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首页> 外文期刊>MBio >Class A Penicillin-Binding Protein-Mediated Cell Wall Synthesis Promotes Structural Integrity during Peptidoglycan Endopeptidase Insufficiency in Vibrio cholerae
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Class A Penicillin-Binding Protein-Mediated Cell Wall Synthesis Promotes Structural Integrity during Peptidoglycan Endopeptidase Insufficiency in Vibrio cholerae

机译：A类Pencillin结合蛋白介导的细胞壁合成促进肽聚糖内肽酶内肽酶的结构完整性<命名含量含量型=“属型”>弧菌霍乱

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Synthesis and turnover of the bacterial cell wall must be tightly coordinated to avoid structural integrity failure and cell death. Details of this coordination are poorly understood, particularly if and how cell wall turnover enzymes are required for the activity of the different cell wall synthesis machines, the aPBPs and the Rod system. ABSTRACT The bacterial cell wall is composed primarily of peptidoglycan (PG), a poly-aminosugar that is essential to sustain cell shape, growth, and structural integrity. PG is synthesized by class A/B penicillin-binding proteins (a/bPBPs) and shape, elongation, division, and sporulation (SEDS) proteins like RodA (as part of the Rod system cell elongation machinery) and degraded by “autolytic” enzymes to accommodate growth processes. It is thought that autolysins (particularly endopeptidases [EPs]) are required for PG synthesis and incorporation by creating gaps that are patched and paved by PG synthases, but the exact relationship between autolysins and PG synthesis remains incompletely understood. Here, we have probed the consequences of EP depletion for PG synthesis in the diarrheal pathogen Vibrio cholerae . We found that EP depletion resulted in severe morphological and division defects, but these cells continued to increase in mass and aberrantly incorporated new cell wall material. Mass increase proceeded in the presence of Rod system inhibitors, but cells lysed upon inhibition of aPBPs, suggesting that aPBPs are required for structural integrity under these conditions. The Rod system, although not essential for the observed mass increase, remained functional even after prolonged EP depletion. Last, heterologous expression of an EP from Neisseria gonorrhoeae fully complemented growth and morphology of an EP-insufficient V. cholerae , highlighting the possibility that the PG synthases may not necessarily function via direct interaction with EPs. Overall, our findings suggest that during EP insufficiency in V. cholerae , aPBPs become essential for structural integrity while the Rod system is unable to promote proper cell expansion.
机译：必须紧密地协调细菌细胞壁的合成和换档，以避免结构完整性衰竭和细胞死亡。这种协调的细节较差地理解，特别是如果需要如何以及如何以及如何为不同的细胞壁合成机器，APBP和杆系统的活性所需的。摘要细菌细胞壁主要由肽聚糖（PG）组成，该聚氨酯蛋白是维持细胞形状，生长和结构完整性至关重要的。 Pg通过类A / B青霉素结合蛋白（A / BPBP）和形状，伸长，分裂和孢子（SED）蛋白（如棒子系统电池伸长机械的一部分）合成，并通过“自变性”酶降解适应增长过程。据认为，PG合成和通过产生由PG合成酶铺设和铺设的间隙来掺入的自溶蛋白（特别是内肽酶[EPS]），但是自溶解素和PG合成之间的确切关系仍然不完全理解。在这里，我们探讨了EP耗尽对腹泻病原体Vibrio Cholerae的PG合成的后果。我们发现EP耗尽导致严重的形态和分裂缺陷，但这些细胞继续增加质量和异常掺入新的细胞壁材料。在棒系统抑制剂存在下进行质量增加，但在抑制APBPS时裂解的细胞，表明在这些条件下需要APBP来进行结构完整性。棒系统，虽然对于观察到的质量增加不是必需的，但即使在长期EP耗尽后，即使在延长的EP耗尽之后也仍然是官能的。最后，EP的异源表达来自Neisseria淋病淋病的完全补充了EP-Insuffie V.霍乱的生长和形态，突出了PG合成酶可能不一定通过与EPS直接相互作用来函数的可能性。总体而言，我们的研究结果表明，在V.霍乱的空气不足期间，APBPS对结构完整性至关重要，而杆系统无法促进适当的细胞扩张。

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