Abstract
Campylobacter jejuni, a foodborne pathogen, is one of the most common bacterial causes of gastroenteritis in the world. Undercooked poultry, raw (unpasteurized) dairy products, untreated water, and contaminated produce are the most common sources associated with infection. C. jejuni establishes a niche in the gut by adhering to and invading epithelial cells, which results in diarrhea with blood and mucus in the stool. The process of colonization is mediated, in part, by surface-exposed molecules (adhesins) that bind directly to host cell ligands or the extracellular matrix (ECM) surrounding cells. In this review, we introduce the known and putative adhesins of the foodborne pathogen C. jejuni. We then focus our discussion on two C. jejuni Microbial Surface Components Recognizing Adhesive Matrix Molecule(s) (MSCRAMMs), termed CadF and FlpA, which have been demonstrated to contribute to C. jejuni colonization and pathogenesis. In vitro studies have determined that these two surface-exposed proteins bind to the ECM glycoprotein fibronectin (FN). In vivo studies have shown that cadF and flpA mutants exhibit impaired colonization of chickens compared to the wild-type strain. Additional studies have revealed that CadF and FlpA stimulate epithelial cell signaling pathways necessary for cell invasion. Interestingly, CadF and FlpA have distinct FN-binding domains, suggesting that the functions of these proteins are non-redundant. In summary, the binding of FN by C. jejuni CadF and FlpA adhesins has been demonstrated to contribute to adherence, invasion, and cell signaling.
Highlights
Specialty section: This article was submitted to Infectious Diseases, a section of the journal Frontiers in Microbiology
C. jejuni establishes a niche in the gut by adhering to and invading epithelial cells, which results in diarrhea with blood and mucus in the stool
We focus our discussion on two C. jejuni Microbial Surface Components Recognizing Adhesive Matrix Molecule(s) (MSCRAMMs), termed CadF and FlpA, which have been demonstrated to contribute to C. jejuni colonization and pathogenesis
Summary
Pathogenic bacteria that have FNBPs can use them to promote tissue adherence and interface with host cell signaling complexes (Stones and Krachler, 2015). A three-component bridge is formed between the FNBPs, host cell-associated FN, and transmembrane integrins (Hymes and Klaenhammer, 2016). The linkage between the bacteria and FN stimulates integrin occupancy and clustering, triggering the recruitment of cell signaling molecules and rearrangement of the host cell actin cytoskeleton (Wu, 2007; Zaidel-Bar et al, 2007; Deakin and Turner, 2008). In some instances, it is the intimate binding mediated by FNBPs that enables host cell invasion and intracellular multiplication, resulting in acute disease (Hymes and Klaenhammer, 2016). The FNBPA and FNBPB proteins from S. aureus have been reported to bind to the heparin-binding domain of FN (Bae and Schneewind, 2003; Schwarz-Linek et al, 2003) and that the deletion of both genes is required to abolish the organism’s
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