Efficient accommodation of recombinant, foot-and-mouth disease virus RGD peptides to cell-surface integrins

Pilar Alcalá, Jordi X. Feliu, Anna Arís, Antonio Villaverde

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13 Citations (Scopus)


The engineering of either complete virus cell-binding proteins or derived ligand peptides generates promising nonviral vectors for cell targeting and gene therapy. In this work, we have explored the molecular interaction between a recombinant, integrin-binding foot-and-mouth disease virus RGD peptide displayed on the surface of a carrier protein and its receptors on the cell surface. By increasing the number of viral segments, cell binding to recombinant proteins was significantly improved. This fact resulted in a dramatic growth stimulation of virus-sensitive BHK21 cells but not virus-resistant HeLa cells in protein-coated wells. Surprisingly, growth stimulation was not observed in vitronectin-coated plates, suggesting that integrins other than αvβ3 could be involved in binding of the recombinant peptide, maybe as coreceptors. On the other hand, both free and cell-linked integrins did not modify the enzymatic activity of RGD-based enzymatic sensors that contrarily, were activated by the induced fit of anti-RGD antibodies. Those findings are discussed in the context of a proper mimicry of the unusually complex architecture of this cell-binding site as engineered in multifunctional proteins. © 2001 Academic Press.
Original languageEnglish
Pages (from-to)201-206
JournalBiochemical and Biophysical Research Communications
Publication statusPublished - 1 Jan 2001


  • Cell receptor
  • FMDV
  • Integrin
  • RGD
  • Recombinant protein

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