ArticleApplied and environmental microbiology2014
Novel highly thermostable endolysin from Thermus scotoductus MAT2119 bacteriophage Ph2119 with amino acid sequence similarity to eukaryotic peptidoglycan recognition proteins.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 55 citations in OpenAlex.
- Residue-level determinants of the thermal stability of the extremophilic Ts2631 endolysin.Scientific reports · 2026Article
- Bacteriophages and Their Enzymes: Allies Against Microbial Biofilms.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Enzymatic property and stabilization mechanism of LysBT1, a novel polyextremotolerant endolysin with a C-terminal S-layer homology domain.Applied and environmental microbiology · 2025Article
- Deep eutectic solvent enhances antibacterial activity of a modular lytic enzyme against Acinetobacter baumannii.Scientific reports · 2025Article
- Characterization of a Thermostable Endolysin of theViruses · 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
- AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase.Protein science : a publication of the Protein Society · 2023Article
- 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
- Cloning and Characterization of a Thermostable Endolysin of Bacteriophage TP-84 as a Potential Disinfectant and Biofilm-Removing Biological Agent.International journal of molecular sciences · 2022Article
- Antimicrobial Potential of the GeneraAntibiotics (Basel, Switzerland) · 2022Review
- Characterization and Genomic Analysis of a Novel Jumbo Bacteriophage vB_StaM_SA1 InfectingFrontiers in microbiology · 2022Article
- Current Status of Endolysin-Based Treatments against Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2021Review
- Novel Lytic Enzyme of Prophage Origin fromInternational journal of molecular sciences · 2021Article
- MMPphg from the thermophilic Meiothermus bacteriophage MMP17 as a potential antimicrobial agent against both Gram-negative and Gram-positive bacteria.Virology journal · 2020Article
- Molecular Characterization of a Novel Lytic Enzyme LysC fromInternational journal of molecular sciences · 2020Article
- Ts2631 Endolysin from the ExtremophilicViruses · 2019Article
- Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding.Scientific reports · 2019Article
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we present the discovery and characterization of a highly thermostable endolysin from bacteriophage Ph2119 infecting Thermus strain MAT2119 isolated from geothermal areas in Iceland. Nucleotide sequence analysis of the 16S rRNA gene affiliated the strain with the species Thermus scotoductus. Bioinformatics analysis has allowed identification in the genome of phage 2119 of an open reading frame (468 bp in length) coding for a 155-amino-acid basic protein with an Mr of 17,555. Ph2119 endolysin does not resemble any known thermophilic phage lytic enzymes. Instead, it has conserved amino acid residues (His(30), Tyr(58), His(132), and Cys(140)) that form a Zn(2+) binding site characteristic of T3 and T7 lysozymes, as well as eukaryotic peptidoglycan recognition proteins, which directly bind to, but also may destroy, bacterial peptidoglycan. The purified enzyme shows high lytic activity toward thermophiles, i.e., T. scotoductus (100%), Thermus thermophilus (100%), and Thermus flavus (99%), and also, to a lesser extent, toward mesophilic Gram-negative bacteria, i.e., Escherichia coli (34%), Serratia marcescens (28%), Pseudomonas fluorescens (13%), and Salmonella enterica serovar Panama (10%). The enzyme has shown no activity against a number of Gram-positive bacteria analyzed, with the exception of Deinococcus radiodurans (25%) and Bacillus cereus (15%). Ph2119 endolysin was found to be highly thermostable: it retains approximately 87% of its lytic activity after 6 h of incubation at 95°C. The optimum temperature range for the enzyme activity is 50°C to 78°C. The enzyme exhibits lytic activity in the pH range of 6 to 10 (maximum at pH 7.5 to 8.0) and is also active in the presence of up to 500 mM NaCl.
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