1, influencing cellular infectivity.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Interactions

Background:

  • Human parechovirus (HPEV) infections are prevalent in young children and can cause severe illness in newborns.
  • Integrins, particularly alpha(V) integrins, have been implicated in HPEV1 cellular entry.
  • The RGD motif in the VP1 capsid protein is hypothesized to mediate HPEV1 interaction with alpha(V) integrins.

Purpose of the Study:

  • To biochemically and structurally characterize the binding of integrins alpha(V)beta(3) and alpha(V)beta(6) to Human parechovirus 1 (HPEV1).
  • To elucidate the role of specific integrins as receptors for HPEV1 and their contribution to viral infectivity.

Main Methods:

  • Biochemical assays to assess integrin-HPEV1 binding affinity.
  • Function-blocking assays using soluble integrins to determine receptor function.
  • Electron cryo-microscopy and image reconstruction to determine the structure of HPEV1-integrin complexes.

Main Results:

  • HPEV1 binds efficiently to immobilized alpha(V)beta(3) and alpha(V)beta(6) integrins, with a higher affinity for alpha(V)beta(6).
  • Soluble alpha(V)beta(6) effectively blocks HPEV1 cellular infectivity, identifying it as a high-affinity receptor.
  • Structural analysis revealed HPEV1's picornavirus-like organization and precise integrin binding footprints.
  • RGD peptide blocking and structural data suggest RGD motif location differences influence integrin specificity.

Conclusions:

  • Integrin alpha(V)beta(6) is a high-affinity receptor for HPEV1, mediating cellular entry.
  • Differences in integrin amino acid sequences, not viral footprints, primarily account for varied receptor binding.
  • This study provides the first structural insights into parechovirus-integrin interactions.

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