Peptidoglycan, found within the cell wall of bacteria, is a structure critical for maintaining cell morphology and providing a protective barrier in diverse environments. Peptidoglycan is a remarkably dynamic structure that is constantly remodeled during cell growth and division by various peptidoglycan enzymes. Numerous peptidoglycan enzymes have been characterized from diverse bacteria and are highly sought after as targets for therapeutics. However, very little is known about these enzymes within the biothreat agent . As the causative agent of tularemia, is classified as a category A biothreat pathogen, in part due to its low infectious dose and lack of FDA-approved vaccine. Many bacterial species encode multiple peptidoglycan enzymes with redundant functions that allow for compensation if one of the enzymes are inactivated. In contrast, appears to lack this redundancy, indicating peptidoglycan enzymes may be completely essential for growth and could be exploited as targets for medical countermeasures. Indeed, several peptidoglycan enzymes in have been shown to play important roles in cell division, cell morphology, virulence, and modulation of host response. The aim of this review is to summarize findings from the current literature on peptidoglycan enzymes present in and discuss areas where future research efforts might be directed. We conclude that harbors a distinct set of peptidoglycan enzymes important for cell growth and virulence and represent potentially valuable targets for the development of novel therapeutics.
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http://dx.doi.org/10.3389/fmicb.2022.1099312 | DOI Listing |
Comb Chem High Throughput Screen
January 2025
Department of Chemistry, Faculty of Mathematics and Natural Science, Universitas Padjadjaran, Sumedang, Indonesia.
Background: Dental root canal failure is a disease caused by gram-positive bacteria, Enterococcus faecalis. The disease is caused by the bacterial cell wall consisting of a peptidoglycan layer that protects the bacteria from internal osmotic pressure. Peptidoglycan biosynthesis includes many enzymes, such as MurA, Penicillin-binding protein (PBP), and SrtA.
View Article and Find Full Text PDFVirulence
December 2025
National Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, China.
The emergence of antibiotic-resistant bacteria has attracted interest in the field of endolysins. Here, we analyzed the diversity of endolysins and identified a new endolysin, Ply2741, that exhibited broad-spectrum bactericidal activity. Our results demonstrated that Ply2741 could effectively eradicate multidrug-resistant gram-positive pathogens and .
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Key Laboratory of Feed Biotechnology of the Ministry of Agriculture and Rural Affairs, Risk Assessment Laboratory of Animal Product Quality Safety Feed Source Factors of the Ministry of Agriculture and Rural Affairs, Institute of Feed Research of Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Peptidoglycan (PGN) is a unique component of prokaryotic cell walls with immune-enhancing capacities. Here, we extracted PGN from , a by-product of amino acid fermentation, using the trichloroacetic acid (TCA) method. SDS-PAGE analysis confirmed the presence of PGN, with a band of approximately 28 kDa.
View Article and Find Full Text PDFFish Shellfish Immunol
January 2025
School of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding, 071002, China; Institute of Life Science and Green Development, Hebei University, Baoding, 071002, China. Electronic address:
This study investigates an L-type lectin, NdLTL1, derived from Neocaridina denticulata sinensis, emphasizing its role in immune defense through carbohydrate binding and bacterial agglutination. Bioinformatics analysis identified 179 lectin sequences, leading to subsequent investigations into the structure and function of NdLTL1. The open reading frame (ORF) of NdLTL1 spans 966 bp and encodes a protein consisting of 321 amino acids (36.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Center of Infectious Diseases, Division of Infectious Diseases in State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China. Electronic address:
Archaeal peptidoglycan, a crucial component of the cell walls of Methanobacteria and Methanopyri, enhances the tightness of methanogenic cells and their resistance to known lytic enzymes and antibiotics. Although archaeal peptidoglycan endoisopeptidases (Pei) can reportedly degrade archaeal peptidoglycan, their biochemistry is still largely unknown. In this study, we investigated the activity and catalytic properties of the endoisopeptidases PeiW and PeiP using synthesized isopeptides identical to natural substrates.
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