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.
filaments by single particle analysis of electron microscope (EM) data. We already defined the 3D structure of myosin filaments of various muscles from different species by both X-ray diffraction modelling and EM and single particle analysis including insect flight muscle, scallop striated muscle, fish skeletal muscle and rabbit cardiac muscle. We are now studying the 3D structure of myosin filaments isolated from human heart muscles. Mutations in cardiac myosin, C-protein and titin are known to be associated with cardiomyopathies (e.g. hypertrophic cardiomyopathy and dilated cardiomyopathy). In order to understand myosin-associated heart disease, it is important to understand the 3D structure of myosin filaments in normal heart muscle. Recently we have developed procedures to isolate human cardiac muscle myosin filaments preserving their highly ordered pseudo-helical structure thus making them amenable, for the first time, to EM and single particle image analysis. We have collected EM data from myosin filaments isolated from both normal and failing hearts, and have so far processed the data from normal heart muscle. Analysis of the 3D structure of myosin filaments in normal heart muscle will permit the structural effects of known myosin filaments-associated mutations to be investigated in detail.
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