Crystal structures of Campylobacter jejuni CadF reveal a potential role for the arginine residue R268 in peptidoglycan recognition and pocket formation.

ABSTRACT: Campylobacter jejuni is a pathogenic gram-negative bacterium that primarily causes foodborne enteritis in humans. The C. jejuni protein CadF is located in the outer membrane and is essential for the adhesion of C. jejuni to human cells. CadF contains an outer membrane-embedded domain and a periplasmic domain (CadF^PD). The transmembrane domain is well known to bind fibronectin, contributing to host cell recognition. However, the exact function of the CadF^PD has never been assessed experimentally. In this study, we present the crystal structures of the CadF^PD and demonstrate that CadF may function as a peptidoglycan-binding protein. The CadF^PD adopts a two-layer α/β structure and harbors a narrow pocket. The CadF^PD interacts with a pepti

SUBMITTER: Oh HB 

PROVIDER: S-EPMC12540904 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature