Antibodies Change the Mechanics of Adhesion Fimbriae: a Case Study of CS20 Fimbriae Expressed by Enterotoxigenic Escherichia Coli
2015 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 108, 602- p.Article in journal, Meeting abstract (Other academic) Published
Enterotoxigenic Escherichia coli (ETEC) express a variety of fimbriae that mediate adhesion to host epithelial cells. It has been shown that the ability of a fimbriated bacterial cell to attach and stay attached to host cells does not merely depend on the adhesin expressed distal of the fimbriae but also the biomechanical properties of the fimbriae are vital for sustained adhesion. Fimbriae can significantly extend under a constant force when exposed to an external force and therefore reduce the load on the adhesin, which is believed to help bacteria to withstand external forces applied by various body defense systems. Thus, it is thought that the fimbrial shaft and adhesin have co-evolved for optimal function when bacteria attach to host cells. To investigate if antibodies, normally found in the intestines, affects the biomechanical properties of fimbriae, we exposed CS20 fimbriae expressed by ETEC to anti-fimbrial antibodies and measured these properties using optical tweezers force spectroscopy. Our data show a change in the force required to extend the fimbriae and that the elasticity is significantly reduced by the presence of antibodies. The reduced elasticity, likely due to cross-linking of fimbrial subunits, could thus be another assignment for antibodies; in addition to their mission in marking bacteria as foreign, our data indicate that antibodies physically compromise fimbrial function. To further confirm interaction of antibodies to their specific target we performed western blot analysis, transmission electron microscopy and immunofluoresence microscopy. In the presence of antibodies, we suggest that our assay and results will be a starting point for further studies aimed at inhibiting bacterial adhesion by antibodies.
Place, publisher, year, edition, pages
Cell Press , 2015. Vol. 108, 602- p.
IdentifiersURN: urn:nbn:se:umu:diva-100729DOI: 10.1016/j.bpj.2014.11.3276ISI: 000362849600643OAI: oai:DiVA.org:umu-100729DiVA: diva2:793647
59th Annual Meeting of the Biophysical-Society, Baltimore, February 7-11, 2015.
Meeting Abstract: 3035-Pos2015-03-092015-03-092015-11-10Bibliographically approved