ArticleBiomolecules2024
Diversity of Endolysin Domain Architectures in Bacteriophages Infecting Bacilli.
Article in Biomolecules, 2024. 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.
- Domain shuffling of endolysin LysKB317 to controlBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Bacteriophage BCP01 and Its Endolysin as Tools for Biocontrol and Rapid Detection ofJournal of microbiology and biotechnology · 2026Article
- Analysis of a Novel T1-like Phage KanT1 Reveals a Standalone SH3 Domain as a Widespread Component ofInternational journal of molecular sciences · 2026Article
- Search for effective bacteriolytic enzymes and their combinations for the treatment of polymicrobial biofilm-associated infections.World journal of microbiology & biotechnology · 2026Article
- Physicochemical and Proteolytic Barriers Limiting Activity of Cpl-1 and Pal Endolysins in Human Circulation.Current issues in molecular biology · 2026Article
- Phage as control strategy against the foodborne pathogen, Bacillus cereus.Archives of microbiology · 2026Review
- NovelInternational journal of molecular sciences · 2025Article
- Integrative In Silico and Experimental Characterization of Endolysin LysPALS22: Structural Diversity, Ligand Binding Affinity, and Heterologous Expression.International journal of molecular sciences · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The increasing number of antibiotic-resistant bacterial pathogens is a serious problem in medicine. Endolysins are bacteriolytic enzymes of bacteriophages, and a promising group of enzymes with antibacterial properties. Endolysins of bacteriophages infecting Gram-positive bacteria have a modular domain organization. This feature can be used to design enzymes with new or improved properties by modifying or shuffling individual domains. This work is a detailed analysis 1of the diversity of endolysin domains found in bacteriophages infecting bacilli. During the course of the work, a database of endolysins of such bacteriophages was created, and their domain structures were analyzed using the NCBI database, RASTtk, BLASTp, HHpred, and InterPro programs. A phylogenetic analysis of endolysins was performed using MEGA X. In 438 phage genomes, 454 genes of endolysins were found. In the endolysin sequences found, eight different types of catalytic domains and seven types of cell wall binding domains were identified. The analysis showed that many types of endolysin domains have not yet been characterized experimentally. Studies of the properties of such domains will help to reveal the potential of endolysins for the creation of new antibacterial agents.
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Registered trials
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