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.
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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
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发表时间:
2014
影响因子:
3.2
通讯作者:
Lamichhane,Gyanu
中科院分区:
文献类型:
--
作者:
Schoonmaker,MaiaK;Bishai,WilliamR;Lamichhane,Gyanu
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.