ReviewFrontiers in microbiology2022
One fold, many functions-M23 family of peptidoglycan hydrolases.
Review in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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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.
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Who cites it
37 citing papers in PubMed, 44 citations in OpenAlex.
- Isolation and genomic characterization of a Teetrevirus phage infecting Klebsiella quasipneumoniae with a putative SAMase gene.Archives of virology · 2026Article
- Jestvirus, a Novel Genus in the Family Autotranscriptaviridae Infecting Aeromonas.Current microbiology · 2026Article
- Bactofilins are essential spatial organizers of peptidoglycan insertion in the Lyme disease spirocheteJournal of bacteriology · 2026Article
- Genomic and Phenotypic Characterization of Avian-DerivedAnimals : an open access journal from MDPI · 2026Article
- Peculiarities of the Interaction of the Bacteriolytic Protease Blp fromInternational journal of molecular sciences · 2026Article
- Novel endopeptidase overcoming lysostaphin resistance.Scientific reports · 2026Article
- The Factors Involved in Plant-Insect-Microbe Interactions Expanded: Genome Analysis and Description of Frigoribacterium adelgis sp. nov.Environmental microbiology reports · 2026Article
- Enzyme therapy as a promising strategy to overcome multi-drug resistance in pathogens: current advances, key challenges, and future directions.RSC advances · 2026Review
- The innate immune protein calprotectin ablates the bactericidal activity of β-lactam antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Enhancing stability and safety of chimeric peptidoglycan hydrolases by linker engineering.Applied microbiology and biotechnology · 2026Article
- Phage enabled precision drug delivery: dual function platforms for therapeutics and genetic cargo transport.Frontiers in microbiology · 2026Review
- Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026Article
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- Enhanced efficiency of virulent and temperate phage combination mediated through bacterial membrane vesicles.Journal of virology · 2025Article
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- Secreted LysM proteins are required for niche competition and full virulence in Pseudomonas savastanoi during host plant infection.PLoS pathogens · 2025Article
- Antibacterial activity of green-synthesized silver nanoparticles against Gram-negative bacteria and insights into potential resistance mechanisms.INNOSC theranostics & pharmacological sciences · 2025Article
- An antibiotic-free antimicrobial combination of bacteriocins and a peptidoglycan hydrolase:Applied and environmental microbiology · 2025Article
- The innate immune protein calprotectin incapacitates the bactericidal activity of β-lactam antibiotics.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cell walls are the guards of cell integrity. They are composed of peptidoglycan that provides rigidity to sustain internal turgor and ensures isolation from the external environment. In addition, they harbor the enzymatic machinery to secure cell wall modulations needed throughout the bacterial lifespan. The main players in this process are peptidoglycan hydrolases, a large group of enzymes with diverse specificities and different mechanisms of action. They are commonly, but not exclusively, found in prokaryotes. Although in most cases, these enzymes share the same molecular function, namely peptidoglycan hydrolysis, they are leveraged to perform a variety of physiological roles. A well-investigated family of peptidoglycan hydrolases is M23 peptidases, which display a very conserved fold, but their spectrum of lytic action is broad and includes both Gram- positive and Gram- negative bacteria. In this review, we summarize the structural, biochemical, and functional studies concerning the M23 family of peptidases based on literature and complement this knowledge by performing large-scale analyses of available protein sequences. This review has led us to gain new insight into the role of surface charge in the activity of this group of enzymes. We present relevant conclusions drawn from the analysis of available structures and indicate the main structural features that play a crucial role in specificity determination and mechanisms of latency. Our work systematizes the knowledge of the M23 family enzymes in the context of their unique antimicrobial potential against drug-resistant pathogens and presents possibilities to modulate and engineer their features to develop perfect antibacterial weapons.
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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.