Observation of Bacterial Type I Pili Extension and Contraction under Fluid Flow
| Autor: | Jaime E. Castro, Manu Forero-Shelton, Nathaly Marín-Medina, Dilia E. Rangel, Andres Gonzalez-Mancera |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Contraction (grammar) Parallel-plate flow chamber Biophysics lcsh:Medicine Models Biological Microbiology Bacterial Adhesion Pilus Fimbriae Proteins Stress Physiological Molecular Cell Biology Biological Fluid Mechanics Cell Adhesion Fluid dynamics Uropathogenic Escherichia coli Cell Mechanics Biomechanics Biomacromolecule-Ligand Interactions lcsh:Science Protein Structure Quaternary Biology Escherichia Coli Multidisciplinary Chemistry Escherichia coli Proteins Physics lcsh:R Force spectroscopy Biomechanical Phenomena Bacterial Pathogens Host-Pathogen Interaction Bacterial adhesin Drag Fimbriae Bacterial Thermodynamics lcsh:Q Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Vol 8, Iss 6, p e65563 (2013) |
| ISSN: | 1932-6203 |
| Popis: | Type I pili are proteinaceous tethers that mediate bacterial adhesion of uropathogenic Escherichia coli to surfaces and are thought to help bacteria resist drag forces imparted by fluid flow via uncoiling of their quaternary structure. Uncoiling and recoiling have been observed in force spectroscopy experiments, but it is not clear if and how this process occurs under fluid flow. Here we developed an assay to study the mechanical properties of pili in a parallel plate flow chamber. We show that pili extend when attached E. coli bacteria are exposed to increasing shear stresses, that pili can help bacteria move against moderate fluid flows, and characterize two dynamic regimes of this displacement. The first regime is consistent with entropic contraction as modeled by a freely jointed chain, and the second with coiling of the quaternary structure of pili. These results confirm that coiling and uncoiling happen under flow but the observed dynamics are different from those reported previously. Using these results and those from previous studies, we review the mechanical properties of pili in the context of other elastic proteins such as the byssal threads of mussels. It has been proposed that the high extensibility of pili may help recruit more pili into tension and lower the force acting on each one by damping changes in force due to fluid flow. Our analysis of the mechanical properties suggests additional functions of pili; in particular, their extensibility may reduce tension by aligning pili with the direction of flow, and the uncoiled state of pili may complement uncoiling in regulating the force of the terminal adhesin. |
| Databáze: | OpenAIRE |
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