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Information on EC 3.4.22.B19 - YopJ protease
for references in articles please use BRENDA:EC3.4.22.B19preliminary BRENDA-supplied EC number
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EC Tree
3.4.22.B19 YopJ proteaseSpecify your search results
Word Map
- 3.4.22.B19
- enterocolitica
- pestis
- pseudotuberculosis
- plague
-
yersinia-infected
-
listeriolysin
-
iii-dependent
The enzyme appears in viruses and cellular organisms
Reaction Schemes
cleaves reversible post-translational modification in form of ubiquitin or a ubiquitin-like protein. It inhibits the host immune response and induces apoptosis by blocking multiple signaling pathways, including the MAPK and NfkappaB pathways in the infected cell
Synonyms
yersinia outer protein, virulence factor yopj, yersinia outer protein j, yersinia outer protein p, yersinia outer protein t, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C55.001
-
-
-
-
virulence factor YopJ
-
-
-
-
Yersinia outer protein
Yersinia outer protein J
Yersinia outer protein P
YopJ
YopJKIM
YopP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleaves reversible post-translational modification in form of ubiquitin or a ubiquitin-like protein. It inhibits the host immune response and induces apoptosis by blocking multiple signaling pathways, including the MAPK and NfkappaB pathways in the infected cell
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
355808-07-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
-
-
-
-
?
TRAF2-ubiquitin + H2O
TRAF2 + ubiquitin
-
YopJ is a promiscuous deubiquitinating enzyme that negatively regulates signaling by removing ubiquitin moieties from proteins, such as TRAF2, TRAF6, and IkappaBalpha. YopJ cleaves both K48- and K63-linked polyubiquitin
-
-
?
TRAF3-ubiquitin + H2O
TRAF3 + ubiquitin
-
YopJ is a deubiquitinating protease that acts on TRAF proteins to prevent or remove the K63-polymerized ubiquitin conjugates required for signal transduction
-
-
?
TRAF6-ubiquitin + H2O
TRAF6 + ubiquitin
-
YopJ is a deubiquitinating protease that acts on TRAF proteins to prevent or remove the K63-polymerized ubiquitin conjugates required for signal transduction
-
-
?
TRAF6-ubiquitin + H2O
TRAF6 + ubiquitin
-
YopJ is a promiscuous deubiquitinating enzyme that negatively regulates signaling by removing ubiquitin moieties from proteins, such as TRAF2, TRAF6, and IkappaBalpha. YopJ cleaves both K48- and K63-linked polyubiquitin
-
-
?
additional information
?
-
-
pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
-
-
?
additional information
?
-
-
interaction of Yersinia pestis with macrophages, limitations in YopJ-dependent apoptosis
-
-
?
additional information
?
-
-
pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
-
-
?
additional information
?
-
-
mice infected with wild-type strain of Yersinia pseudotuberculosis show the highest TNF-alpha production on the 21st day after infection in the culture supernatant of cells incubated with LPS. During the infection with mutant strains unable to secrete YopJ, there is no TNF-alpha production on both the 7th and 28th days after infection, but the production is increased on the 21st day with the cells incubated with LPS and HKY (2.1fold higher than the control group)
-
-
?
additional information
?
-
-
pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
-
-
?
additional information
?
-
-
no cleavage of (SUMO-1)-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the virulence factor YopJ cleaves reversibly post-translational modification in form of ubiquitin or a ubiquitin-like protein. It inhibits the host immune response and induces apoptosis by blocking multiple signaling pathways, including the MAPK and NfkappaB pathways in the infected cell
-
-
?
additional information
?
-
-
substrates are highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ protease exerts its pathogenic effect on cells by disrupting this posttranslational modification
-
-
?
additional information
?
-
-
YopJ is delivered into the target host cytosol via a type III secretion system. YopJ blocks activation of the superfamily of MAPK kinases, including MKKs and IKKbeta. The inhibition results in the inability of the cell to produce cytokines and antiapoptotic machinery
-
-
?
additional information
?
-
-
YopJ uses acetyl-coenzyme A to modify the critical serine and threonine residues in the activation loop of MAPKK6 and thereby blocking phosphorylation
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
TRAF3-ubiquitin + H2O
TRAF3 + ubiquitin
-
YopJ is a deubiquitinating protease that acts on TRAF proteins to prevent or remove the K63-polymerized ubiquitin conjugates required for signal transduction
-
-
?
TRAF2-ubiquitin + H2O
TRAF2 + ubiquitin
-
YopJ is a promiscuous deubiquitinating enzyme that negatively regulates signaling by removing ubiquitin moieties from proteins, such as TRAF2, TRAF6, and IkappaBalpha. YopJ cleaves both K48- and K63-linked polyubiquitin
-
-
?
TRAF6-ubiquitin + H2O
TRAF6 + ubiquitin
-
YopJ is a deubiquitinating protease that acts on TRAF proteins to prevent or remove the K63-polymerized ubiquitin conjugates required for signal transduction
-
-
?
TRAF6-ubiquitin + H2O
TRAF6 + ubiquitin
-
YopJ is a promiscuous deubiquitinating enzyme that negatively regulates signaling by removing ubiquitin moieties from proteins, such as TRAF2, TRAF6, and IkappaBalpha. YopJ cleaves both K48- and K63-linked polyubiquitin
-
-
?
additional information
?
-
-
pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
-
-
?
additional information
?
-
-
interaction of Yersinia pestis with macrophages, limitations in YopJ-dependent apoptosis
-
-
?
additional information
?
-
-
pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
-
-
?
additional information
?
-
-
mice infected with wild-type strain of Yersinia pseudotuberculosis show the highest TNF-alpha production on the 21st day after infection in the culture supernatant of cells incubated with LPS. During the infection with mutant strains unable to secrete YopJ, there is no TNF-alpha production on both the 7th and 28th days after infection, but the production is increased on the 21st day with the cells incubated with LPS and HKY (2.1fold higher than the control group)
-
-
?
additional information
?
-
-
pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
-
-
?
additional information
?
-
-
the virulence factor YopJ cleaves reversibly post-translational modification in form of ubiquitin or a ubiquitin-like protein. It inhibits the host immune response and induces apoptosis by blocking multiple signaling pathways, including the MAPK and NfkappaB pathways in the infected cell
-
-
?
additional information
?
-
-
substrates are highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ protease exerts its pathogenic effect on cells by disrupting this posttranslational modification
-
-
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Amebiasis
Oral vaccination with recombinant Yersinia enterocolitica expressing hybrid type III proteins protects gerbils from amebic liver abscess.
Bacterial Infections
Yersinia YopJ negatively regulates IRF3-mediated antibacterial response through disruption of STING-mediated cytosolic DNA signaling.
Hepatitis E
New route for fast detection of antibodies against zoonotic pathogens in sera of slaughtered pigs by means of flow-through chemiluminescence immunochips.
Infections
Pre-existing anti-Salmonella vector immunity prevents the development of protective antigen-specific CD8 T-cell frequencies against murine listeriosis.
Infections
Rapid clearance of a recombinant Salmonella vaccine carrier prevents enhanced antigen-specific CD8 T-cell responses after oral boost immunizations.
Infections
Tumor necrosis factor-alpha expression induced by anti-YopB antibodies coincides with protection against Yersinia enterocolitica infection in mice.
Infections
Yersinia outer protein P inhibits CD8 T cell priming in the mouse infection model.
Infections
Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation.
Liver Abscess, Amebic
Attenuated recombinant Yersinia as live oral vaccine carrier to protect against amoebiasis.
Liver Abscess, Amebic
Oral vaccination with recombinant Yersinia enterocolitica expressing hybrid type III proteins protects gerbils from amebic liver abscess.
Neoplasms
Tumor necrosis factor-alpha expression induced by anti-YopB antibodies coincides with protection against Yersinia enterocolitica infection in mice.
Persistent Infection
Yersinia YopJ negatively regulates IRF3-mediated antibacterial response through disruption of STING-mediated cytosolic DNA signaling.
Plague
Antigenic profiling of yersinia pestis infection in the Wyoming coyote (Canis latrans).
Plague
High-resolution structure of the Yersinia pestis protein tyrosine phosphatase YopH in complex with a phosphotyrosyl mimetic-containing hexapeptide.
Yersinia Infections
Serological crossreactivity between Brucella abortus and Yersinia enterocolitica 0:9 II the use of Yersinia outer proteins for the specific detection of Yersinia enterocolitica infections in ruminants.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serogroup O:1 strain 32777 (previously known as IP2777)
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-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
-
different Yersinia strains exhibit a range of cytotoxic activities on macrophages and this heterogeneity has been linked to allelic variation of genes encoding YopJ/YopP proteins, overview
evolution
-
different Yersinia strains exhibit a range of cytotoxic activities on macrophages and this heterogeneity has been linked to allelic variation of genes encoding YopJ/YopP proteins, overview
-
metabolism
-
mechanism of enzme YopJKIM-induced cell death, caspase-1 activation, and IL-1beta secretion in primary murine macrophages, overview. Caspase-3/7 activity is low and the caspase-3 substrate poly (ADP-ribose) polymerase is not cleaved in Yersinia pestis KIM5-infected macrophages. Enzyme YopJKIM-mediated cell death and caspase-1 activation occur independent of mitochondrial-directed apoptosis, Apoptotic signaling through caspase-8 and mitochondria is dispensable for KIM5-induced macrophage death, RIP1 and reactive oxygen species are not required for YopJKIM-induced cell death or IL-beta secretion
metabolism
-
mechanism of enzme YopJKIM-induced cell death, caspase-1 activation, and IL-1beta secretion in primary murine macrophages, overview. Caspase-3/7 activity is low and the caspase-3 substrate poly (ADP-ribose) polymerase is not cleaved in Yersinia pestis KIM5-infected macrophages. Enzyme YopJKIM-mediated cell death and caspase-1 activation occur independent of mitochondrial-directed apoptosis, Apoptotic signaling through caspase-8 and mitochondria is dispensable for KIM5-induced macrophage death, RIP1 and reactive oxygen species are not required for YopJKIM-induced cell death or IL-beta secretion
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physiological function
-
expression of YopP in Yersinia pestis enhances its cytotoxicity in macrophages and reduces its virulence
physiological function
-
when expressed in Schizosaccharomyces pombe, YopJ sensitizes cells to osmotic and oxidative stresses through a Hri2-dependent mechanism, however, when co-expressed with Yersinia protein kinase A, YopJ protects cells from Yersinia protein kinase A-mediated toxicity, and this protection is entirely dependent on Hri2. YopJ does not confer protection against the toxic effects of the Yersinia virulence factor YopE
physiological function
-
Yersinia YopJ induces caspase activation in J774A.1 macrophages and human monocyte-derived macrophages. YopJ does not induce pronounced apoptosis in human neutrophils
physiological function
-
YopJ deactivates MAPK- and NF-kappaB signaling pathways, and induces apoptosis of immune cells, YopJ inhibits the c-JNK pathway, attenuates the inflammatory responses, and interferes with the cell apoptotic process. When YopJ is replaced with YopP, the YopP-expressing Yersinia pestis strain exhibits high cytotoxic activity against macrophages
physiological function
-
YopJ kills macrophages and dendritic cells, reduces their production of tumor necrosis factor alpha and interleukin-12, and promotes systemic colonization in mouse models of intestinal Yersinia infection. YopJ-promoted cytotoxicity and systemic colonization are associated with significant increases in neutrophils in spleens and the proinflammatory cytokines interleukin-18 and gamma interferon in serum samples of mice vaccinated with Yersinia pseudotuberculosis. A proinflammatory, rather than anti-inflammatory, process accompanies YopJ-promoted cytotoxicity leading to increased systemic colonization by Yersinia pseudotuberculosis and potentially enhancing adaptive immunity to a live vaccine
physiological function
-
YopP induces caspase activation in J774A.1 macrophages and human monocyte-derived macrophages. YopP does not induce pronounced apoptosis in human neutrophils
physiological function
-
YopT from Yersinia enterocolitica induces klf2 mRNA expression in cell lines of macrophage and epithelial origin
physiological function
-
YopT is a cysteine protease which cleaves Rho proteins directly upstream of the post-translationally modified cysteine. Thereby, it releases the GTPases from the membrane leading to their inactivation
physiological function
-
the enzyme YopJ is involved in the reduction of maturation markers and immunostimulatory capacity of infected dendritic cells, together with enzymes YopH and mainly YopE, which contributes to the ability of Yersinia pseudotuberculosis to evade adaptive immune responses and subsequently inhibit the host's ability to clear the infection, overview
physiological function
-
Yersinia outer protein J is a type III secretion system effector of pathogenic Yersinia, i.e. Yersinia pestis, Yersinia enterocolitica and Yersinia pseudotuberculosis, that is secreted into host cells. YopJ inhibits survival response pathways in macrophages, causing cell death. Allelic variation of enzyme YopJ is responsible for differential cytotoxicity in Yersinia strains. Enzme YopJKIM-induced macrophage death is associated with caspase-1 activation and interleukin-1beta secretion
physiological function
-
deletion of gene YopJ results in significantly increased IL-8 production. Plasmid-encoded effector Yop proteins, particularly YopJ, prevent IL-8 secretion by human polymorphonuclear leukocytes
physiological function
-
Yersinia outer protein J is a type III secretion system effector of pathogenic Yersinia, i.e. Yersinia pestis, Yersinia enterocolitica and Yersinia pseudotuberculosis, that is secreted into host cells. YopJ inhibits survival response pathways in macrophages, causing cell death. Allelic variation of enzyme YopJ is responsible for differential cytotoxicity in Yersinia strains. Enzme YopJKIM-induced macrophage death is associated with caspase-1 activation and interleukin-1beta secretion
-
physiological function
-
expression of YopP in Yersinia pestis enhances its cytotoxicity in macrophages and reduces its virulence
-
physiological function
-
YopP induces caspase activation in J774A.1 macrophages and human monocyte-derived macrophages. YopP does not induce pronounced apoptosis in human neutrophils
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C172A
C172A
-
YopJ mutant C172A is inactive against ubiquitin-7-amido-4-methylcoumarin
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Galyov, E.E.; Haakansson, S.; Wolf-Watz, H.
Characterization of the operon encoding the YpkA Ser/Thr protein kinase and the YopJ protein of Yersinia pseudotuberculosis
J. Bacteriol.
176
4532-4548
1994
Yersinia pseudotuberculosis (P31498)
-
brenda
Krause, M.; Harwood, J.; Fierer, J.; Guiney, D.
Genetic analysis of homology between the virulence plasmids of Salmonella dublin and Yersinia pseudotuberculosis
Infect. Immun.
59
1860-1863
1991
Yersinia pseudotuberculosis (P31498)
brenda
Orth, K.; Xu, Z.; Mudgett, M.B.; Bao, Z.Q.; Palmer, L.E.; Bliska, J.B.; Mangel, W.F.; Staskawicz, B.; Dixon, J.E.
Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease
Science
290
1594-1597
2000
Yersinia sp.
brenda
Orth, K.
Function of the Yersinia effector YopJ
Curr. Opin. Microbiol.
5
38-43
2002
Yersinia sp.
brenda
Monnazzi, L.G.; Carlos, I.Z.; de Medeiros, B.M.
Influence of Yersinia pseudotuberculosis outer proteins (Yops) on interleukin-12, tumor necrosis factor alpha and nitric oxide production by peritoneal macrophages
Immunol. Lett.
94
91-98
2004
Yersinia pseudotuberculosis
brenda
Zauberman, A.; Cohen, S.; Mamroud, E.; Flashner, Y.; Tidhar, A.; Ber, R.; Elhanany, E.; Shafferman, A.; Velan, B.
Interaction of Yersinia pestis with macrophages: limitations in YopJ-dependent apoptosis
Infect. Immun.
74
3239-3250
2006
Yersinia pestis
brenda
Bliska, J.B.
Yersinia inhibits host signaling by acetylating MAPK kinases
ACS Chem. Biol.
1
349-351
2006
Yersinia pestis, Yersinia pseudotuberculosis, Yersinia enterocolitica
brenda
Sweet, C.R.; Conlon, J.; Golenbock, D.T.; Goguen, J.; Silverman, N.
YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction
Cell. Microbiol.
9
2700-2715
2007
Yersinia pestis
brenda
Zhou, H.; Monack, D.M.; Kayagaki, N.; Wertz, I.; Yin, J.; Wolf, B.; Dixit, V.M.
Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappaB activation
J. Exp. Med.
202
1327-1332
2005
Yersinia pseudotuberculosis
brenda
Sun, J.
Pathogenic bacterial proteins and their anti-inflammatory effects in the eukaryotic host
Antiinflamm. Antiallergy Agents Med. Chem.
8
214-227
2009
Yersinia sp.
brenda
Dach, K.; Zovko, J.; Hogardt, M.; Koch, I.; van Erp, K.; Heesemann, J.; Hoffmann, R.
Bacterial toxins induce sustained mRNA expression of the silencing transcription factor klf2 via inactivation of RhoA and Rhophilin 1
Infect. Immun.
77
5583-5592
2009
Yersinia enterocolitica
brenda
Zhang, Y.; Bliska, J.B.
YopJ-promoted cytotoxicity and systemic colonization are associated with high levels of murine interleukin-18, gamma interferon, and neutrophils in a live vaccine model of Yersinia pseudotuberculosis infection
Infect. Immun.
78
2329-2341
2010
Yersinia pseudotuberculosis
brenda
Wiley, D.J.; Shrestha, N.; Yang, J.; Atis, N.; Dayton, K.; Schesser, K.
The activities of the Yersinia protein kinase A (YpkA) and outer protein J (YopJ) virulence factors converge on an eIF2alpha kinase
J. Biol. Chem.
284
24744-24753
2009
Yersinia pestis
brenda
Zauberman, A.; Tidhar, A.; Levy, Y.; Bar-Haim, E.; Halperin, G.; Flashner, Y.; Cohen, S.; Shafferman, A.; Mamroud, E.
Yersinia pestis endowed with increased cytotoxicity is avirulent in a bubonic plague model and induces rapid protection against pneumonic plague
PLoS ONE
4
e5938
2009
Yersinia pestis, Yersinia pestis Kimberley53
brenda
Spinner, J.L.; Seo, K.S.; OLoughlin, J.L.; Cundiff, J.A.; Minnich, S.A.; Bohach, G.A.; Kobayashi, S.D.
Neutrophils are resistant to Yersinia YopJ/P-induced apoptosis and are protected from ROS-mediated cell death by the type III secretion system
PLoS ONE
5
e9279
2010
Yersinia pestis, Yersinia enterocolitica, Yersinia enterocolitica 8081v
brenda
Schmidt, G.
Yersinia enterocolitica outer protein T (YopT)
Eur. J. Cell Biol.
90
955-958
2011
Yersinia enterocolitica
brenda
Tansini, A.; Da Silva, F.; Dos Santos Jr., R.; Placeres, M.; De Medeiros, B.; Carlos, I.
Yop effector proteins from Yersinia pseudotuberculosis impair dendritic cell activation
Adv. Exp. Med. Biol.
954
203-208
2012
Yersinia pseudotuberculosis
brenda
Zheng, Y.; Lilo, S.; Mena, P.; Bliska, J.B.
YopJ-induced caspase-1 activation in Yersinia-infected macrophages: independent of apoptosis, linked to necrosis, dispensable for innate host defense
PLoS ONE
7
e36019
2012
Yersinia pestis, Yersinia pestis KIM5
brenda
Spinner, J.; Hasenkrug, A.; Shannon, J.; Kobayashi, S.; Hinnebusch, B.
Role of the Yersinia YopJ protein in suppressing interleukin-8 secretion by human polymorphonuclear leukocytes
Microbes Infect.
18
21-29
2016
Yersinia pestis
brenda
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