ArticleVirologica Sinica2015
Multiple-site mutations of phage Bp7 endolysin improves its activities against target bacteria.
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 8 papers.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Bacteriophage as a potential biotherapeutics to combat present-day crisis of multi-drug resistant pathogens.Heliyon · 2024Review
- Engineering strategies and challenges of endolysin as an antibacterial agent against Gram-negative bacteria.Microbial biotechnology · 2024Review
- Design, Screening, and Characterization of Engineered Phage Endolysins with Extracellular Antibacterial Activity against Gram-Negative Bacteria.Applied and environmental microbiology · 2023Article
- Endolysins of bacteriophage vB_Sal-S-S10 can naturally lyse Salmonella enteritidis.BMC veterinary research · 2022Article
- Characterization and genome analysis of Pseudomonas aeruginosa phage vB_PaeP_Lx18 and the antibacterial activity of its lysozyme.Archives of virology · 2022Article
- Isolation, characterization, and genomic analysis of the novel T4-like bacteriophage ΦCJ20.Food science and biotechnology · 2021Article
- Characterization of a Novel Bacteriophage swi2 Harboring Two Lysins Can Naturally LyseFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The widespread use of antibiotics has caused serious drug resistance. Bacteria that were once easily treatable are now extremely difficult to treat. Endolysin can be used as an alternative to antibiotics for the treatment of drug-resistant bacteria. To analyze the antibacterial activity of the endolysin of phage Bp7 (Bp7e), a 489-bp DNA fragment of endolysin Bp7e was PCR-amplified from a phage Bp7 genome and cloned, and then a pET28a-Bp7e prokaryotic expression vector was constructed. Two amino acids were mutated (L99A, M102E) to construct pET28a-Bp7Δe, with pET28a-Bp7e as a template. Phylogenetic analysis suggested that BP7e belongs to a T4-like phage endolysin group. Bp7e and its mutant Bp7Δe were expressed in Escherichia coli BL21(DE3) as soluble proteins. They were purified by affinity chromatography, and then their antibacterial activities were analyzed. The results demonstrated that the recombinant proteins Bp7e and Bp7Δe showed obvious antibacterial activity against Micrococcus lysodeikticus but no activity against Staphylococcus aureus. In the presence of malic acid, Bp7e and Bp7Δe exhibited an effect on most E. coli strains which could be lysed by phage Bp7, but no effect on Salmonella paratyphi or Pseudomonas aeruginosa. Moreover, Bp7Δe with double-site mutations showed stronger antibacterial activity and a broader lysis range than Bp7e.
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