The Mycobacteriophage Ms6 LysB N-Terminus Displays Peptidoglycan Binding Affinity.

ABSTRACT: Double-stranded DNA bacteriophages end their lytic cycle by disrupting the host cell envelope, which allows the release of the virion progeny. Each phage must synthesize lysis proteins that target each cell barrier to phage release. In addition to holins, which permeabilize the cytoplasmic membrane, and endolysins, which disrupt the peptidoglycan (PG), mycobacteriophages synthesize a specific lysis protein, LysB, capable of detaching the outer membrane from the complex cell wall of mycobacteria. The family of LysB proteins is highly diverse, with many members presenting an extended N-terminus. The N-terminal region of mycobacteriophage Ms6 LysB shows structural similarity to the PG-binding domain (PGBD) of the φKZ endolysin. A fusion of this region with enhanced green fluores

SUBMITTER: Gigante AM 

PROVIDER: S-EPMC8309991 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature