Affiliation:
1. Division of Infectious Diseases, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
2. Howard Hughes Medical Institute, Center for Tuberculosis Research, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
3. Taskforce To Study Resistance Emergence & Antibiotic Discovery Technology, Johns Hopkins University, Baltimore, Maryland, USA
Abstract
ABSTRACT
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, inhibit
d,d
-transpeptidases, which catalyze the final step in peptidoglycan biosynthesis. The existence of a second class of transpeptidases, the
l,d
-transpeptidases, was recently reported.
Mycobacterium tuberculosis
, an infectious pathogen that causes tuberculosis (TB), is known to possess as many as five proteins with
l,d
-transpeptidase activity. Here, for the first time, we demonstrate that loss of
l,d
-transpeptidases 1 and 2 of
M. tuberculosis
(Ldt
Mt1
and Ldt
Mt2
) 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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
80 articles.
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