Unfolding individual Als5p adhesion proteins on live cells

David Alsteens, Vincent Dupres, Stephen A. Klotz, Nand K. Gaur, Peter N. Lipke, Yves F. Dufrêne

Research output: Contribution to journalArticle

76 Scopus citations

Abstract

Elucidating the molecular mechanisms behind the strength and mechanics of cell adhesion proteins is of central importance in cell biology and offers exciting avenues for the identification of potential drug targets. Here we use single-molecule force spectroscopy to investigate the adhesive and mechanical properties of the widely expressed Als5p cell adhesion protein from the opportunistic pathogen Candida albicans. We show that the forces required to unfold individual tandem repeats of the protein are in the 150-250 pN range, both on isolated molecules and on live cells. We also find that the unfolding probability increases with the number of tandem repeats and correlates with the level of cell adherence. We suggest that the modular and flexible nature of Als5p conveys both strength and toughness to the protein, making it ideally suited for cell adhesion. The single-molecule measurements presented here open new avenues for understanding the mechanical properties of adhesion molecules from mammalian and microbial cells and may help us to elucidate their potentialimplications in diseases such as inflammation, cancer, and infection.

Original languageEnglish (US)
Pages (from-to)1677-1682
Number of pages6
JournalACS Nano
Volume3
Issue number7
DOIs
StatePublished - Jul 28 2009

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Keywords

  • AFM
  • Candida albicans
  • Cell adhesion proteins
  • Pathogens
  • Protein unfolding
  • Single-molecule force spectroscopy

ASJC Scopus subject areas

  • Materials Science(all)
  • Engineering(all)
  • Physics and Astronomy(all)

Cite this

Alsteens, D., Dupres, V., Klotz, S. A., Gaur, N. K., Lipke, P. N., & Dufrêne, Y. F. (2009). Unfolding individual Als5p adhesion proteins on live cells. ACS Nano, 3(7), 1677-1682. https://doi.org/10.1021/nn900078p