## Abstract Bacterial adhesion on biomaterial surfaces is the initial step in establishing infections and leads to the formation of biofilms. In this study, silicone was modified with different biopolymers and silanes, including: heparin, hyaluronan, and selfβassembled octadecyltrichlorosilane (OTS
Atomic force microscopy study of the role of LPS O-antigen on adhesion of E. coli
β Scribed by Joshua Strauss; Nancy A. Burnham; Terri A. Camesano
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 504 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0952-3499
- DOI
- 10.1002/jmr.955
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The Oβantigen is a highly variable component of the lipopolysaccharide (LPS) among Escherichia coli strains and is useful for strain identification and assessing virulence. While the Oβantigen has been chemically well characterized in terms of sugar composition, physical properties such as Oβantigen length of E. coli LPS have not been well studied, even though LPS length is important for determining binding of bacteria to biomolecules and epithelial cells. Atomic force microscopy (AFM) was used to characterize the physicochemical properties of the LPS of eight E. coli strains. Steric repulsion between the AFM tip (silicon nitride) and the E. coli cells was measured and modeled, to determine LPS lengths for three O157 and two O113 E. coli strains, and three control (K12) strains that do not express the Oβantigen. For strains with an Oβantigen, the LPS lengths ranged from 17βΒ±β10 to 37βΒ±β9βnm, and LPS length was positively correlated with the force of adhesion (F~adh~). Longer lengths of LPS may have allowed for more hydrogen bonding between the Oβantigen and silanol groups of the AFM silicon nitride tip, which controlled the magnitude of F~adh~. For control strains, LPS lengths ranged from 3βΒ±β2 to 5βΒ±β3βnm, and there was no relationship between LPS length and adhesion force between the bacterium and the silicon nitride tip. In the absence of the Oβantigen, we attributed F~adh~ to electrostatic interactions with lipids in the bacterial membrane. Copyright Β© 2009 John Wiley & Sons, Ltd.
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