Abstract
Bacterial adhesins play a pivotal role in the tight bacteria-host cells attachment to initiate the downstream processes and bacterial infection of hosts. In this study, we identified a novel adhesin, VpadF in V. parahaemolyticus. Deletion of VpadF in V. parahaemolyticus markedly impaired its attachment and cytotoxicity to epithelial cells, as well as attenuated the virulence in murine model. Biochemical studies revealed that VpadF recognized both fibronectin and fibrinogen. The binding of VpadF to these two host receptors was mainly dependent on the its fifth bacterial immunoglobulin-like group domain and its C-terminal tail. Our finding suggested that VpadF is a major virulence factor of V. parahaemolyticus and a potential good candidate for V. parahaemolyticus infection control for both vaccine development and drug target.
Highlights
Bacterial adhesins play a pivotal role in the tight bacteria-host cells attachment to initiate the downstream processes and bacterial infection of hosts
VpadF consists of a putative transmembrane domain at the N-terminal, followed by five bacterial immunoglobulin-like tandem repeats (Bigs)
In the case of V. parahaemolyticus, its infectious processes require the adherence to intestinal epithelial cells, resulting in epithelial cell extrusion, villus disintegration and formation V. parahaemolyticus-filled cavities[44]
Summary
Bacterial adhesins play a pivotal role in the tight bacteria-host cells attachment to initiate the downstream processes and bacterial infection of hosts. The multivalent adhesion molecule 7 (MAM7), mannose-sensitive haemagglutinin (MSHA) pilus, enolase, capsular polysaccharide and two type VI secretion systems (T6SSs) have been reported to contribute to cell attachment of V. parahaemolyticus[18,19,20,21,22] Among these adhesive organelles, only mam[7] was found to be required for the pathogenesis of V. parahaemolyticus in the worm infection model. We identified a novel adhesin gene vp1767, which was referred to as VpadF (V. parahaemolyticus adhesive Factor), contributing to the attachment to and cytotoxicity against epithelial cells. This gene is essential for the lethal effect of V. parahaemolyticus on mice. VpadF bound to cell surface receptors, fibronectin (Fn) and fibrinogen (Fg), which may contribute to its host colonization and pathogenesis
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