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alpha2-antiplasmin + H2O
?
PAI-1 + H2O
?
a serpin
-
-
?
plasminogen + H2O
plasmin + ?
plasminogen activator inhibitor-1 + H2O
?
single-chain urokinase + H2O
?
activation
-
-
?
tissue factor pathway inhibitor + H2O
?
YapE + H2O
?
Yersinia pestis autotransporter YapE protein
cleavage of YapE occurs in Yersinia pestis but not in the enteric Yersinia species, and requires the omptin Pla
-
?
YapG + H2O
?
Yersinia pestis autotransporter YapG protein
sites K512, (K548-R549) and K594-R595 represent the primary cleavage sites of YapG, whereas sites K'558 and K'604 represent the secondary alternative cleavage sites
-
?
alpha2-antiplasmin + H2O
?
C3 protein of complement system + H2O
fragments of C3 protein of complement system
-
-
-
?
complement C3 + H2O
?
-
Pla proteolyzes complement C3 which may amiliorate the host inflammatory response by abolishing its chemoattractant properties
-
-
?
complement protein C3 + H2O
?
-
-
-
-
?
human alpha2-antiplasmin + H2O
fragments of alpha2-antiplasmin
-
-
-
-
?
human Glu-plasminogen + H2O
plasmin + ?
-
Pla activates Glu-plasminogen to plasmin, in vitro, TFPI is found to be a much better substrate for Pla than plasminogen
-
-
?
human tissue factor pathway inhibitor + H2O
?
-
Pla can proteolytically degrade TFPI, completely abrogating its anticoagulant function. In vitro, TFPI is found to be a much better substrate for Pla than plasminogen
-
-
?
plasminogen + H2O
plasmin + ?
plasminogen activator inhibitor-1 + H2O
?
serpin alpha2-antiplasmin + H2O
?
-
-
-
-
?
Yersinia outer proteins + H2O
fragments of Yersinia outer proteins
-
-
-
?
zymogen factor VII + H2O
factor VIIa
-
Pla proteolytically converts zymogen factor VII to the active form, factor VIIa. Pla activates factor VII about twice as fast as it activates plasminogen
-
-
?
additional information
?
-
alpha2-antiplasmin + H2O
?
inactivation
-
-
?
alpha2-antiplasmin + H2O
?
a serpin
-
-
?
alpha2-antiplasmin + H2O
?
alpha2AP is the main inhibitor of free plasmin in the circulation. Pla cleaves and inactivates alpha2AP by a single, rapid cut. It appears likely that the R376-M377 bait peptide bond is targeted by Pla
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
activation
-
-
?
plasminogen + H2O
plasmin + ?
identification and analysis of small-peptide substrates and inhibitors of plasminogen activator Pla by use of parallel synthesis and positional scanning
-
-
?
plasminogen + H2O
plasmin + ?
plasminogen activator Pla shown to be essential to cause primary pneumonic plague, minor importance determined for dissemination during pneumonic plague than during bubonic plague, inhibition of plasminogen activator Pla expression shown to prolong survival of infected mice
-
-
?
plasminogen activator inhibitor-1 + H2O
?
inactivation
-
-
?
plasminogen activator inhibitor-1 + H2O
?
inactivation. PAI-1 is the primary physiological inhibitor of uPA and t-PA and a major inhibitor of fibrinolysis. Pla rapidly inactivates PAI-1 by a single cleavage of the bait peptide at R346-M347. In circulation, most PAI-1 is bound to vitronectin, which is also degraded by Pla
-
-
?
TAFI + H2O
TAFIa + ?
inactivation
-
-
?
TAFI + H2O
TAFIa + ?
TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. Pla cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa
-
-
?
tissue factor pathway inhibitor + H2O
?
inactivation
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme Pla cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
alpha2-antiplasmin + H2O
?
-
Pla inactivates the main physiologic inhibitor of plasmin
-
-
?
alpha2-antiplasmin + H2O
?
-
Pla inactivates alpha2-antiplasmin
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
Pla also expresses a weak coagulase activity
-
?
plasminogen + H2O
plasmin + ?
-
activates plasminogen by cleaving the Arg560-Val561 bond
-
?
plasminogen + H2O
plasmin + ?
-
Pla has the additional ability to bind to the basement membrane component type IV collagen rendering adhesive properties to Yersina pestis cells
-
?
plasminogen + H2O
plasmin + ?
-
Pla belongs to the omptin family of enterobacterial surface proteases and is responsible for the highly efficient invasion of the plague bacterium from the subcutaneous infection site into the circulation
-
-
?
plasminogen + H2O
plasmin + ?
-
plasminogen activator is a surface virulence factor that contributes to the highly imvasive nature of the pathogen by binding various tissue matrix components
-
-
?
plasminogen + H2O
plasmin + ?
-
cleavage of Arg560-/-Val561
-
-
?
plasminogen activator inhibitor-1 + H2O
?
-
-
-
-
?
plasminogen activator inhibitor-1 + H2O
?
-
PAI-1 is cleaved and inactivated by the Pla protease of Yersinia pestis in the lung airspace of C57BL/6 mice
-
-
?
additional information
?
-
-
plasminogen activator Pla is essential for the spread of Yersinia pestis from the subcutaneous infection site into circulation, and the proteolytic activation of plasminogen is involved in virulence function. In addition to proteolysis plasminogen activator Pla promotes bacterial adhesion to mammalian extracellular matrices and epithelial cells as well as bacterial invasion into eukayotic cells. Laminin functions as an adhesion target for plasminogen activator Pla, which also expresses a lower adhesion affinity for heparan sulfate proteoglycan. the adhesion targets are not directly degraded by plasminogen activator Pla, but Pla-mediated generation of plasmin leads to their degradation
-
-
?
additional information
?
-
-
plasminogen activator plays a pivotal role in internalisation of bacteria by HeLa cells. Intracellular signalling and cytoskeletal rearrangement is involved in Yersinia pestis plasminogen activator mediated HeLa cell invasion
-
-
?
additional information
?
-
-
no degradation of Val-Leu-Lys-p-nitroanilide. Plasminogen activator degrades outer membrane proteins of Yersinia cell surface and exhibits a weak coagulase activity. In addition to proteolysis plasminogen activator Pla promotes bacterial adhesion to mammalian extracellular matrices and epithelial cells as well as bacterial invasion into eukaryotic cells. Laminin functions as an adhesion target for plasminogen activator Pla, which also expresses a lower adhesion affinity for heparan sulfate proteoglycan. The adhesion targets are not directly degraded by plasminogen activator Pla, but Pla-mediated generation of plasmin leads to their degradation
-
-
?
additional information
?
-
-
the invasion of alveolar macrophages by Yersinia pestis depends both in vitro and in vivo on the expression of plasminogen activator Pla. Macrophages and transfectants expressing C-type lectin receptor DEC-205, but not their negative counterparts, phagocytose plasminogen activator Pla-expressing Yersinia pestis and Escherichia coli K12 more efficiently than Pla-negative controls. The interactions between Pla-expressing bacteria and DEC-205-expressing transfectants or alveolar macrophages can be inhibited by an anti-DEC-205 antibody. The blockage of the Pla-DEC-205 interaction reduces the dissemination of Yersinia pestis in mice
-
-
?
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alpha2-antiplasmin + H2O
?
alpha2AP is the main inhibitor of free plasmin in the circulation. Pla cleaves and inactivates alpha2AP by a single, rapid cut. It appears likely that the R376-M377 bait peptide bond is targeted by Pla
-
-
?
plasminogen + H2O
plasmin + ?
plasminogen activator inhibitor-1 + H2O
?
inactivation. PAI-1 is the primary physiological inhibitor of uPA and t-PA and a major inhibitor of fibrinolysis. Pla rapidly inactivates PAI-1 by a single cleavage of the bait peptide at R346-M347. In circulation, most PAI-1 is bound to vitronectin, which is also degraded by Pla
-
-
?
single-chain urokinase + H2O
?
activation
-
-
?
TAFI + H2O
TAFIa + ?
TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. Pla cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme Pla cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
YapE + H2O
?
Yersinia pestis autotransporter YapE protein
cleavage of YapE occurs in Yersinia pestis but not in the enteric Yersinia species, and requires the omptin Pla
-
?
YapG + H2O
?
Yersinia pestis autotransporter YapG protein
sites K512, (K548-R549) and K594-R595 represent the primary cleavage sites of YapG, whereas sites K'558 and K'604 represent the secondary alternative cleavage sites
-
?
alpha2-antiplasmin + H2O
?
-
Pla inactivates alpha2-antiplasmin
-
-
?
C3 protein of complement system + H2O
fragments of C3 protein of complement system
-
-
-
-
?
human alpha2-antiplasmin + H2O
fragments of alpha2-antiplasmin
-
-
-
-
?
plasminogen + H2O
plasmin + ?
plasminogen activator inhibitor-1 + H2O
?
-
PAI-1 is cleaved and inactivated by the Pla protease of Yersinia pestis in the lung airspace of C57BL/6 mice
-
-
?
Yersinia outer proteins + H2O
fragments of Yersinia outer proteins
-
-
-
-
?
additional information
?
-
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
activation
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
Pla also expresses a weak coagulase activity
-
-
?
plasminogen + H2O
plasmin + ?
-
activates plasminogen by cleaving the Arg560-Val561 bond
-
-
?
plasminogen + H2O
plasmin + ?
-
Pla has the additional ability to bind to the basement membrane component type IV collagen rendering adhesive properties to Yersina pestis cells
-
-
?
plasminogen + H2O
plasmin + ?
-
Pla belongs to the omptin family of enterobacterial surface proteases and is responsible for the highly efficient invasion of the plague bacterium from the subcutaneous infection site into the circulation
-
-
?
plasminogen + H2O
plasmin + ?
-
plasminogen activator is a surface virulence factor that contributes to the highly imvasive nature of the pathogen by binding various tissue matrix components
-
-
?
additional information
?
-
-
plasminogen activator Pla is essential for the spread of Yersinia pestis from the subcutaneous infection site into circulation, and the proteolytic activation of plasminogen is involved in virulence function. In addition to proteolysis plasminogen activator Pla promotes bacterial adhesion to mammalian extracellular matrices and epithelial cells as well as bacterial invasion into eukayotic cells. Laminin functions as an adhesion target for plasminogen activator Pla, which also expresses a lower adhesion affinity for heparan sulfate proteoglycan. the adhesion targets are not directly degraded by plasminogen activator Pla, but Pla-mediated generation of plasmin leads to their degradation
-
-
?
additional information
?
-
-
plasminogen activator plays a pivotal role in internalisation of bacteria by HeLa cells. Intracellular signalling and cytoskeletal rearrangement is involved in Yersinia pestis plasminogen activator mediated HeLa cell invasion
-
-
?
additional information
?
-
-
the invasion of alveolar macrophages by Yersinia pestis depends both in vitro and in vivo on the expression of plasminogen activator Pla. Macrophages and transfectants expressing C-type lectin receptor DEC-205, but not their negative counterparts, phagocytose plasminogen activator Pla-expressing Yersinia pestis and Escherichia coli K12 more efficiently than Pla-negative controls. The interactions between Pla-expressing bacteria and DEC-205-expressing transfectants or alveolar macrophages can be inhibited by an anti-DEC-205 antibody. The blockage of the Pla-DEC-205 interaction reduces the dissemination of Yersinia pestis in mice
-
-
?
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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
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
evolution
the enzyme belongs to the omptin family of enzymes
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
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
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
Pla of the enteropathogen Yersinia pestis is a surface-exposed, transmembrane beta-barrel proteases of the omptin family that exhibit a complex array of interactions with the hemostatic systems in vitro, the protease is an established virulence factor. Pla favors fibrinolysis by direct activation of plasminogen, inactivation of the serpins plasminogen activator inhibitor-1 and alpha2-antiplasmin, inactivation of the thrombin-activable fibrinolysis inhibitor, and activation of single-chain urokinase. Inactivation of alpha2AP enables proteolysis by the Pla-generated plasmin. The enzymatic activity of the protease is strongly influenced by the environment-induced variations in lipopolysaccharide that binds to the beta-barrel. The protease cleaves the tissue factor pathway inhibitor and thus also expresses procoagulant activity. Some of the functions observed for Pla, such as adhesiveness to laminin and invasiveness into human cells as well as efficient plasmin generation are not shown by PgtE (EC 3.4.23.49) or OmpT. Pla is adapted to support efficient plasminogen activation in the bubonic plague and to enhance bacterial survival in the lungs
physiological function
the activity of the plasminogen activator protease Pla is the key to the progression of infection of Yersinia pestis in humans. Enzyme Pla facilitates type 3 secretion into primary alveolar macrophages but not into the commonly used THP-1 cell line. Analysis of the role of Pla in promoting optimal type 3 secretion using primary human tissue with relevant host cell heterogeneity in human precision-cut lung slices, a model of living tissue. Pla is a key player in the early host/pathogen interactions and a key virulence factor. Pla plays a role in adherence to alveolar macrophages that may not be detected using immortalized cell lines
physiological function
the plasminogen activator Pla is a protease that promotes fibrin degradation and prevents T cell-mediated defense against fully virulent Yersinia pestis. Pla functions to thwart fibrin-dependent T-cell-mediated defense against plague by promoting fibrinolysis. The presence of primed CD8 T-cells can suffice to protect against a lethal dose (LD) of a virulent Yersinia pestis strain rendered deficient in Pla activity in a fibrin-dependent manner
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
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
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
physiological function
-
1. Pla expression results in attenuated inflammatory cell recruitment (particularly neutrophils) to infected lesions 2. Pla expression causes a structural derangement of infected lymph tissue characterized by lymphadenitis, necrosis, hemorrhage, thrombosis, and disorganized masses of infiltrating bacteria. 3. Pla expression promotes the systemic dissemination of the infection
physiological function
-
Pla works to accelerate the initiation phase of blood clotting by activating the first enzyme in blood clotting (factor VIIa) and inactivating its most important protease inhibitor in plasma (TFPI). This is highly reminiscent of the ability of Pla to activate plasminogen to plasmin and to inactivate its plasma inhibitor, alpha2-antiplasmin
physiological function
-
the outer membrane plasminogen activator Pla of Yersinia pestis is a central virulence factor in plague
physiological function
-
Yersinia pestis binding to fibronectin is mediated through Ail protein and plasminogen activator Pla
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
-
plasminogen activator inhibitor-1 (PAI-1) is an in vivo target of the Pla protease in the lungs during pneumonic plague. PAI-1 is a key regulator of the pulmonary innate immune response and contributes to the regulation of cytokine production and promotion of neutrophil recruitment during Yerisnia pestis respiratory infection. The inactivation of PAI-1 by Yersinia pestis alters the host environment to promote virulence. PAI-1 restricts the proliferation of Yersinia pestis in the absence of enzyme Pla
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Kienle, Z.; Emody, L.; Svanborg, C.; O'Toole, P.W.
Adhesive properties conferred by the plasminogen activator of Yersinia pestis
J. Gen. Microbiol.
138
1679-1687
1992
Yersinia pestis
-
brenda
Lahteenmaki, K.; Virkola, R.; Saren, A.; Emody, L.; Korhonen, T.K.
Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix
Infect. Immun.
66
5755-5762
1998
Yersinia pestis
brenda
Kutyrev, V.; Mehigh, R.J.; Motin, V.L.; Pokrovskaya, M.S.; Smirnov, G.B.; Brubaker, R.R.
Expression of the plague plasminogen activator in Yersinia pseudotuberculosis and Escherichia coli
Infect. Immun.
67
1359-1367
1999
Yersinia pestis
brenda
Lahteenmaki, K.; Kukkonen, M.; Korhonen, T.K.
The Pla surface protease/adhesin of Yersinia pestis mediates bacterial invasion into human endothelial cells
FEBS Lett.
504
69-72
2001
Yersinia pestis
brenda
Kukkonen, M.; Lahteenmaki, K.; Suomalainen, M.; Kalkkinen, N.; Emody, L.; Lang, H.; Korhonen, T.K.
Protein regions important for plasminogen activation and inactivation of a2-antiplasmin in the surface protease Pla of Yersinia pestis
Mol. Microbiol.
40
1097-1111
2001
Yersinia pestis
brenda
Lahteenmaki, K.; Kuusela, P.; Korhonen, T.K.
Bacterial plasminogen activators and receptors
FEMS Microbiol. Rev.
25
531-552
2001
Mammalia, Mycobacterium tuberculosis, Yersinia pestis, Streptococcus uberis
brenda
Benedek, O.; Bene, J.; Melegh, B.; Emody, L.
Mapping of possible laminin binding sites of Y. pestis plasminogen activator (Pla) via phage display
Adv. Exp. Med. Biol.
529
101-104
2003
Yersinia pestis
brenda
Lobo, L.A.
Adhesive properties of the purified plasminogen activator Pla of Yersinia pestis
FEMS Microbiol. Lett.
262
158-162
2006
Yersinia pestis
brenda
Korhonen, T.K.; Lahteenmaki, K.; Kukkonen, M.; Lang, H.
Plasminogen activator of Yersinia pestis
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
217-219
2004
Yersinia pestis
-
brenda
Benedek, O.; Khan, A.S.; Schneider, G.; Nagy, G.; Autar, R.; Pieters, R.J.; Emody, L.
Identification of laminin-binding motifs of Yersinia pestis plasminogen activator by phage display
Int. J. Med. Microbiol.
295
87-98
2005
Yersinia pestis
brenda
Chromy, B.A.; Choi, M.W.; Murphy, G.A.; Gonzales, A.D.; Corzett, C.H.; Chang, B.C.; Fitch, J.P.; McCutchen-Maloney, S.L.
Proteomic characterization of Yersinia pestis virulence
J. Bacteriol.
187
8172-8180
2005
Yersinia pestis
brenda
Benedek, O.; Nagy, G.; Emody, L.
Intracellular signalling and cytoskeletal rearrangement involved in Yersinia pestis plasminogen activator (Pla) mediated HeLa cell invasion
Microb. Pathog.
37
47-54
2004
Yersinia pestis
brenda
Agarkov, A.; Chauhan, S.; Lory, P.J.; Gilbertson, S.R.; Motin, V.L.
Substrate specificity and screening of the integral membrane protease Pla
Bioorg. Med. Chem. Lett.
18
427-431
2008
Yersinia pestis (P17811), Yersinia pestis
brenda
Lathem, W.W.; Price, P.A.; Miller, V.L.; Goldman, W.E.
A plasminogen-activating protease specifically controls the development of primary pneumonic plague
Science
315
509-513
2007
Yersinia pestis (P17811), Yersinia pestis
brenda
Matero, P.; Pasanen, T.; Laukkanen, R.; Tissari, P.; Tarkka, E.; Vaara, M.; Skurnik, M.
Real-time multiplex PCR assay for detection of Yersinia pestis and Yersinia pseudotuberculosis
APMIS
117
34-44
2009
Yersinia pestis
brenda
Zhang, S.S.; Park, C.G.; Zhang, P.; Bartra, S.S.; Plano, G.V.; Klena, J.D.; Skurnik, M.; Hinnebusch, B.J.; Chen, T.
Plasminogen activator Pla of Yersinia pestis utilizes murine DEC-205 (CD205) as a receptor to promote dissemination
J. Biol. Chem.
283
31511-31521
2008
Yersinia pestis
brenda
Yun, T.; Morrissey, J.
Polyphosphate and omptins: Novel bacterial procoagulant agents
J. Cell. Mol. Med.
13
4146-4153
2009
Yersinia pestis
brenda
Tsang, T.M.; Felek, S.; Krukonis, E.S.
Ail binding to fibronectin facilitates Yersinia pestis binding to host cells and Yop delivery
Infect. Immun.
78
3358-3368
2010
Yersinia pestis
brenda
Haiko, J.; Kukkonen, M.; Ravantti, J.J.; Westerlund-Wikstroem, B.; Korhonen, T.K.
The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity
J. Bacteriol.
191
4758-4766
2009
Yersinia pestis
brenda
Feodorova, V.; Pankina, L.; Savostina, E.; Kuznetsov, O.; Konnov, N.; Sayapina, L.; Dentovskaya, S.; Shaikhutdinova, R.; Ageev, S.; Lindner, B.; Kondakova, A.; Kocharova, N.; Senchenkova, S.; Holst, O.; Pier, G.; Knirel, Y.; Anisimov, A.; Motin, V.
Yersinia pestis live vaccine with improved characteristics
Procedia Vaccinol.
1
97-100
2009
Yersinia pestis
-
brenda
Haiko, J.; Laakkonen, L.; Westerlund-Wikstroem, B.; Korhonen, T.K.
Molecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor Pla
BMC Evol. Biol.
11
43
2011
Yersinia pestis (P17811)
brenda
Eren, E.; Murphy, M.; Goguen, J.; van den Berg, B.
An active site water network in the plasminogen activator pla from Yersinia pestis
Structure
18
809-818
2010
Yersinia pestis (P17811), Yersinia pestis
brenda
Eren, E.; Van Den Berg, B.
Structural basis for activation of an integral membrane protease by lipopolysaccharide
J. Biol. Chem.
287
23971-23976
2012
Yersinia pestis (P17811)
brenda
Ruback, E.; Lobo, L.A.; Franca, T.C.; Pascutti, P.G.
Structural analysis of Pla protein from the biological warfare agent Yersinia pestis: docking and molecular dynamics of interactions with the mammalian plasminogen system
J. Biomol. Struct. Dyn.
31
477-484
2013
Yersinia pestis
brenda
Lane, M.C.; Lenz, J.D.; Miller, V.L.
Proteolytic processing of the Yersinia pestis YapG autotransporter by the omptin protease Pla and the contribution of YapG to murine plague pathogenesis
J. Med. Microbiol.
62
1124-1134
2013
Yersinia pestis (P17811)
brenda
van Lier, C.J.; Tiner, B.L.; Chauhan, S.; Motin, V.L.; Fitts, E.C.; Huante, M.B.; Endsley, J.J.; Ponnusamy, D.; Sha, J.; Chopra, A.K.
Further characterization of a highly attenuated Yersinia pestis CO92 mutant deleted for the genes encoding Braun lipoprotein and plasminogen activator protease in murine alveolar and primary human macrophages
Microb. Pathog.
80
27-38
2015
Yersinia pestis
brenda
Lawrenz, M.B.; Pennington, J.; Miller, V.L.
Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestis
Mol. Microbiol.
89
276-287
2013
Yersinia pestis (P17811)
brenda
Simon, S.; Demeure, C.; Lamourette, P.; Filali, S.; Plaisance, M.; Creminon, C.; Volland, H.; Carniel, E.
Fast and simple detection of Yersinia pestis applicable to field investigation of plague foci
PLoS ONE
8
e54947
2013
Yersinia pestis
brenda
Brannon, J.R.; Burk, D.L.; Leclerc, J.M.; Thomassin, J.L.; Portt, A.; Berghuis, A.M.; Gruenheid, S.; Le Moual, H.
Inhibition of outer membrane proteases of the omptin family by aprotinin
Infect. Immun.
83
2300-2311
2015
Yersinia pestis (P17811)
brenda
Smiley, S.T.; Szaba, F.M.; Kummer, L.W.; Duso, D.K.; Lin, J.S.
Yersinia pestis Pla protein thwarts T cell defense against plague
Infect. Immun.
87
e00126-19
2019
Yersinia pestis (P17811), Yersinia pestis, Yersinia pestis D27 (P17811)
brenda
Banerjee, S.K.; Huckuntod, S.D.; Mills, S.D.; Kurten, R.C.; Pechous, R.D.
Modeling pneumonic plague in human precision-cut lung slices highlights a role for the plasminogen activator protease in facilitating type 3 secretion
Infect. Immun.
87
e00175-19
2019
Yersinia pestis (P17811), Yersinia pestis
brenda
Korhonen, T.K.
Fibrinolytic and procoagulant activities of Yersinia pestis and Salmonella enterica
J. Thromb. Haemost.
13 Suppl 1
S115-S120
2015
Yersinia pestis (P17811)
brenda
Eddy, J.L.; Schroeder, J.A.; Zimbler, D.L.; Caulfield, A.J.; Lathem, W.W.
Proteolysis of plasminogen activator inhibitor-1 by Yersinia pestis remodulates the host environment to promote virulence
J. Thromb. Haemost.
14
1833-1843
2016
Yersinia pestis, Yersinia pestis CO92
brenda
Feodorova, V.A.; Lyapina, A.M.; Zaitsev, S.S.; Khizhnyakova, M.A.; Sayapina, L.V.; Ulianova, O.V.; Ulyanov, S.S.; Motin, V.L.
New promising targets for synthetic omptin-based peptide vaccine against Gram-negative pathogens
Vaccines (Basel)
7
E36
2019
Yersinia pestis (P17811), Yersinia pestis CO92 (P17811)
brenda