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Results 1 - 4 of 4
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General Information
Commentary
Reference
physiological function
cleavage of Yersinia pestis autotransporter YapE by protease Pla is required to mediate bacterial aggregation and adherence to eukaryotic cells. Post-translation modification of YapE appears to be specific to Yersinia pestis. It was acquired along with the acquisition ofplasmid pPCP1 during the divergence of Yersinia pestis from Yersinia pseudotuberculosis, and is the first evidence of a mechanism to regulate bacterial adherence
physiological function
the outer membrane plasminogen activator Pla of Yersinia pestis is a central virulence factor in plague
physiological function
the plasminogen activator Pla single and the Braun lipoprotein Lpp Pla double mutant are unable to survive efficiently in murine and human macrophages. The levels of Pla and its associated protease activity are not affected in the Lpp single mutant, and, likewise, deletion of the Pla gene from wild-type does not alter Lpp levels. The ability of the Lpp Pla double mutant to be phagocytized by macrophages, to stimulate production of tumor necrosis factor-alpha and interleukin-6, and to activate the nitric oxide killing pathways of the host cells remains unaltered when compared to the wild-type-infected macrophages. Macrophages infected with either the wild-type or the Lpp Pla double mutant are equally efficient in their uptake of zymosan particles
physiological function
Yersinia pestis binding to fibronectin is mediated through Ail protein and plasminogen activator Pla
Results 1 - 4 of 4