ArticlePloS one2015
Biochemical Characterization and Validation of a Catalytic Site of a Highly Thermostable Ts2631 Endolysin from the Thermus scotoductus Phage vB_Tsc2631.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- Cell-free synthesis and characterization of Salmonella, Escherichia coli, and Shigella-specific bacteriophages.Microbial cell factories · 2026Article
- Human Gut Phageome Analysis Uncovers Thousands of Highly Modular Endolysins.MicrobiologyOpen · 2026Article
- Residue-level determinants of the thermal stability of the extremophilic Ts2631 endolysin.Scientific reports · 2026Article
- Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025Review
- Combined experimental and in silico elucidation of KP27 endolysin reveals a phage derived antibacterial with pH and thermal robustness.Scientific reports · 2025Article
- Characterization of a Peptidoglycan-Degrading Protein: Biochemical and Antimicrobial Characteristics, Antibiotic Synergism, and Delivery System Innovation.Probiotics and antimicrobial proteins · 2025Article
- In Vitro Antibacterial Efficacy of Recombinant Phage-Derived Endolysin LysTAC1 Against Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2025Article
- Enzymatic property and stabilization mechanism of LysBT1, a novel polyextremotolerant endolysin with a C-terminal S-layer homology domain.Applied and environmental microbiology · 2025Article
- Endolysins and membrane-active peptides: innovative engineering strategies against gram-negative bacteria.Frontiers in microbiology · 2025Review
- Characterization of Two Novel Endolysins from Bacteriophage PEF1 and Evaluation of Their Combined Effects on the Control ofAntibiotics (Basel, Switzerland) · 2024Article
- Antimicrobial peptide thanatin fused endolysin PA90 (Tha-PA90) for the control of Acinetobacter baumannii infection in mouse model.Journal of biomedical science · 2024Article
- The antibacterial activity of a novel highly thermostable endolysin, LysKP213, against Gram-negative pathogens is enhanced when combined with outer membrane permeabilizing agents.Frontiers in microbiology · 2024Article
- Functional biology and biotechnology of thermophilic viruses.Essays in biochemistry · 2023Review
- Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods.Applied microbiology and biotechnology · 2023Article
- AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase.Protein science : a publication of the Protein Society · 2023Article
- Article
- Molecular characterization of the PhiKo endolysin fromFrontiers in microbiology · 2023Article
- A Novel Cryptic Clostridial Peptide That Kills Bacteria by a Cell Membrane Permeabilization Mechanism.Microbiology spectrum · 2022Article
- Molecular Characterization of a DNA Polymerase fromInternational journal of molecular sciences · 2022Article
- Bacteriophage Lytic Enzyme P9ly as an Alternative Antibacterial Agent Against Antibiotic-ResistantFrontiers in microbiology · 2022Article
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Authors and funding
14 authors at 9 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phage vB_Tsc2631 infects the extremophilic bacterium Thermus scotoductus MAT2631 and uses the Ts2631 endolysin for the release of its progeny. The Ts2631 endolysin is the first endolysin from thermophilic bacteriophage with an experimentally validated catalytic site. In silico analysis and computational modelling of the Ts2631 endolysin structure revealed a conserved Zn2+ binding site (His30, Tyr58, His131 and Cys139) similar to Zn2+ binding site of eukaryotic peptidoglycan recognition proteins (PGRPs). We have shown that the Ts2631 endolysin lytic activity is dependent on divalent metal ions (Zn2+ and Ca2+). The Ts2631 endolysin substitution variants H30N, Y58F, H131N and C139S dramatically lost their antimicrobial activity, providing evidence for the role of the aforementioned residues in the lytic activity of the enzyme. The enzyme has proven to be not only thermoresistant, retaining 64.8% of its initial activity after 2 h at 95°C, but also highly thermodynamically stable (Tm = 99.82°C, ΔHcal = 4.58 × 10(4) cal mol(-1)). Substitutions of histidine residues (H30N and H131N) and a cysteine residue (C139S) resulted in variants aggregating at temperatures ≥75°C, indicating a significant role of these residues in enzyme thermostability. The substrate spectrum of the Ts2631 endolysin included extremophiles of the genus Thermus but also Gram-negative mesophiles, such as Escherichia coli, Salmonella panama, Pseudomonas fluorescens and Serratia marcescens. The broad substrate spectrum and high thermostability of this endolysin makes it a good candidate for use as an antimicrobial agent to combat Gram-negative pathogens.
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