SeaB is a conserved Salmonella enterica extracellular matrix binding protein involved in biofilm formation and infection
Da Costa, R.; Rooke, J.; Morris, F. C.; Yang, Z.; Lian, Z. J.; Rossiter, A. E.; Cole, J. A.; Forde, B. M.; Cunningham, A. F.; Henderson, I. R.
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Salmonella enterica is a leading cause of gastroenteritis worldwide. Exacerbating this issue is the emergence of multi-drug-resistant strains, posing a major threat to human health. Type 5 secretion system proteins play a major role in virulence and are viable vaccine targets. However, only a limited number of these proteins have been functionally characterized to date. In this study, we characterized SeaB, which belongs to the Type 5a secretion system. We demonstrated that SeaB is localized to the cell surface and is involved in binding to the extracellular matrix. Our results indicate that SeaB is involved in aggregation, biofilm formation and contributes to virulence. Furthermore, immunization with SeaB elicits antibodies and provides protection against Salmonella challenge in a mouse model of infection.
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