ArticleVirologica Sinica2015
Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity.
Article in Virologica Sinica, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- The novel prophage lysin Lys1459 exhibits broad-spectrum antibacterial activity via triple-binding domain.Applied and environmental microbiology · 2026Article
- Clinical implementation of endolysins targeting gram-positive bacteria points toward a combination strategy with standard-of-care antibiotics: a selective review.European journal of medical research · 2026Review
- A novel broad-spectrum phage lysin CP02 for biocontrol ofCurrent research in food science · 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
- Characterization of the host specificity of the SH3 cell wall binding domain of the staphylococcal phage 88 endolysin.Archives of microbiology · 2025Article
- A novel lysin Ply691 exhibits potent bactericidal activity againstFrontiers in veterinary science · 2025Article
- Identification and Characterization of a Novel Prophage Lysin againstMolecules (Basel, Switzerland) · 2024Article
- You get what you test for: The killing effect of phage lysins is highly dependent on buffer tonicity and ionic strength.Microbial biotechnology · 2024Article
- Bacteriophage-derived endolysins as innovative antimicrobials against bovine mastitis-causing streptococci and staphylococci: a state-of-the-art review.Acta veterinaria Scandinavica · 2024Review
- Bacteriophage endolysin treatment for systemic infection of Streptococcus iniae in hybrid striped bass.Fish & shellfish immunology · 2024Article
- Development of engineered endolysins with in vitro intracellular activity against streptococcal bovine mastitis-causing pathogens.Microbial biotechnology · 2023Article
- Article
- Activity of Exebacase (CF-301) against Biofilms Formed by Staphylococcus epidermidis Strains Isolated from Prosthetic Joint Infections.Antimicrobial agents and chemotherapy · 2022Article
- Expanding the Database of Signal-Anchor-Release Domain Endolysins Through Metagenomics.Probiotics and antimicrobial proteins · 2022Article
- Electrostatic-Mediated Affinity Tuning of Lysostaphin Accelerates Bacterial Lysis Kinetics and EnhancesAntimicrobial agents and chemotherapy · 2021Article
- Article
- Characterization of the Bacteriophage-Derived Endolysins PlySs2 and PlySs9 with In Vitro Lytic Activity against Bovine MastitisAntibiotics (Basel, Switzerland) · 2020Article
- Contributions of Net Charge on the PlyC Endolysin CHAP Domain.Antibiotics (Basel, Switzerland) · 2019Article
- ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain.Antimicrobial agents and chemotherapy · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The novel phage lysin PlySs2, is reported to be highly active against various bacteria, including staphylococci, streptococci and Listeria. However, the molecular mechanisms underlying its broad lytic spectrum remain to be established. In the present study, the lytic activity of the catalytic domain (CD, PlySc) and binding specificity of the cell wall binding domain (CBD, PlySb) of PlySs2 were examined. Our results showed that PlySc alone maintains very limited lytic activity. Enhanced green fluorescent protein (EGFP)-fused PlySb displayed high binding affinity to the streptococcal strains tested, including S. suis, S. dysgalactiae, and S. agalactiae, but not staphylococci, supporting its utility as a good CBD donor for streptococcal-targeted lysin engineering. EGFP-fused intact PlySs2 similarly displayed high affinity for streptococci, but not staphylococci. Notably, four truncated PlySb fragments showed no binding capacity. These findings collectively indicate that integrity of the PlySc and PlySb domains is an essential determinant of the broad lytic activity of PlySs2.
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