ArticleScientific reports2015
Substrate recognition and catalysis by LytB, a pneumococcal peptidoglycan hydrolase involved in virulence.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- Label-free microscopy enables high-throughput identification of genes controlling biofilm development.bioRxiv : the preprint server for biology · 2025Article
- Structure, Function, and Regulation of LytA: TheMicroorganisms · 2025Review
- Article
- Inhibition ofMicrobiology (Reading, England) · 2022Article
- TheApplied and environmental microbiology · 2020Article
- Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis.Communications biology · 2020Article
- Cyclic-di-GMP Regulates Autoaggregation Through the Putative Peptidoglycan Hydrolase, EagA, and Regulates Transcription of theFrontiers in microbiology · 2020Article
- Tackling Multidrug Resistance in Streptococci - From Novel Biotherapeutic Strategies to Nanomedicines.Frontiers in microbiology · 2020Review
- The Cell Wall ofMicrobiology spectrum · 2019Review
- Antibiotic-Induced Cell Chaining Triggers Pneumococcal Competence by Reshaping Quorum Sensing to Autocrine-Like Signaling.Cell reports · 2018Article
- Applications of bacteriophages versus phage enzymes to combat and cure bacterial infections: an ambitious and also a realistic application?Applied microbiology and biotechnology · 2018Review
- PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae.Nature microbiology · 2018Article
- Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.Scientific reports · 2017Article
- Bacterial size matters: Multiple mechanisms controlling septum cleavage and diplococcus formation are critical for the virulence of the opportunistic pathogen Enterococcus faecalis.PLoS pathogens · 2017Article
- Modular Architecture and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L (CbpL) Contributing to Pneumococcal Pathogenesis.Scientific reports · 2016Article
- Choline Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New Antimicrobials.Antibiotics (Basel, Switzerland) · 2016Review
- The Streptococcus pneumoniae pezAT Toxin-Antitoxin System Reduces β-Lactam Resistance and Genetic Competence.Frontiers in microbiology · 2016Article
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Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
Abstract
Streptococcus pneumoniae is a major cause of life-threatening diseases worldwide. Here we provide an in-depth functional characterization of LytB, the peptidoglycan hydrolase responsible for physical separation of daughter cells. Identified herein as an N-acetylglucosaminidase, LytB is involved also in colonization and invasion of the nasopharynx, biofilm formation and evasion of host immunity as previously demonstrated. We have shown that LytB cleaves the GlcNAc-β-(1,4)-MurNAc glycosidic bond of peptidoglycan building units. The hydrolysis occurs at sites with fully acetylated GlcNAc moieties, with preference for uncross-linked muropeptides. The necessity of GlcN acetylation and the presence of a single acidic moiety (Glu585) essential for catalysis strongly suggest a substrate-assisted mechanism with anchimeric assistance of the acetamido group of GlcNAc moieties. Additionally, modelling of the catalytic region bound to a hexasaccharide tripentapeptide provided insights into substrate-binding subsites and peptidoglycan recognition. Besides, cell-wall digestion products and solubilisation rates might indicate a tight control of LytB activity to prevent unrestrained breakdown of the cell wall. Choline-independent localization at the poles of the cell, mediated by the choline-binding domain, peptidoglycan modification, and choline-mediated (lipo)teichoic-acid attachment contribute to the high selectivity of LytB. Moreover, so far unknown chitin hydrolase and glycosyltransferase activities were detected using GlcNAc oligomers as substrate.
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Registered trials
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.