Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape

Elife. 2018 Oct 16:7:e37516. doi: 10.7554/eLife.37516.

Abstract

In most well-studied rod-shaped bacteria, peptidoglycan is primarily crosslinked by penicillin-binding proteins (PBPs). However, in mycobacteria, crosslinks formed by L,D-transpeptidases (LDTs) are highly abundant. To elucidate the role of these unusual crosslinks, we characterized Mycobacterium smegmatis cells lacking all LDTs. We find that crosslinks generate by LDTs are required for rod shape maintenance specifically at sites of aging cell wall, a byproduct of polar elongation. Asymmetric polar growth leads to a non-uniform distribution of these two types of crosslinks in a single cell. Consequently, in the absence of LDT-mediated crosslinks, PBP-catalyzed crosslinks become more important. Because of this, Mycobacterium tuberculosis (Mtb) is more rapidly killed using a combination of drugs capable of PBP- and LDT- inhibition. Thus, knowledge about the spatial and genetic relationship between drug targets can be exploited to more effectively treat this pathogen.

Keywords: Mycobacterium smegmatis; Mycobacterium tuberculosis; infectious disease; microbiology; peptidoglycan; polar growth; rod shape maintenance.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / metabolism
  • Aminoacyltransferases / metabolism
  • Amoxicillin / pharmacology
  • Bacillus / metabolism
  • Cell Wall / metabolism
  • Cross-Linking Reagents / metabolism*
  • Escherichia coli / metabolism
  • Fluorescence
  • Kinetics
  • Meropenem / pharmacology
  • Microbial Viability
  • Models, Biological
  • Mycobacterium smegmatis / drug effects
  • Mycobacterium smegmatis / metabolism*
  • Penicillin-Binding Proteins / metabolism
  • Peptidoglycan / chemistry
  • Peptidoglycan / metabolism*

Substances

  • Amino Acids
  • Cross-Linking Reagents
  • Penicillin-Binding Proteins
  • Peptidoglycan
  • Amoxicillin
  • Aminoacyltransferases
  • peptidoglycan transpeptidase
  • Meropenem