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.
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