The twin arginine translocation system is essential for virulence of Yersinia pseudotuberculosis.
Yersinia species pathogenic to humans have been extensively characterized with respect to type III secretion and its essential role in virulence. This study concerns the twin arginine translocation (Tat) pathway utilized by gram-negative bacteria to secrete folded proteins across the bacterial inner membrane into the periplasmic compartment. We have shown that the Yersinia Tat system is functional and required for motility and contributes to acid resistance. A Yersinia pseudotuberculosis mutant strain with a disrupted Tat system (tatC) was, however, not affected in in vitro growth or more susceptible to high osmolarity, oxidative stress, or high temperature, nor was it impaired in type III secretion. Interestingly, the tatC mutant was severely attenuated via both the oral and intraperitoneal routes in the systemic mouse infection model and highly impaired in colonization of lymphoid organs like Peyer's patches and the spleen. Our work highlights that Tat secretion plays a key role in the virulence of Y. pseudotuberculosis.
Lavander
Moa
M
Department of Medical Countermeasures, Division of NBC Defense, Swedish Defense Research Agency, SE-901 82 Umeå, Sweden.
Ericsson
Solveig K
SK
Bröms
Jeanette E
JE
Forsberg
Ake
A
D000818:Animals; D001120:Arginine / Q000378:metabolism; D018929:Cell Culture Techniques; D006367:HeLa Cells; D006801:Humans; D008264:Macrophages / Q000382:microbiology*; D026901:Membrane Transport Proteins / Q000378:metabolism / Q000502:physiology*; D051379:Mice; D021381:Protein Transport; D014774:Virulence / Q000502:physiology*; D015011:Yersinia pseudotuberculosis / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*
D026901:Membrane Transport Proteins; D001120:Arginine