EC Number   |
General Information |
Reference |
|---|
   3.4.23.48 | evolution |
comparative analysis of the sequences of the pro-omptin Pla with other omptin family proteases, such as PgtE from Salmonella enterica (EC 3.4.23.49), SopA from Shigella flexneri, and OmpT and OmpP from Escherichia coli reveals the location of predicted linear B-cell epitopes in either identical positions or in a very close proximity to all nine Pla epitopes predicted from library, and identified serologically using human anti-Pla antisera, overview |
-, 755637 |
| 3.4.23.48 | evolution |
the enzyme belongs to the omptin family of enzymes |
753795 |
| 3.4.23.48 | evolution |
the modern isoform of Pla (T259) with an increased protease activity is found in Yersinia pestis subsp. pestis strains that are highly virulent for humans. The pathogenicity factor is absent in representatives of the Yersinia pestis subsp. microtus bv. caucasica/SNP-type 0.PE2, while an ancestral Pla isoform (I259) with characteristics similar to the properties of omptins from less virulent enterobacteria is found in three representatives of Yersinia pestis subsp. microtus (SNP-types 0.PE3 and 0.PE4), which are, as a rule, avirulent to guinea pigs and humans. Distribution of Pla isoforms among natural isolates of Yersinia pestis of different origin, overview |
755136 |
| 3.4.23.48 | evolution |
the pathogenicity factor is absent in representatives of the Yersinia pestis subsp. microtus bv. caucasica/SNP-type 0.PE2, while an ancestral Pla isoform (I259) with characteristics similar to the properties of omptins from less virulent enterobacteria is found in three representatives of Yersinia pestis subsp. microtus (SNP-types 0.PE3 and 0.PE4), which are, as a rule, avirulent to guinea pigs and humans. The modern isoform of Pla (T259) with an increased protease activity is found in Yersinia pestis subsp. pestis strains that are highly virulent for humans. Sequencing of pla genes from 118 Yersinia pestis subsp. microtus isolates reveals the absence of this gene in the strains belonging to bv. caucasica. All remaining isolates of Yersinia pestis subsp. microtus contain the ancestral Pla isoform (I259). Distribution of Pla isoforms among natural isolates of Yersinia pestis of different origin, overview |
-, 755136 |
| 3.4.23.48 | malfunction |
deletion of Pla results in a decreased Yersinia pestis bacterial burden in the host lung and failure to progress into the lethal proinflammatory phase of disease. Deletion of Pla does not alter adherence to and/or secretion into THP-1 cells. Infection of human precision-cut lung slices (hPCLS) with the knockout DELTApla strain results in significantly reduced Yersinia outer protein (Yop) translocation early after infection and continuing to 4 hours-post-infection. And deletion of Pla results in decreased Yersinia pestis T3S into alveolar macrophages in vivo during pneumonic plague. Addition of Pla to Yersinia pestis lacking all five known adhesins partially restores adherence and Yop delivery to macrophages derived from the human monocytic cell line THP-1 and human epithelial type 2 (HEp-2) cells, suggesting that Pla may contribute to adherence and Yop translocation in vitro |
753805 |
| 3.4.23.48 | malfunction |
eliminating Pla expression in a fully virulent Yersinia pestis strain decreases its LD50 by 6 orders of magnitude in a mouse model of bubonic plague |
709237 |
| 3.4.23.48 | malfunction |
introducing the single point mutation D206A into the active site of Pla suffices to render fully virulent Yersinia pestis susceptible to primed T-cells |
-, 753803 |
| 3.4.23.48 | malfunction |
Pla deficient Yersinia pestis disseminate to regional lymph nodes after subcutaneous inoculation but do not cause the lymphadenopathy observed with wild-type Yersinia pestis infections |
709237 |
| 3.4.23.48 | malfunction |
survival of mice infected with Pla-deficient Yersinia pestis is greater than cohorts infected with wild-type Yersinia Pestis. Survival advantage is negated, if fibrinogen knockout mice are infected instead, directly implicating the host coagulation system as a target for Pla's role in virulence |
709237 |
| 3.4.23.48 | metabolism |
plasminogen is an abundant circulating zymogen of the serine protease plasmin, which is the key enzyme in fibrinolysis. The physiological plasminogen activation by uPA (EC 3.4.21.73) or tPA (EC 3.4.21.68) is a single cut at the peptide bond R560-V561, which yields the two-chain active plasmin enzyme. Pla rapidly cleaves the same peptide as do the human physiological activators, and the formed plasmin remains enzymatically active as Pla does not degrade the B chain of plasmin that contains the protease catalytic domain |
754513 |
