ArticleJournal of bacteriology2011
Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
83 citing papers in PubMed, 124 citations in OpenAlex.
- Eradication of catheter-associated MDR Acinetobacter baumannii biofilms mediated by novel phage encoded depolymerase activity.NPJ biofilms and microbiomes · 2026Article
- Far-UV circular dichroism datasets describing salt dependent secondary structure ofData in brief · 2026Article
- Designing the Next Generation of Endolysins: A Triple Strategy Integrating Bioinformatics Mining, Engineering Modification and Encapsulation Formulation.Probiotics and antimicrobial proteins · 2026Review
- Phage endolysin therapy: a modern antimicrobial strategy against highly drug-resistant superbugs.Archives of microbiology · 2026Review
- Characterization of Endolysin LysG77YL fromJournal of microbiology and biotechnology · 2026Article
- Nanoluciferase-Based Reporters for Clostridioides difficile.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Selective antimicrobial potential of fucoidans against the pathogenFrontiers in microbiology · 2026Article
- Bacteriophage lysins: a promising strategy for combating foodborne pathogens in food safety.Frontiers in microbiology · 2026Review
- Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025Review
- Comparative antibacterial activity of N-terminal and C-terminal domains of a recombinant endolysin againstApplied and environmental microbiology · 2025Article
- Endolysin-based biocontrol strategies againstFood science and biotechnology · 2025Review
- Phage and enzyme therapies in wound infections: From lab to bedside.Chinese medical journal · 2025Review
- The Synergistic and Chimeric Mechanism of Bacteriophage Endolysins: Opportunities for Application in Biotherapeutics, Food, and Health Sectors.Probiotics and antimicrobial proteins · 2025Review
- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Article
- A Clostridioides difficile endolysin modulates toxin secretion without cell lysis.Communications biology · 2024Article
- Research Progress on Strategies for Improving the Enzyme Properties of Bacteriophage Endolysins.Journal of microbiology and biotechnology · 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
- Pathogenicity and virulence ofVirulence · 2023Review
23 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Endolysin CD27L causes cell lysis of the pathogen Clostridium difficile, a major cause of nosocomial infection. We report a structural and functional analysis of the catalytic activity of CD27L against C. difficile and other bacterial strains. We show that truncation of the endolysin to the N-terminal domain, CD27L1-179, gave an increased lytic activity against cells of C. difficile, while the C-terminal region, CD27L180-270, failed to produce lysis. CD27L1-179 also has increased activity against other bacterial species that are targeted by the full-length protein and in addition was able to lyse some CD27L-insensitive strains. However, CD27L1-179 retained a measure of specificity, failing to lyse a wide range of bacteria. The use of green fluorescent protein (GFP)-labeled proteins demonstrated that both CD27L and CD27L1-179 bound to C. difficile cell walls. The crystal structure of CD27L1-179 confirms that the enzyme is a zinc-dependent N-acetylmuramoyl-l-alanine amidase. A structure-based sequence analysis allowed us to identify four catalytic residues, a proton relay cascade, and a substrate binding pocket. A BLAST search shows that the closest-related amidases almost exclusively target Clostridia. This implied that the catalytic domain alone contained features that target a specific bacterial species. To test this hypothesis, we modified Leu 98 to a Trp residue which is found in an endolysin from a bacteriophage of Listeria monocytogenes (PlyPSA). This mutation in CD27L resulted in an increased activity against selected serotypes of L. monocytogenes, demonstrating the potential to tune the species specificity of the catalytic domain of an endolysin.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.