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Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin

Danielle Dicara1, Alison Burman, Stuart Clark

  • 1Centre for Tumour Biology, Barts and the London Queen Mary's Medical and Dental School, Charterhouse Square, London EC1M 6BQ, United Kingdom.

Journal of Virology
|November 30, 2007
PubMed

Insights

Foot-and-mouth disease virus (FMDV) uses its VP1 protein to bind cell integrins. Specific structural features allow FMDV to form stable, EDTA-resistant bonds with integrin alphavbeta6, enhancing its infectiousness.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Foot-and-mouth disease virus (FMDV) infection initiates through binding to cell surface integrins.
  • This interaction is mediated by the RGD motif in the VP1 capsid protein's GH loop and is cation-dependent.
  • Initial FMDV-integrin contact is sensitive to EDTA, which chelates cations.

Purpose of the Study:

  • To investigate the binding mechanism between FMDV VP1-derived peptides and integrins.
  • To identify structural determinants of stable FMDV-integrin interactions.
  • To understand the biological significance of stable binding for FMDV infectivity.

Main Methods:

  • Used RGD-containing peptides from FMDV VP1 to study integrin binding.
  • Investigated the effect of specific peptide substitutions on binding stability.
  • Assessed the EDTA resistance of peptide-integrin and FMDV-integrin complexes.
  • Examined binding to integrin alphavbeta6.

Main Results:

  • Some FMDV VP1-derived peptides form highly stable, EDTA-resistant associations with integrin alphavbeta6.
  • Stable binding requires a helical structure C-terminal to the RGD motif, specifically leucine residues at positions RGD+1 and RGD+4.
  • FMDV particles also exhibit stable, EDTA-resistant binding to integrin alphavbeta6.

Conclusions:

  • The integrin-binding loop of FMDV has evolved to form very stable complexes with its primary receptor, integrin alphavbeta6.
  • This stable complex formation likely contributes significantly to the high infectiousness of FMDV.
  • Structural insights into FMDV-integrin interactions could inform antiviral strategies.

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