Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell size, morphology, the cytosolic matrix, protein localization, virulence, and resistance to β-lactams.

Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell size, morphology, the cytosolic matrix, protein localization, virulence, and resistance to β-lactams.
复制标题

结核分枝杆菌的非经典转肽酶改变细胞大小、形态、胞质基质、蛋白质定位、毒力和对β-内酰胺的抵抗力。

DOI:
10.1128/jb.01396-13
复制
发表时间:
2014
影响因子:
3.2
通讯作者:
Lamichhane,Gyanu
Lamichhane,Gyanu
中科院分区:
生物学3区
文献类型:
--
作者:
Schoonmaker,MaiaK;Bishai,WilliamR;Lamichhane,Gyanu

文献摘要

相似文献

几乎所有的细菌都有一个肽聚糖层,这对它们的生长和生存至关重要。β-内酰胺类抗生素是人类历史上应用最广泛的一类抗生素,它能抑制d-转肽酶,而d-转肽酶催化肽聚糖生物合成的最后一步。最近报道了另一类转肽酶,即d-转肽酶的存在。结核分枝杆菌是一种引起结核病的传染性病原体,已知它拥有多达5种具有转肽酶活性的蛋白质。在这里,我们首次证明了结核分枝杆菌的1、d转肽酶1和2 (ldtmt1和LdtMt2)的缺失改变了细胞表面形态、形状、大小、细胞内基质的组织、一些靶向膜或分泌的低分子量蛋白质的分选、细胞生理学、生长、毒力以及结核分枝杆菌对阿莫西林-克拉维酸和万古霉素的耐药性。
Virtually all bacteria possess a peptidoglycan layer that is essential for their growth and survival. The β-lactams, the most widely used class of antibiotics in human history, inhibitd,d-transpeptidases, which catalyze the final step in peptidoglycan biosynthesis. The existence of a second class of transpeptidases, thel,d-transpeptidases, was recently reported. Mycobacterium tuberculosis, an infectious pathogen that causes tuberculosis (TB), is known to possess as many as five proteins withl,d-transpeptidase activity. Here, for the first time, we demonstrate that loss ofl,d-transpeptidases 1 and 2 of M. tuberculosis (LdtMt1and LdtMt2) alters cell surface morphology, shape, size, organization of the intracellular matrix, sorting of some low-molecular-weight proteins that are targeted to the membrane or secreted, cellular physiology, growth, virulence, and resistance of M. tuberculosis to amoxicillin-clavulanate and vancomycin.