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一种多糖脱乙酰酶可增强细菌在高离子强度环境中的黏附能力。

A polysaccharide deacetylase enhances bacterial adhesion in high-ionic-strength environments.

作者信息

Chepkwony Nelson K, Brun Yves V

机构信息

Département de microbiologie, infectiologie et immunologie, Université de Montréal, C.P. 6128, succ. Centre-ville, Montréal, QC H3C 3J7, Canada.

出版信息

iScience. 2021 Sep 2;24(9):103071. doi: 10.1016/j.isci.2021.103071. eCollection 2021 Sep 24.

Abstract

Differences in ionic strength, pH, temperature, shear forces, and other environmental factors impact adhesion, and organisms have evolved various strategies to optimize their adhesins for their specific environmental conditions. Many species of Alphaproteobacteria, including members of the order Caulobacterales, use a polar adhesin, called holdfast, for surface attachment and subsequent biofilm formation in both freshwater and marine environments. a marine member of Caulobacterales, produces a holdfast adhesin that tolerates a drastically higher ionic strength than the holdfast produced by its freshwater relative, . In this work, we show that the holdfast polysaccharide deacetylase HfsH plays an important role in adherence in high-ionic-strength environments. We show that increasing expression of HfsH improves holdfast binding in high-ionic-strength environments. We conclude that HfsH plays a role in modulating holdfast binding at high ionic strength and hypothesize that this modulation occurs through varied deacetylation of holdfast polysaccharides.

摘要

离子强度、pH值、温度、剪切力和其他环境因素的差异会影响黏附作用,生物体已经进化出各种策略来针对其特定环境条件优化它们的黏附素。许多α-变形菌纲物种,包括柄杆菌目成员,在淡水和海洋环境中都使用一种称为固着器的极性黏附素来进行表面附着及随后的生物膜形成。柄杆菌目的一个海洋成员产生一种固着器黏附素,其耐受的离子强度比其淡水近亲产生的固着器要高得多。在这项研究中,我们表明固着器多糖脱乙酰酶HfsH在高离子强度环境中的黏附中起重要作用。我们发现增加HfsH的表达可改善在高离子强度环境中的固着器结合。我们得出结论,HfsH在高离子强度下调节固着器结合中发挥作用,并推测这种调节是通过固着器多糖的不同脱乙酰化作用发生的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0a0d/8449245/ab31604e15cb/fx1.jpg

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