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The unfolding of the P pili quaternary structure by stretching is reversible, not plastic
Umeå University, Faculty of Science and Technology, Department of Physics.
Umeå University, Faculty of Science and Technology, Department of Applied Physics and Electronics.ORCID iD: 0000-0002-9031-4331
Department of Microbiology and Immunology, The Lawson Health Research Institute, University of Western Ontario, London, Ontario, Canada.
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). (Uhlin)
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2005 (English)In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 6, no 1, p. 52-56Article in journal (Refereed) Published
Abstract [en]

P pili are protein filaments expressed by uropathogenic Escherichia coli that mediate binding to glycolipids on epithelial cell surfaces, which is a prerequisite for bacterial infection. When a bacterium, attached to a cell surface, is exposed to external forces, the pili, which are composed of ∼103PapA protein subunits arranged in a helical conformation, can elongate by unfolding to a linear conformation. This property is considered important for the ability of a bacterium to withstand shear forces caused by urine flow. It has hitherto been assumed that this elongation is plastic, thus constituting a permanent conformational deformation. We demonstrate, using optical tweezers, that this is not the case; the unfolding of the helical structure to a linear conformation is fully reversible. It is surmised that this reversibility helps the bacteria regain close contact to the host cells after exposure to significant shear forces, which is believed to facilitate their colonization.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2005. Vol. 6, no 1, p. 52-56
Keywords [en]
folding, helical structure, optical tweezers, PapA, uropathogenic Escherichia coli
National Category
Cell and Molecular Biology Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-12118DOI: 10.1038/sj.embor.7400310ISI: 000226183500012PubMedID: 15592451OAI: oai:DiVA.org:umu-12118DiVA, id: diva2:151789
Available from: 2007-10-03 Created: 2007-10-03 Last updated: 2019-01-24Bibliographically approved

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Fällman, ErikSchedin, StaffanUhlin, Bernt EricAxner, Ove

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