Endolysins have drawn considerable attention as viable modalities for antibiotic use. The most significant obstacle for Gram-negative targeting endolysins is the presence of the outer membrane barrier. A heterologously expressed endolysin encoded by bacteriophage PBPA90 infecting Pseudomonas aeruginosa exhibited intrinsic antibacterial activity against P. aeruginosa. The antibacterial efficacy was improved by substituting 15 amino acids and by fusing cecropin A to the N-terminus. The resulting engineered endolysin, LNT103, demonstrated strong antibacterial activity, with minimum inhibitory concentrations as low as 4 μg/ml, against various Gram-negative pathogens in addition to P. aeruginosa, including Acinetobacter baumannii, Escherichia coli, Klebsiella pneumoniae, Klebsiella aerogenes, and Enterobacter cloacae. The engineered endolysin rendered both the outer and the inner bacterial membranes permeable. It exhibited a synergistic effect with colistin, and additive effects with carbapenem antibiotics. Bacterial resistance development to LNT103 was none to minimal in vitro. Its in vivo efficacy was verified in bacteremia models of mice infected with A. baumannii. The endolysin led to a resensitization of resistant bacteria to meropenem when used in combination in vivo.
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http://dx.doi.org/10.1016/j.ijbiomac.2025.140463 | DOI Listing |
Viruses
January 2025
bitBiome, Inc., 513 Wasedatsurumaki-Cho, Shinjuku-Ku 162-0041, Tokyo, Japan.
Bacteriophage-derived endolysins are being developed as an alternative to antimicrobials. The development of endolysins against Gram-negative bacteria requires the discovery of effective endolysins against the target species and the capability to penetrate the outer membrane of bacteria by endolysin. Here, we propose an efficient endolysin development approach that combines a data-driven endolysin search utilizing bacterial genomes with high-throughput laboratory assays.
View Article and Find Full Text PDFJ Xenobiot
January 2025
Molecular Biotechnology Division, National Institute of Biotechnology, Savar, Dhaka 1349, Bangladesh.
The lack of new antibacterial medicines and the rapid rise in bacterial resistance to antibiotics pose a major threat to individuals and healthcare systems. Despite the availability of various antibiotics, bacterial resistance has emerged for almost every antibiotic discovered to date. The increasing prevalence of multidrug-resistant bacterial strains has rendered some infections nearly untreatable, posing severe challenges to health care.
View Article and Find Full Text PDFACS Omega
February 2025
KTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.
Functionalization of biomaterials with extra protein domains will expand their functional roles in biomedical research. The recombinant spider silk protein FN-4RepCT has been shown able to adapt various formats like coatings, nanowires, and macroscopic fibers. Functionalizing these various formats of FN-4RepCT in a site-specific manner will provide the next generation of biomaterials.
View Article and Find Full Text PDFFood Microbiol
June 2025
National Health Commission Science and Technology Innovation Platform for Nutrition and Safety of Microbial Food, Guangdong Provincial Key Laboratory of Microbial Safety and Health, State Key Laboratory of Applied Microbiology Southern China, Institute of Microbiology, Guangdong Academy of Sciences, 510070, China. Electronic address:
Staphylococcus aureus, a foodborne bacterial pathogen, poses a serious challenge due to antibiotic resistance, highlighting the urgent need for effective and alternative antimicrobial agents. Undoubtedly, bacteriophages and bacteriophage-encoded antibacterial proteins have been considered effective biopreservatives. Herein, we report the isolation and characterization of a novel lytic bacteriophage, vB_SA_STAP152, along with its endolysin LysP152.
View Article and Find Full Text PDFInt J Food Microbiol
March 2025
Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education, Inner Mongolia Agricultural University, Hohhot 010018, China; Key Laboratory of Dairy Products Processing, Ministry of Agriculture and Rural Affairs, Inner Mongolia Agricultural University, Hohhot 010018, China; Inner Mongolia Key Laboratory of Dairy Biotechnology and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, China. Electronic address:
Lyase, a peptidoglycan hydrolase derived from phage, has been considered as a promising alternative antimicrobial agent. To date, adequate information regarding the characteristics of the Lactobacillus phage lyase is lacking. In this study, a lyase from Lactobacillus phage LFP01 was cloned and heterologously expressed in Escherichia coli (E.
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