ArticlePLoS pathogens2014
Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 96 citations in OpenAlex.
- Phage endolysins as alternative antimicrobials: mechanisms, clinical progress, and emerging resistance frameworks.Frontiers in microbiology · 2026Review
- Prophage landscapes in clinical MRSA: safety profiling and discovery of Lys81, a broad-spectrum bacteriolytic enzyme.Frontiers in microbiology · 2026Article
- Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025Review
- Structural and functional analysis reveals the catalytic mechanism and substrate binding mode of the broad-spectrum endolysin Ply2741.Virulence · 2025Article
- Next-generation antimicrobials: A review of phage lysins as precision weapons against drug-resistant pathogens.Virulence · 2025Review
- Detection of Staphylococcus aureus via IgY-based immunomagnetic separation and a phage lysin LysGH15-based colloidal gold immunochromatographic assay.Journal of advanced research · 2025Article
- Bacteriophage Power: Next-Gen Biocontrol Strategies for Safer Meat.Molecules (Basel, Switzerland) · 2025Review
- Characterization and therapeutic potential of newly isolated bacteriophages againstJournal of virology · 2025Article
- Development of a novel chimeric lysin to combine parental phage lysin and cefquinome for preventing sow endometritis after artificial insemination.Veterinary research · 2025Article
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Endolysin EN572-5 as an alternative to treat urinary tract infection caused by Streptococcus agalactiae.Applied microbiology and biotechnology · 2024Article
- Biological characterization of the phage lysin AVPL and its efficiency againstApplied and environmental microbiology · 2024Article
- Prediction of key amino acids of Salmonella phage endolysin LysST-3 and detection of its mutants' activity.Archives of microbiology · 2024Article
- Cellular and Enzymatic Determinants Impacting the Exolytic Action of an Anti-Staphylococcal Enzybiotic.International journal of molecular sciences · 2023Article
- Article
- Structural biology and functional features of phage-derived depolymerase Depo32 onMicrobiology spectrum · 2023Article
- Structural and biochemical insights into the bacteriophage PlyGRCS endolysin targeting methicillin-resistant Staphylococcus aureus (MRSA) and serendipitous discovery of its interaction with a cold shock protein C (CspC).Protein science : a publication of the Protein Society · 2023Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- PlyKp104, a Novel Phage Lysin for the Treatment of Klebsiella pneumoniae, Pseudomonas aeruginosa, and Other Gram-Negative ESKAPE Pathogens.Antimicrobial agents and chemotherapy · 2023Article
- Structural and functional features of a broad-spectrum prophage-encoded enzybiotic from Enterococcus faecium.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
19 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lysin LysGH15, which is derived from the staphylococcal phage GH15, demonstrates a wide lytic spectrum and strong lytic activity against methicillin-resistant Staphylococcus aureus (MRSA). Here, we find that the lytic activity of the full-length LysGH15 and its CHAP domain is dependent on calcium ions. To elucidate the molecular mechanism, the structures of three individual domains of LysGH15 were determined. Unexpectedly, the crystal structure of the LysGH15 CHAP domain reveals an "EF-hand-like" calcium-binding site near the Cys-His-Glu-Asn quartet active site groove. To date, the calcium-binding site in the LysGH15 CHAP domain is unique among homologous proteins, and it represents the first reported calcium-binding site in the CHAP family. More importantly, the calcium ion plays an important role as a switch that modulates the CHAP domain between the active and inactive states. Structure-guided mutagenesis of the amidase-2 domain reveals that both the zinc ion and E282 are required in catalysis and enable us to propose a catalytic mechanism. Nuclear magnetic resonance (NMR) spectroscopy and titration-guided mutagenesis identify residues (e.g., N404, Y406, G407, and T408) in the SH3b domain that are involved in the interactions with the substrate. To the best of our knowledge, our results constitute the first structural information on the biochemical features of a staphylococcal phage lysin and represent a pivotal step forward in understanding this type of lysin.
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