ArticleScientific reports2017
Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 45 citations in OpenAlex.
- Designing the Next Generation of Endolysins: A Triple Strategy Integrating Bioinformatics Mining, Engineering Modification and Encapsulation Formulation.Probiotics and antimicrobial proteins · 2026Review
- Search for effective bacteriolytic enzymes and their combinations for the treatment of polymicrobial biofilm-associated infections.World journal of microbiology & biotechnology · 2026Article
- Investigation of Recombinantly Produced Endolysins Reveals a Modular Enzyme Shared by Several Enterobacteria Phages to Exhibit Broad-Range Lytic Activity Against Different Orders of Gammaproteobacteria.MicrobiologyOpen · 2026Article
- Bacteriophage lysins: a promising strategy for combating foodborne pathogens in food safety.Frontiers in microbiology · 2026Review
- Phage endolysins as alternative antimicrobials: mechanisms, clinical progress, and emerging resistance frameworks.Frontiers in microbiology · 2026Review
- Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025Review
- Discovery of potent endolysins against Pseudomonas aeruginosa and other gram-negative ESKAPE pathogens by an agar-based screening method.Scientific reports · 2025Article
- Phage and Endolysin Therapy Against Antibiotics Resistant Bacteria: From Bench to Bedside.MedComm · 2025Review
- The Unique Capability of Endolysin to Tackle Antibiotic Resistance: Cracking the Barrier.Journal of xenobiotics · 2025Review
- Molecular Docking of Endolysins for Studying Peptidoglycan Binding Mechanism.Molecules (Basel, Switzerland) · 2024Article
- Bacteriophage as a potential biotherapeutics to combat present-day crisis of multi-drug resistant pathogens.Heliyon · 2024Review
- Decoding the Structure-Function Relationship of the Muramidase Domain in E. coli O157.H7 Bacteriophage Endolysin: A Potential Building Block for Chimeric Enzybiotics.The protein journal · 2024Article
- Engineering strategies and challenges of endolysin as an antibacterial agent against Gram-negative bacteria.Microbial biotechnology · 2024Review
- Antibacterial synergy between a phage endolysin and citric acid against the Gram-negative kiwifruit pathogenApplied and environmental microbiology · 2024Article
- Phage therapy to treat cystic fibrosisFrontiers in microbiology · 2024Review
- LysP53 activity against Salmonella and its application in decontamination of Salmonella on fresh romaine lettuce.Applied microbiology and biotechnology · 2023Article
- What's in a Name? An Overview of the Proliferating Nomenclature in the Field of Phage Lysins.Cells · 2023Review
- Beyond antibiotics: phage-encoded lysins against Gram-negative pathogens.Frontiers in microbiology · 2023Review
- The l,d-Transpeptidase LdtACS infectious diseases · 2022Article
- Monomodular Pseudomonas aeruginosa phage JG004 lysozyme (Pae87) contains a bacterial surface-active antimicrobial peptide-like region and a possible substrate-binding subdomain.Acta crystallographica. Section D, Structural biology · 2022Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endolysins are peptidoglycan-degrading enzymes utilized by bacteriophages to release the progeny from bacterial cells. The lytic properties of phage endolysins make them potential antibacterial agents for medical and industrial applications. Here, we present a comprehensive characterization of phage AP3 modular endolysin (AP3gp15) containing cell wall binding domain and an enzymatic domain (DUF3380 by BLASTP), both widespread and conservative. Our structural analysis demonstrates the low similarity of an enzymatic domain to known lysozymes and an unusual catalytic centre characterized by only a single glutamic acid residue and no aspartic acid. Thus, our findings suggest distinguishing a novel class of muralytic enzymes having the activity and catalytic centre organization of DUF3380. The lack of amino acid sequence homology between AP3gp15 and other known muralytic enzymes may reflect the evolutionary convergence of analogous glycosidases. Moreover, the broad antibacterial spectrum, lack of cytotoxic effect on human cells and the stability characteristics of AP3 endolysin advocate for its future application development.
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