The Structure and Function of Biomaterial Endolysin EFm1 from E. faecalis Phage.

ABSTRACT: The endolysin EFm1 from the E. faecalis 002 (002) phage IME-EF1 efficiently lyses E. faecalis, a gram-positive bacterium that severely threatens human health. Here, the structure and lytic activity of EFm1 toward E. faecalis were further investigated. Lytic activity shows that EFm1 specifically lyses 002 and 22 other clinically isolated E. faecalis, but not E. faecalis 945. Therefore, EFm1 may be an alternative biomaterial to prevent and treat diseases caused by E. faecalis. A structural analysis showed that EFm1_D166Q is a tetramer consisting of one full-length unit with additional C-terminal domains (CTDs), while EFm1_{166-237 aa} is an octamer in an asymmetric unit. Several crucial domains and novel residues affecting the lytic

SUBMITTER: Zhou X 

PROVIDER: S-EPMC9316690 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature