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利用基因敲除突变体研究[具体对象]与非生物表面的粘附

Using Knock-Out Mutants to Investigate the Adhesion of to Abiotic Surfaces.

作者信息

Spengler Christian, Nolle Friederike, Thewes Nicolas, Wieland Ben, Jung Philipp, Bischoff Markus, Jacobs Karin

机构信息

Experimental Physics and Center for Biophysics, Saarland University, 66123 Saarbrücken, Germany.

Institute of Medical Microbiology and Hygiene and Center for Biophysics, Saarland University, 66421 Homburg, Germany.

出版信息

Int J Mol Sci. 2021 Nov 4;22(21):11952. doi: 10.3390/ijms222111952.

DOI:10.3390/ijms222111952
PMID:34769382
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8584566/
Abstract

The adhesion of to abiotic surfaces is crucial for establishing device-related infections. With a high number of single-cell force spectroscopy measurements with genetically modified cells, this study provides insights into the adhesion process of the pathogen to abiotic surfaces of different wettability. Our results show that utilizes different cell wall molecules and interaction mechanisms when binding to hydrophobic and hydrophilic surfaces. We found that covalently bound cell wall proteins strongly interact with hydrophobic substrates, while their contribution to the overall adhesion force is smaller on hydrophilic substrates. Teichoic acids promote adhesion to hydrophobic surfaces as well as to hydrophilic surfaces. This, however, is to a lesser extent. An interplay of electrostatic effects of charges and protein composition on bacterial surfaces is predominant on hydrophilic surfaces, while it is overshadowed on hydrophobic surfaces by the influence of the high number of binding proteins. Our results can help to design new models of bacterial adhesion and may be used to interpret the adhesion of other microorganisms with similar surface properties.

摘要

[病原体名称]对非生物表面的粘附对于引发与器械相关的感染至关重要。通过对经过基因改造的[病原体名称]细胞进行大量单细胞力谱测量,本研究深入了解了该病原体对不同润湿性非生物表面的粘附过程。我们的结果表明,[病原体名称]在与疏水和亲水表面结合时利用了不同的细胞壁分子和相互作用机制。我们发现,共价结合的细胞壁蛋白与疏水底物强烈相互作用,而它们对整体粘附力的贡献在亲水底物上较小。磷壁酸促进对疏水表面以及亲水表面的粘附。然而,程度较小。电荷的静电效应与细菌表面蛋白质组成之间的相互作用在亲水表面上占主导地位,而在疏水表面上,大量结合蛋白的影响使其黯然失色。我们的结果有助于设计新的细菌粘附模型,并可用于解释具有相似表面特性的其他微生物的粘附。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/9b39e7510b15/ijms-22-11952-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/0d727fa3ba54/ijms-22-11952-g0A1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/0ae5a966bda4/ijms-22-11952-g0A2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/7238c20e93c5/ijms-22-11952-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/697edefbce8c/ijms-22-11952-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/cb1629debe6f/ijms-22-11952-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/9b39e7510b15/ijms-22-11952-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/0d727fa3ba54/ijms-22-11952-g0A1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/0ae5a966bda4/ijms-22-11952-g0A2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/7238c20e93c5/ijms-22-11952-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/697edefbce8c/ijms-22-11952-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/cb1629debe6f/ijms-22-11952-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c01/8584566/9b39e7510b15/ijms-22-11952-g004.jpg

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Different binding mechanisms of Staphylococcus aureus to hydrophobic and hydrophilic surfaces.
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