ArticleThe Journal of biological chemistry2011
Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed.
- In silico analysis, expression, and characterization of LysStp1 endolysin with L-alanyl-D-glutamate carboxypeptidase activity.Virus genes · 2026Article
- Designing the Next Generation of Endolysins: A Triple Strategy Integrating Bioinformatics Mining, Engineering Modification and Encapsulation Formulation.Probiotics and antimicrobial proteins · 2026Review
- 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
- Enzymatic property and stabilization mechanism of LysBT1, a novel polyextremotolerant endolysin with a C-terminal S-layer homology domain.Applied and environmental microbiology · 2025Article
- 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
- Characterization of the host specificity of the SH3 cell wall binding domain of the staphylococcal phage 88 endolysin.Archives of microbiology · 2025Article
- Phage-Derived Endolysins Against Resistant Staphylococcus spp.: A Review of Features, Antibacterial Activities, and Recent Applications.Infectious diseases and therapy · 2025Review
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Synergistic Enzybiotic Effect of a Bacteriophage Endolysin and an Engineered Glucose Oxidase AgainstBiomolecules · 2024Article
- Identification of cell wall binding domains and repeats inBiochemistry and biophysics reports · 2024Article
- Molecular Docking of Endolysins for Studying Peptidoglycan Binding Mechanism.Molecules (Basel, Switzerland) · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Uncovering Endolysins against Methicillin-ResistantACS infectious diseases · 2024Article
- Review
- You get what you test for: The killing effect of phage lysins is highly dependent on buffer tonicity and ionic strength.Microbial biotechnology · 2024Article
- Lysins as a powerful alternative to combat Bacillus anthracis.Applied microbiology and biotechnology · 2024Review
- Engineering of chimeric enzymes with expanded tolerance to ionic strength.Microbiology spectrum · 2024Article
- 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
29 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
The recombinant lysins of lytic phages, when applied externally to Gram-positive bacteria, can be efficient bactericidal agents, typically retaining high specificity. Their development as novel antibacterial agents offers many potential advantages over conventional antibiotics. Protein engineering could exploit this potential further by generating novel lysins fit for distinct target populations and environments. However, access to the peptidoglycan layer is controlled by a variety of secondary cell wall polymers, chemical modifications, and (in some cases) S-layers and capsules. Classical lysins require a cell wall-binding domain (CBD) that targets the catalytic domain to the peptidoglycan layer via binding to a secondary cell wall polymer component. The cell walls of Gram-positive bacteria generally have a negative charge, and we noticed a correlation between (positive) charge on the catalytic domain and bacteriolytic activity in the absence of the CBD (nonclassical behavior). We investigated a physical basis for this correlation by comparing the structures and activities of pairs of lysins where the lytic activity of one of each pair was CBD-independent. We found that by engineering a reversal of sign of the net charge of the catalytic domain, we could either eliminate or create CBD dependence. We also provide evidence that the S-layer of Bacillus anthracis acts as a molecular sieve that is chiefly size-dependent, favoring catalytic domains over full-length lysins. Our work suggests a number of facile approaches for fine-tuning lysin activity, either to enhance or reduce specificity/host range and/or bactericidal potential, as required.
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