Characterization of the LysP2110-HolP2110 Lysis System in Ralstonia solanacearum Phage P2110

• Published in: International journal of molecular sciences Vol. 24; no. 12; p. 10375
• Main Authors: Chen, Kaihong, Guan, Yanhui, Hu, Ronghua, Cui, Xiaodong, Liu, Qiongguang
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 20.06.2023; MDPI
• Subjects: Amino acids; Antibacterial activity; Antimicrobial agents; Bacteria; Bacterial infections; Biocompatibility; biocontrol; Bioinformatics; Biological control; broad-spectrum antibacterial activity; Chemical control; Control methods; Drug resistance; Ethylenediaminetetraacetic acids; Genomes; holin; Holins; Infections; lysins; Lysis; Membranes; Optimal control; Pathogens; Peptides; Phages; Phylogenetics; Plant bacterial diseases; plant bacterial wilt disease; Plant diseases; Proteins; Ralstonia solanacearum; Risk management; Wilt; lysins; Ralstonia solanacearum; biocontrol; plant bacterial wilt disease; broad-spectrum antibacterial activity; holin
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms241210375

, a pathogen causing widespread bacterial wilt disease in numerous crops, currently lacks an optimal control agent. Given the limitations of traditional chemical control methods, including the risk of engendering drug-resistant strains and environmental harm, there is a dire need for sustainable alternatives. One alternative is lysin proteins that selectively lyse bacteria without contributing to resistance development. This work explored the biocontrol potential of the LysP2110-HolP2110 system of phage P2110. Bioinformatics analyses pinpointed this system as the primary phage-mediated host cell lysis mechanism. Our data suggest that LysP2110, a member of the superfamily, requires HolP2110 for efficient bacterial lysis, presumably via translocation across the bacterial membrane. LysP2110 also exhibits broad-spectrum antibacterial activity in the presence of the outer membrane permeabilizer EDTA. Additionally, we identified HolP2110 as a distinct holin structure unique to the phages, underscoring its crucial role in controlling bacterial lysis through its effect on bacterial ATP levels. These findings provide valuable insights into the function of the LysP2110-HolP2110 lysis system and establish LysP2110 as a promising antimicrobial agent for biocontrol applications. This study underpins the potential of these findings in developing effective and environment-friendly biocontrol strategies against bacterial wilt and other crop diseases.