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赋予细菌细胞壁变异性和适应性的机制。

Mechanisms conferring bacterial cell wall variability and adaptivity.

机构信息

Department of Molecular Biology and Laboratory for Molecular Infection Medicine Sweden, Umeå Centre for Microbial Research, SciLifeLab, Umeå University, Umeå, Sweden.

出版信息

Biochem Soc Trans. 2024 Oct 30;52(5):1981-1993. doi: 10.1042/BST20230027.

DOI:10.1042/BST20230027
PMID:39324635
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11555704/
Abstract

The bacterial cell wall, a sophisticated and dynamic structure predominantly composed of peptidoglycan (PG), plays a pivotal role in bacterial survival and adaptation. Bacteria actively modify their cell walls by editing PG components in response to environmental challenges. Diverse variations in peptide composition, cross-linking patterns, and glycan strand structures empower bacteria to resist antibiotics, evade host immune detection, and adapt to dynamic environments. This review comprehensively summarizes the most common modifications reported to date and their associated adaptive role and further highlights how regulation of PG synthesis and turnover provides resilience to cell lysis.

摘要

细菌细胞壁是一种复杂而动态的结构,主要由肽聚糖(PG)组成,在细菌的生存和适应中起着关键作用。细菌通过编辑 PG 成分来积极地改变细胞壁,以应对环境挑战。肽组成、交联模式和聚糖链结构的多样性使细菌能够抵抗抗生素、逃避宿主免疫检测,并适应动态环境。这篇综述全面总结了迄今为止报道的最常见的修饰及其相关的适应作用,并进一步强调了 PG 合成和周转的调节如何为细胞裂解提供弹性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/f716506750f1/BST-52-1981-g0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/bcf539479a76/BST-52-1981-g0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/895c0ce10b80/BST-52-1981-g0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/f716506750f1/BST-52-1981-g0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/bcf539479a76/BST-52-1981-g0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/895c0ce10b80/BST-52-1981-g0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/de41/11555704/f716506750f1/BST-52-1981-g0003.jpg

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mBio. 2024 Jul 17;15(7):e0141924. doi: 10.1128/mbio.01419-24. Epub 2024 Jun 26.
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A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria.
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Nat Commun. 2024 Feb 13;15(1):1343. doi: 10.1038/s41467-024-45620-5.
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