Evaluating the Role of an Outer Membrane Lipoprotein Cj1279c in the Pathogenesis of Campylobacter jejuni
Author(s): Fayez Alghofaili*
Abstract
Campylobacter jejuni is considered to be the most common bacterial cause of human gastroenteritis worldwide, and is often acquired from contaminated poultry products. However, fundamental aspects of its pathogenesis remain poorly understood. Proteomic technology and bioinformatic analysis have identified a number of membrane-associated proteins including lipoproteins in C. jejuni. Among those proteins is (designated Cj1279c), which seems to be involved in the interaction of C. jejuni with the host cell surface and contribute to pathogenesis. Cj1279c contains at least three fibronectin type III domains, which often associated with cell surface binding. Importantly, it has been found to be required for chicken colonization in vivo and efficient binding to LMH chicken cells in vitro. The Cj1279c gene is highly conserved in eight C. jejuni genome sequences. The aim of this study was to explore its contribution to Campylobacter adhesion to human cells by using Cj1279c mutants in an existing cell-association assay (Caco-2 cells). Cj1279c mutants were also examined in association and ELISA assays. The Cj1279c mutants did not show a significant reduction in adherence to the human enteric-like cell line Caco-2 as well as to fibronectin. This finding may eliminate the involvement of this lipoprotein in the pathogenesis of C. jejuni and suggest a different role for Cj1279c in chicken and human hosts. Further work is required to examine the binding of Cj1279c to other potential ligands by performing adhesion and invasion assays.