Evidence map›Paper›PMID 36541811›Full record

ArticleJournal of bacteriology2023

LdtC Is a Key l,d-Transpeptidase for Peptidoglycan Assembly in Mycobacterium smegmatis.

Zanah K Francis, Akeisha N Sanders, Dean C Crick, Sebabrata Mahapatra, M Nurul Islam, Martin S Pavelka

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 51% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026
    Article
  3. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Article
  6. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Zanah K FrancisUniversity of Rochester Medical Center, Department of Microbiology and Immunology, Rochester, New York, USA.
Akeisha N SandersUniversity of Rochester Medical Center, Department of Microbiology and Immunology, Rochester, New York, USA.
Dean C CrickMycobacterial Research Laboratories, Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, Colorado, USA.
Sebabrata MahapatraMycobacterial Research Laboratories, Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, Colorado, USA.
M Nurul IslamMycobacterial Research Laboratories, Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, Colorado, USA.
Martin S PavelkaUniversity of Rochester Medical Center, Department of Microbiology and Immunology, Rochester, New York, USA.ORCID 0000-0003-3265-8555
Colorado State University · USUniversity of Rochester Medical Center · US

Funding

Training in Cellular, Biochemical and Molecular SciencesT32GM068411 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2005 to 2019
$3.9M
Analysis of a novel peptidoglycan assembly pathway in mycobacteriaR01AI139058 · NIAID · UNIVERSITY OF ROCHESTER · PI PAVELKA, MARTIN S. · 2018 to 2022
$2.6M
Training in Microbial PathogenesisT32AI007362 · NIAID · UNIVERSITY OF ROCHESTER · PI IGLEWSKI, BARBARA H. · 1990 to 2010
$2.6M
Assembly of the mycobacterial cell wallR01AI073772 · NIAID · UNIVERSITY OF ROCHESTER · PI PAVELKA, MARTIN S. · 2008 to 2012
$1.9M
NIAID NIH HHS R01 AI073772NIAID NIH HHS R01 AI139058NIAID NIH HHS T32 AI007362NIGMS NIH HHS T32 GM068411
6 · The paper itself

Abstract

The peptidoglycan of mycobacteria has two types of direct cross-links, classical 4-3 cross-links that occur between diaminopimelate (DAP) and alanine residues, and nonclassical 3-3 cross-links that occur between DAP residues on adjacent peptides. The 3-3 cross-links are synthesized by the concerted action of d,d-carboxypeptidases and l,d-transpeptidases (Ldts). Mycobacterial genomes encode several Ldt proteins that can be classified into six classes based upon sequence identity. As a group, the Ldt enzymes are resistant to most β-lactam antibiotics but are susceptible to carbapenem antibiotics, with the exception of LdtC, a class 5 enzyme. In previous work, we showed that loss of LdtC has the greatest effect on the carbapenem susceptibility phenotype of Mycobacterium smegmatis (also known as Mycolicibacterium smegmatis) compared to other

Indexed as

MycobacteriumPeptidyl TransferasesAnti-Bacterial AgentsBacterial ProteinsCarbapenemsCell WallMycobacterium smegmatisPeptidoglycanAnti-Bacterial AgentsBacterial ProteinsCarbapenemsPeptidoglycanPeptidyl Transferasesantibiotic resistancecell walll,d-transpeptidasemycobacteriapeptidoglycan

Identifiers

PMID36541811
PMCPMC9879121
OpenAlexW4312066192

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.