ArticleApplied and environmental microbiology2012
Genomic sequence of bacteriophage ATCC 8074-B1 and activity of its endolysin and engineered variants against Clostridium sporogenes.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 37 citations in OpenAlex.
- Comparative antibacterial activity of N-terminal and C-terminal domains of a recombinant endolysin againstApplied and environmental microbiology · 2025Article
- The Unique Capability of Endolysin to Tackle Antibiotic Resistance: Cracking the Barrier.Journal of xenobiotics · 2025Review
- Expression of a recombinant endolysin from bacteriophage CAP 10-3 with lytic activity against Cutibacterium acnes.Scientific reports · 2023Article
- Review
- AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase.Protein science : a publication of the Protein Society · 2023Article
- A comprehensive review of the applications of bacteriophage-derived endolysins for foodborne bacterial pathogens and food safety: recent advances, challenges, and future perspective.Frontiers in microbiology · 2023Review
- Potential Role of the Host-Derived Cell-Wall Binding Domain of Endolysin CD16/50L as a Molecular Anchor in Preservation of Uninfected Clostridioides difficile for New Rounds of Phage Infection.Microbiology spectrum · 2022Article
- Endolysin, a Promising Solution against Antimicrobial Resistance.Antibiotics (Basel, Switzerland) · 2021Review
- Novel Lytic Enzyme of Prophage Origin fromInternational journal of molecular sciences · 2021Article
- Phages and Enzybiotics in Food Biopreservation.Molecules (Basel, Switzerland) · 2021Review
- Isolation and Characterization of a Lytic Staphylococcus aureus Phage WV against Staphylococcus aureus Biofilm.Intervirology · 2021Article
- Phage lysin that specifically eliminates Clostridium botulinum Group I cells.Scientific reports · 2020Article
- Engineering of Phage-Derived Lytic Enzymes: Improving Their Potential as Antimicrobials.Antibiotics (Basel, Switzerland) · 2018Review
- Development of a specific fluorescent phage endolysin for in situ detection of Clostridium species associated with cheese spoilage.Microbial biotechnology · 2018Article
- Potential for Bacteriophage Endolysins to Supplement or Replace Antibiotics in Food Production and Clinical Care.Antibiotics (Basel, Switzerland) · 2018Review
- Bacteriophage endolysins and their applications.Science progress · 2016Article
- Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product.The Journal of biological chemistry · 2016Article
- Diversity in a Polymicrobial Community Revealed by Analysis of Viromes, Endolysins and CRISPR Spacers.PloS one · 2016Article
- Bacteriophage PBC1 and its endolysin as an antimicrobial agent against Bacillus cereus.Applied and environmental microbiology · 2015Article
- The CD27L and CTP1L endolysins targeting Clostridia contain a built-in trigger and release factor.PLoS pathogens · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Lytic bacteriophage ATCC 8074-B1 produces large plaques on its host Clostridium sporogenes. Sequencing of the 47,595-bp genome allowed the identification of 82 putative open reading frames, including those encoding proteins for head and tail morphogenesis and lysis. However, sequences commonly associated with lysogeny were absent. ORF 22 encodes an endolysin, CS74L, that shows homology to N-acetylmuramoyl-L-alanine amidases, and when expressed in Escherichia coli, the protein causes effective lysis of C. sporogenes cells when added externally. CS74L was also active on Clostridium tyrobutyricum and Clostridium acetobutylicum. The catalytic domain expressed alone (CS74L(1-177)) exhibited a similar activity and the same host range as the full-length endolysin. A chimeric endolysin consisting of the CS74L catalytic domain fused to the C-terminal domain of endolysin CD27L, derived from Clostridium difficile bacteriophage ΦCD27, was produced. This chimera (CSCD) lysed C. sporogenes cells with an activity equivalent to that of the catalytic domain alone. In contrast, the CD27L C-terminal domain reduced the efficacy of the CS74L catalytic domain when tested against C. tyrobutyricum. The addition of the CD27L C-terminal domain did not enable the lysin to target C. difficile or other CD27L-sensitive bacteria.
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