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

Maia K. Schoonmaker, William R. Bishai, Gyanu Lamichhanea

Research output: Contribution to journalArticlepeer-review

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 (LdtMt1 and 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.

Original languageEnglish (US)
Pages (from-to)1394-1402
Number of pages9
JournalJournal of bacteriology
Volume196
Issue number7
DOIs
StatePublished - Apr 2014

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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