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Salmonella  spp. are Gram-negative enteropathogenic bacteria that infect a variety of vertebrate hosts. Like any other living organism, protein secretion is a fundamental process essential for various aspects of  Salmonella  biology. Herein we report the identification and characterization of a horizontally acquired, autonomous and previously unreported secretion pathway. In  Salmonella enterica  serovar Typhimurium, this novel secretion pathway is encoded by STM1669 and STM1668, designated  zirT  and  zirS , respectively. We show that ZirT is localized to the bacterial outer membrane, expected to adopt a compact β-barrel conformation, and functions as a translocator for ZirS. ZirS is an exoprotein, which is secreted into the extracellular environment in a ZirT-dependent manner. The ZirTS secretion pathway was found to share several important features with two-partner secretion (TPS) systems and members of the intimin/invasin family of adhesions. We show that  zirTS  expression is affected by zinc; and that in vivo, induction of  zirT  occurs distinctively in  Salmonella  colonizing the small intestine, but not in systemic sites. Additionally, strong expression of  zirT  takes place in  Salmonella  shed in fecal pellets during acute and persistent infections of mice. Inactivation of ZirTS results in a hypervirulence phenotype of  Salmonella  during oral infection of mice. Cumulatively, these results indicate that the ZirTS pathway plays a unique role as an antivirulence modulator during systemic disease and is involved in fine-tuning a host–pathogen balance during salmonellosis.

A Novel Secretion Pathway of Salmonella enterica Acts as an Antivirulence Modulator during Salmonellosis