ArticleEuropean biophysics journal : EBJ2009
Physical properties of the specific PapG-galabiose binding in E. coli P pili-mediated adhesion.
Article in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 33 citations in OpenAlex.
- A review on pilus assembly mechanisms in Gram-positive and Gram-negative bacteria.Cell surface (Amsterdam, Netherlands) · 2022Article
- The Role of Glycans in Bacterial Adhesion to Mucosal Surfaces: How Can Single-Molecule Techniques Advance Our Understanding?Microorganisms · 2018Review
- Theory for nonlinear dynamic force spectroscopy.European biophysics journal : EBJ · 2017Article
- A structural basis for sustained bacterial adhesion: biomechanical properties of CFA/I pili.Journal of molecular biology · 2012Article
- Article
- Catch-bond behavior of bacteria binding by slip bonds.Biophysical journal · 2010Article
- Unfolding and refolding properties of S pili on extraintestinal pathogenic Escherichia coli.European biophysics journal : EBJ · 2010Article
- Population structure of gut Escherichia coli and its role in development of extra-intestinal infections.Iranian journal of microbiology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Detailed analyses of the mechanisms that mediate binding of the uropathogenic Escherichia coli to host cells are essential, as attachment is a prerequisite for the subsequent infection process. We explore, by means of force measuring optical tweezers, the interaction between the galabiose receptor and the adhesin PapG expressed by P pili on single bacterial cells. Two variants of dynamic force spectroscopy were applied based on constant and non-linear loading force. The specific PapG-galabiose binding showed typical slip-bond behaviour in the force interval (30-100 pN) set by the pilus intrinsic biomechanical properties. Moreover, it was found that the bond has a thermodynamic off-rate and a bond length of 2.6 x 10(-3) s(-1) and 5.0 A, respectively. Consequently, the PapG-galabiose complex is significantly stronger than the internal bonds in the P pilus structure that stabilizes the helical chain-like macromolecule. This finding suggests that the specific binding is strong enough to enable the P pili rod to unfold when subjected to strong shear forces in the urinary tract. The unfolding process of the P pili rod promotes the formation of strong multipili interaction, which is important for the bacterium to maintain attachment to the host cells.
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