Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.

ABSTRACT: Bacteriophage endolysins targeting Gram-positive bacteria typically feature a modular architecture of one or more enzymatically active domains (EADs) and cell wall binding domains (CBDs). Several endolysins also feature internal translational start sites (iTSSs) that produce short variant (SV) isoforms alongside the full-length (FL) endolysin. While the lytic activity of endolysins and their isoforms has been extensively studied as exogenous agents, the purpose behind producing the SV isoform during the phage infection cycle remains to be explored. In this study, we used staphylococcal phage φ2638A as a model to determine the interplay between its FL endolysin, Ply2638A, and its SV isoform during phage infection. X-ray crystallography structures and AlphaFold-generated models enabled eluci

SUBMITTER: Zinsli LV 

PROVIDER: S-EPMC12203907 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature