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Correction: Coulter et al. OrgTRx: A Platform Developed in Queensland for the Extraction and Visualisation of Antimicrobial Susceptibility Data for the Surveillance of Resistance in Microorganisms. <i>Antibiotics</i> 2026, <i>15</i>, 63.

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Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics
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Peptidoglycan LD-Transpeptidases.

Samuel Gastrell1, Waldemar Vollmer1

  • 1Centre for Superbug Solutions, Institute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia.

Antibiotics (Basel, Switzerland)
|December 30, 2025
PubMed
Summary
This summary is machine-generated.

LD-transpeptidases (LDTs) are crucial bacterial enzymes, essential for pathogen survival and β-lactam resistance. Targeting LDTs offers a promising strategy for developing new antibiotic treatments against resistant bacteria.

Keywords:
LD-transpeptidaseantibacterialsbacteriacell envelopepeptidoglycanresistanceβ-lactam

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Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • LD-transpeptidases (LDTs) are conserved bacterial enzymes involved in peptidoglycan (PG) crosslinking, often acting secondary to penicillin-binding proteins (PBPs).
  • LDTs are critical in pathogens like *Clostridioides difficile* and confer β-lactam resistance in *Mycobacterium tuberculosis* and *Enterococcus faecium* due to their low affinity for common antibiotics.
  • Their ability to form LD-crosslinks when PBPs are inhibited makes LDTs attractive therapeutic targets.

Purpose of the Study:

  • To elucidate the diverse enzymatic functions and roles of LD-transpeptidases in bacterial cell wall synthesis and integrity.
  • To explore the potential of LDTs as targets for novel antibiotic development against resistant pathogens.
  • To investigate recent discoveries, including new LDT subgroups, to expand research into PG synthesis and modification.

Main Methods:

  • Comparative analysis of LDT sequences and structures.
  • Enzymatic assays to characterize LDT activity (e.g., crosslinking, D-amino acid incorporation).
  • Investigating the role of LDTs in cell envelope integrity and virulence in various bacterial species.

Main Results:

  • LDTs reinforce PG via 3,3-LD- or 1,3-LD-crosslinks, particularly under stress conditions.
  • Some LDTs incorporate non-canonical D-amino acids into PG.
  • Specialized LDTs in Gram-negative bacteria are involved in tethering outer membrane proteins and regulating virulence.

Conclusions:

  • LD-transpeptidases play multifaceted roles beyond simple PG crosslinking, including stress response and cell envelope maintenance.
  • The identification of novel LDT families (e.g., VanW) and subgroups expands the understanding of their diversity and function.
  • Targeting LDTs presents a viable strategy for combating antibiotic resistance and developing new antimicrobial therapies.