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A structural basis for sustained bacterial adhesion : Biomechanical properties of CFA/I Pili

Andersson, Magnus (författare)
Umeå universitet,Institutionen för fysik,The Biophysics and Biophotonics group
Svantesson, Mats (författare)
Umeå universitet,Institutionen för fysik
Björnham, Oscar (författare)
Swedish Defence Research Agency (FOI), SE-906 21 Umeå, Sweden
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Badahdah, Arwa (författare)
Department of Oral Biology, Boston University School of Dental Medicine
Uhlin, Bernt Eric (författare)
Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
Bullitt, Esther (författare)
Department of Physiology and Biophysics, Boston University School of Medicine
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 (creator_code:org_t)
Elsevier, 2012
2012
Engelska.
Ingår i: Journal of Molecular Biology. - : Elsevier. - 0022-2836 .- 1089-8638. ; 415:5, s. 918-928
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • Enterotoxigenic Escherichia coli (ETEC) are a major cause of diarrheal disease worldwide. Adhesion pili (or fimbriae), such as the CFA/I (colonization factor antigen I) organelles that enable ETEC to attach efficiently to the host intestinal tract epithelium, are critical virulence factors for initiation of infection. We characterized at single organelle level the intrinsic biomechanical properties and kinetics of individual CFA/I pili, demonstrating that weak external forces (7.5 pN) are sufficient to unwind the intact helical filament of this prototypical ETEC pilus and that it quickly regains its original structure when the force is removed. While the general relationship between exertion of force and an increase in the filament length for CFA/I pili associated with diarrheal disease is analogous to that of P-pili and type 1 pili, associated with urinary tract and other infections, the biomechanical properties of these different pili differ in key quantitative details. Unique features of CFA/I pili, including the significantly lower force required for unwinding, the higher extension speed at which the pili enter a dynamic range of unwinding, and the appearance of sudden force drops during unwinding can be attributed to morphological features of CFA/I pili including weak layer-to-layer interactions between subunits on adjacent turns of the helix, and the approximately horizontal orientation of pilin subunits with respect to the filament axis. Our results indicate that ETEC CFA/I pili are flexible organelles optimized to withstand harsh motion without breaking, resulting in continued attachment to the intestinal epithelium by the pathogenic bacteria that express these pili.

Ämnesord

NATURVETENSKAP  -- Fysik -- Annan fysik (hsv//swe)
NATURAL SCIENCES  -- Physical Sciences -- Other Physics Topics (hsv//eng)

Nyckelord

optical tweezers
unwinding
force spectroscopy
fimbria
fysik
Physics

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