Identification and analysis of the crucial holin domain and sites and the bactericidal activity of a holin-endolysin lysis cassette from phage PZL-Ah152 against <i>Aeromonas hydrophila</i>.

ABSTRACT: With the increasing prevalence of antibiotic-resistant bacteria, phage therapy has garnered significant attention. Holin and lysin play essential roles in the phage-induced lysis of bacteria. This study investigated the functions of the holin protein Hol 46 and the lysozyme protein Lys 17 from the phage PZL-Ah152 and the mechanisms underlying the action of the fusion protein Hol 46_Lys 17. Assays, including membrane protein extraction tests and fluorescence microscopy, verified that the Hol 46 protein localized to the cell membrane and significantly inhibited the growth of Aeromonas hydrophila Ah152. We determined that the Hol 46 C-terminal domain and glutamic acid residue at position 66, along with the lysine residues at positions 63 and 64, were critical for its cell-penetrating a

SUBMITTER: Feng C 

PROVIDER: S-EPMC12817945 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature