Abstract
Due to the global spread of multidrug resistant pathogenic bacteria, alternative approaches in combating infectious diseases are required. One such approach is the use of probiotics. Lactobacillus fermentum 3872 is a promising probiotic bacterium producing a range of antimicrobial compounds, such as hydrogen peroxide and lactic acid. In addition, previous studies involving genome sequencing and analysis of L. fermentum 3872 allowed the identification of a gene encoding a cell surface protein referred to as collagen binding protein (CBP) (not found in other strains of the species, according to the GenBank database), consisting of a C-terminal cell wall anchor domain (LPXT), multiple repeats of 'B domains' that form stalks presenting an "A domain" required for adhesion. In this study, we found that the CBP of L. fermentum 3872 binds to collagen I present on the surface of the epithelial cells lining the gastrointestinal tract. Moreover, we found that this host receptor is also used for attachment by the major gastrointestinal pathogen, Campylobacter jejuni. Furthermore, we identified an adhesin involved in such interaction and demonstrated that both L. fermentum 3872 and its CBP can inhibit binding of this pathogen to collagen I. Combined with the observation that C. jejuni growth is affected in the acidic environment produced by L. fermentum 3872, the finding provides a good basis for further investigation of this strain as a potential tool for fighting Campylobacter infections.