Molecular Machinery of the Triad Holin, Endolysin, and Spanin: Key Players Orchestrating Bacteriophage-Induced Cell Lysis and their Therapeutic Applications

Bibliographic Information
Authors: Samir S.
Journal: Protein and Peptide Letters
Publisher: Bentham Science Publishers
Publication Date: February 2024
Volume / Issue: Volume 31 / Issue 2
Pages: 85–96
ISSN: 9298665
DOI: 10.2174/0109298665181166231212051621
Scopus: View on Scopus
PubMed: 38258777
Document Type: Short survey
Authors and Affiliations
Samir S., Department of Biochemistry and Molecular Biology, Theodor Bilharz Research Institute, Giza, Egypt
Abstract
Phage therapy, a promising alternative to combat multidrug-resistant bacterial infections, harnesses the lytic cycle of bacteriophages to target and eliminate bacteria. Key players in this process are the phage lysis proteins, including holin, endolysin, and spanin, which work synergistically to disrupt the bacterial cell wall and induce lysis. Understanding the structure and function of these proteins is crucial for the development of effective therapies. Recombinant versions of these proteins have been engineered to enhance their stability and efficacy. Recent progress in the field has led to the approval of bacteriophage-based therapeutics as drugs, paving the way for their clinical use. These proteins can be combined in phage cocktails or combined with antibiotics to enhance their activity against bacterial biofilms, a common cause of treatment failure. Animal studies and clinical trials are being conducted to evaluate the safety and efficacy of phage therapy in humans. Overall, phage therapy holds great potential as a valuable tool in the fight against multidrug-resistant bacteria, offering hope for the future of infectious disease treatment. © 2024 Bentham Science Publishers.
Keywords
bacteriophage; holin; Multidrug-resistant; multigene lysis; phage endolysin; spanin; Animals; Anti-Bacterial Agents; Bacteria; Bacterial Infections; Bacteriolysis; Bacteriophages; Drug Resistance, Multiple, Bacterial; Endopeptidases; Humans; Phage Therapy; Viral Proteins; antiinfective agent; ceftriaxone; daptomycin; endolysin; gentamicin; unclassified drug; proteinase; viral protein; Acinetobacter baumannii infection; acne; amino terminal sequence; antimicrobial activity; bacterial infection; biofilm; bloodstream infection; bovine mastitis; carboxy terminal sequence; cardiovascular infection; cell membrane; clinical evaluation; cytolysis; drug approval; eczema; food poisoning; genetic code; human; inner membrane; lung infection; molecular biology; multidrug resistant bacterium; nonhuman; outer membrane; pneumococcal infection; progeny; protein domain; protein structure; rosacea; safety procedure; Short Survey; skin disease; therapy effect; treatment failure; upper respiratory tract infection; animal; bacterium; chemistry; drug effect; genetics; metabolism; multidrug resistance; procedures; therapy; virology
Citation Information
Scopus Citations: 18
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