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Volumn 84, Issue 4, 2016, Pages 1062-1072

Uncovering an important role for YopJ in the inhibition of caspase-1 in activated macrophages and promoting Yersinia pseudotuberculosis virulence

Author keywords

[No Author keywords available]

Indexed keywords

INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; LIPOPOLYSACCHARIDE; BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN; YOPM PROTEIN, YERSINIA; YOPP PROTEIN, YERSINIA;

EID: 84962821741     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00843-15     Document Type: Article
Times cited : (20)

References (65)
  • 1
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov R. 2007. Recognition of microorganisms and activation of the immune response. Nature 449:819-826. http://dx.doi.org/10.1038/nature06246.
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 2
    • 84919818703 scopus 로고    scopus 로고
    • NOD-like receptors: versatile cytosolic sentinels
    • Motta V, Soares F, Sun T, Philpott DJ. 2015. NOD-like receptors: versatile cytosolic sentinels. Physiol Rev 95:149-178. http://dx.doi.org/10.1152/physrev.00009.2014.
    • (2015) Physiol Rev , vol.95 , pp. 149-178
    • Motta, V.1    Soares, F.2    Sun, T.3    Philpott, D.J.4
  • 3
    • 77955906264 scopus 로고    scopus 로고
    • The nuclear factor NF-κB pathway in inflammation
    • Lawrence T. 2009. The nuclear factor NF-κB pathway in inflammation. Cold Spring Harb Perspect Biol 1:a001651. http://dx.doi.org/10.1101/cshperspect.a001651.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Lawrence, T.1
  • 4
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-κB by Toll-like receptors
    • Kawai T, Akira S. 2007. Signaling to NF-κB by Toll-like receptors. Trends Mol Med 13:460-469. http://dx.doi.org/10.1016/j.molmed.2007.09.002.
    • (2007) Trends Mol Med , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 5
    • 32944462309 scopus 로고    scopus 로고
    • Anti-immunology: evasion of the host immune system by bacterial and viral pathogens
    • Finlay BB, McFadden G. 2006. Anti-immunology: evasion of the host immune system by bacterial and viral pathogens. Cell 124:767-782. http://dx.doi.org/10.1016/j.cell.2006.01.034.
    • (2006) Cell , vol.124 , pp. 767-782
    • Finlay, B.B.1    McFadden, G.2
  • 6
    • 33646942975 scopus 로고    scopus 로고
    • Host-pathogen interactions: a biological rendez-vous of the infectious nonself and danger models?
    • Tournier JN, Quesnel-Hellmann A. 2006. Host-pathogen interactions: a biological rendez-vous of the infectious nonself and danger models? PLoS Pathog 2:e44. http://dx.doi.org/10.1371/journal.ppat.0020044.
    • (2006) PLoS Pathog , vol.2
    • Tournier, J.N.1    Quesnel-Hellmann, A.2
  • 7
    • 26844521751 scopus 로고    scopus 로고
    • Type III secretion: more systems than you think
    • Troisfontaines P, Cornelis GR. 2005. Type III secretion: more systems than you think. Physiology (Bethesda) 20:326-339. http://dx.doi.org/10.1152/physiol.00011.2005.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 326-339
    • Troisfontaines, P.1    Cornelis, G.R.2
  • 8
    • 84881029343 scopus 로고    scopus 로고
    • Subversion of trafficking, apoptosis, and innate immunity by type III secretion system effectors
    • Raymond B, Young JC, Pallett M, Endres RG, Clements A, Frankel G. 2013. Subversion of trafficking, apoptosis, and innate immunity by type III secretion system effectors. Trends Microbiol 21:430-441. http://dx.doi.org/10.1016/j.tim.2013.06.008.
    • (2013) Trends Microbiol , vol.21 , pp. 430-441
    • Raymond, B.1    Young, J.C.2    Pallett, M.3    Endres, R.G.4    Clements, A.5    Frankel, G.6
  • 9
    • 84857546470 scopus 로고    scopus 로고
    • Beyond pattern recognition: five immune checkpoints for scaling the microbial threat
    • Blander JM, Sander LE. 2012. Beyond pattern recognition: five immune checkpoints for scaling the microbial threat. Nat Rev Immunol 12:215-225. http://dx.doi.org/10.1038/nri3167.
    • (2012) Nat Rev Immunol , vol.12 , pp. 215-225
    • Blander, J.M.1    Sander, L.E.2
  • 10
    • 67651091732 scopus 로고    scopus 로고
    • Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system
    • Vance RE, Isberg RR, Portnoy DA. 2009. Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system. Cell Host Microbe 6:10-21. http://dx.doi.org/10.1016/j.chom.2009.06.007.
    • (2009) Cell Host Microbe , vol.6 , pp. 10-21
    • Vance, R.E.1    Isberg, R.R.2    Portnoy, D.A.3
  • 12
    • 84931567250 scopus 로고    scopus 로고
    • The inflammasome: learning from bacterial evasion strategies
    • Shin S, Brodsky IE. 2015. The inflammasome: learning from bacterial evasion strategies. Semin Immunol 27:102-110. http://dx.doi.org/10.1016/j.smim.2015.03.006.
    • (2015) Semin Immunol , vol.27 , pp. 102-110
    • Shin, S.1    Brodsky, I.E.2
  • 14
    • 84875813739 scopus 로고    scopus 로고
    • Inflammasomes and host defenses against bacterial infections
    • Vladimer GI, Marty-Roix R, Ghosh S, Weng D, Lien E. 2013. Inflammasomes and host defenses against bacterial infections. Curr Opin Microbiol 16:23-31. http://dx.doi.org/10.1016/j.mib.2012.11.008.
    • (2013) Curr Opin Microbiol , vol.16 , pp. 23-31
    • Vladimer, G.I.1    Marty-Roix, R.2    Ghosh, S.3    Weng, D.4    Lien, E.5
  • 15
    • 84858677223 scopus 로고    scopus 로고
    • Sensing and reacting to microbes through the inflammasomes
    • Franchi L, Munoz-Planillo R, Nunez G. 2012. Sensing and reacting to microbes through the inflammasomes. Nat Immunol 13:325-332. http://dx.doi.org/10.1038/ni.2231.
    • (2012) Nat Immunol , vol.13 , pp. 325-332
    • Franchi, L.1    Munoz-Planillo, R.2    Nunez, G.3
  • 16
    • 80052687210 scopus 로고    scopus 로고
    • Coordinated host responses during pyroptosis: caspase-1-dependent lysosome exocytosis and inflammatory cytokine maturation
    • Bergsbaken T, Fink SL, den Hartigh AB, Loomis WP, Cookson BT. 2011. Coordinated host responses during pyroptosis: caspase-1-dependent lysosome exocytosis and inflammatory cytokine maturation. J Immunol 187:2748-2754. http://dx.doi.org/10.4049/jimmunol.1100477.
    • (2011) J Immunol , vol.187 , pp. 2748-2754
    • Bergsbaken, T.1    Fink, S.L.2    den Hartigh, A.B.3    Loomis, W.P.4    Cookson, B.T.5
  • 17
    • 84872451259 scopus 로고    scopus 로고
    • The CARD plays a critical role in ASC foci formation and inflammasome signalling
    • Proell M, Gerlic M, Mace PD, Reed JC, Riedl SJ. 2013. The CARD plays a critical role in ASC foci formation and inflammasome signalling. Biochem J 449:613-621. http://dx.doi.org/10.1042/BJ20121198.
    • (2013) Biochem J , vol.449 , pp. 613-621
    • Proell, M.1    Gerlic, M.2    Mace, P.D.3    Reed, J.C.4    Riedl, S.J.5
  • 21
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES. 2012. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem 287:36617-36622. http://dx.doi.org/10.1074/jbc.M112.407130.
    • (2012) J Biol Chem , vol.287 , pp. 36617-36622
    • Juliana, C.1    Fernandes-Alnemri, T.2    Kang, S.3    Farias, A.4    Qin, F.5    Alnemri, E.S.6
  • 22
    • 40849116186 scopus 로고    scopus 로고
    • Biochemical functions of Yersinia type III effectors
    • Shao F. 2008. Biochemical functions of Yersinia type III effectors. Curr Opin Microbiol 11:21-29. http://dx.doi.org/10.1016/j.mib.2008.01.005.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 21-29
    • Shao, F.1
  • 23
    • 84884704592 scopus 로고    scopus 로고
    • Modulation of innate immune responses by Yersinia type III secretion system translocators and effectors
    • Bliska JB, Wang X, Viboud GI, Brodsky IE. 2013. Modulation of innate immune responses by Yersinia type III secretion system translocators and effectors. Cell Microbiol 15:1622-1631. http://dx.doi.org/10.1111/cmi.12164.
    • (2013) Cell Microbiol , vol.15 , pp. 1622-1631
    • Bliska, J.B.1    Wang, X.2    Viboud, G.I.3    Brodsky, I.E.4
  • 25
    • 25444476788 scopus 로고    scopus 로고
    • Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis
    • Viboud GI, Bliska JB. 2005. Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis. Annu Rev Microbiol 59: 69-89. http://dx.doi.org/10.1146/annurev.micro.59.030804.121320.
    • (2005) Annu Rev Microbiol , vol.59 , pp. 69-89
    • Viboud, G.I.1    Bliska, J.B.2
  • 26
    • 42949122126 scopus 로고    scopus 로고
    • Interaction between Yersinia pestis and the host immune system
    • Li B, Yang R. 2008. Interaction between Yersinia pestis and the host immune system. Infect Immun 76:1804-1811. http://dx.doi.org/10.1128/IAI.01517-07.
    • (2008) Infect Immun , vol.76 , pp. 1804-1811
    • Li, B.1    Yang, R.2
  • 27
    • 13444254004 scopus 로고    scopus 로고
    • Functions of the Yersinia effector proteins in inhibiting host immune responses
    • Navarro L, Alto NM, Dixon JE. 2005. Functions of the Yersinia effector proteins in inhibiting host immune responses. Curr Opin Microbiol 8:21-27 http://dx.doi.org/10.1016/j.mib.2004.12.014.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 21-27
    • Navarro, L.1    Alto, N.M.2    Dixon, J.E.3
  • 28
    • 84891484173 scopus 로고    scopus 로고
    • The Yersinia pestis type III secretion system: expression, assembly and role in the evasion of host defenses
    • Plano GV, Schesser K. 2013. The Yersinia pestis type III secretion system: expression, assembly and role in the evasion of host defenses. Immunol Res 57:237-245. http://dx.doi.org/10.1007/s12026-013-8454-3.
    • (2013) Immunol Res , vol.57 , pp. 237-245
    • Plano, G.V.1    Schesser, K.2
  • 29
    • 51949097139 scopus 로고    scopus 로고
    • Caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ
    • Lilo S, Zheng Y, Bliska JB. 2008. Caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ. Infect Immun 76:3911-3923. http://dx.doi.org/10.1128/IAI.01695-07.
    • (2008) Infect Immun , vol.76 , pp. 3911-3923
    • Lilo, S.1    Zheng, Y.2    Bliska, J.B.3
  • 30
    • 84924217271 scopus 로고    scopus 로고
    • Inflammasome activation in response to the Yersinia type III secretion system requires hyperinjection of translocon proteins YopB and YopD
    • Zwack EE, Snyder AG, Wynosky-Dolfi MA, Ruthel G, Philip NH, Marketon MM, Francis MS, Bliska JB, Brodsky IE. 2015. Inflammasome activation in response to the Yersinia type III secretion system requires hyperinjection of translocon proteins YopB and YopD. mBio 6:e02095-14 http://dx.doi.org/10.1128/mBio.02095-14.
    • (2015) mBio , vol.6
    • Zwack, E.E.1    Snyder, A.G.2    Wynosky-Dolfi, M.A.3    Ruthel, G.4    Philip, N.H.5    Marketon, M.M.6    Francis, M.S.7    Bliska, J.B.8    Brodsky, I.E.9
  • 31
    • 84908305287 scopus 로고    scopus 로고
    • IQGAP1 is important for activation of caspase-1 in macrophages and is targeted by Yersinia pestis type III effector YopM
    • Chung LK, Philip NH, Schmidt VA, Koller A, Strowig T, Flavell RA, Brodsky IE, Bliska JB. 2014. IQGAP1 is important for activation of caspase-1 in macrophages and is targeted by Yersinia pestis type III effector YopM. mBio 5:e01402-14. http://dx.doi.org/10.1128/mBio.01402-14.
    • (2014) mBio , vol.5
    • Chung, L.K.1    Philip, N.H.2    Schmidt, V.A.3    Koller, A.4    Strowig, T.5    Flavell, R.A.6    Brodsky, I.E.7    Bliska, J.B.8
  • 32
    • 2942537824 scopus 로고    scopus 로고
    • Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1beta
    • Schotte P, Denecker G, Van Den Broeke A, Vandenabeele P, Cornelis GR, Beyaert R. 2004. Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1beta. J Biol Chem 279:25134-25142. http://dx.doi.org/10.1074/jbc.M401245200.
    • (2004) J Biol Chem , vol.279 , pp. 25134-25142
    • Schotte, P.1    Denecker, G.2    Van Den Broeke, A.3    Vandenabeele, P.4    Cornelis, G.R.5    Beyaert, R.6
  • 34
    • 79955776183 scopus 로고    scopus 로고
    • A Yersinia effector with enhanced inhibitory activity on the NF-κB pathway activates the NLRP3/ASC/caspase-1 inflammasome in macrophages
    • Zheng Y, Lilo S, Brodsky IE, Zhang Y, Medzhitov R, Marcu KB, Bliska JB. 2011. A Yersinia effector with enhanced inhibitory activity on the NF-κB pathway activates the NLRP3/ASC/caspase-1 inflammasome in macrophages. PLoS Pathog 7:e1002026. http://dx.doi.org/10.1371/journal.ppat.1002026.
    • (2011) PLoS Pathog , vol.7
    • Zheng, Y.1    Lilo, S.2    Brodsky, I.E.3    Zhang, Y.4    Medzhitov, R.5    Marcu, K.B.6    Bliska, J.B.7
  • 36
    • 84871001488 scopus 로고    scopus 로고
    • The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing
    • LaRock CN, Cookson BT. 2012. The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing. Cell Host Microbe 12:799-805. http://dx.doi.org/10.1016/j.chom.2012.10.020.
    • (2012) Cell Host Microbe , vol.12 , pp. 799-805
    • LaRock, C.N.1    Cookson, B.T.2
  • 37
    • 84860354862 scopus 로고    scopus 로고
    • YopJ-induced caspase-1 activation in Yersinia-infected macrophages: independent of apoptosis, linked to necrosis, dispensable for innate host defense
    • Zheng Y, Lilo S, Mena P, Bliska JB. 2012. YopJ-induced caspase-1 activation in Yersinia-infected macrophages: independent of apoptosis, linked to necrosis, dispensable for innate host defense. PLoS One 7:e36019. http://dx.doi.org/10.1371/journal.pone.0036019.
    • (2012) PLoS One , vol.7
    • Zheng, Y.1    Lilo, S.2    Mena, P.3    Bliska, J.B.4
  • 38
    • 37349046671 scopus 로고    scopus 로고
    • Macrophage activation redirects Yersinia-infected host cell death from apoptosis to caspase-1-dependent pyroptosis
    • Bergsbaken T, Cookson BT. 2007. Macrophage activation redirects Yersinia-infected host cell death from apoptosis to caspase-1-dependent pyroptosis. PLoS Pathog 3:e161. http://dx.doi.org/10.1371/journal.ppat.0030161.
    • (2007) PLoS Pathog , vol.3
    • Bergsbaken, T.1    Cookson, B.T.2
  • 39
    • 33845480946 scopus 로고    scopus 로고
    • Acetylation of MEK2 and IκB kinase (IKK) activation loop residues by YopJ inhibits signaling
    • Mittal R, Peak-Chew SY, McMahon HT. 2006. Acetylation of MEK2 and IκB kinase (IKK) activation loop residues by YopJ inhibits signaling. Proc Natl Acad Sci U S A 103:18574-18579. http://dx.doi.org/10.1073/pnas.0608995103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18574-18579
    • Mittal, R.1    Peak-Chew, S.Y.2    McMahon, H.T.3
  • 40
    • 77953782586 scopus 로고    scopus 로고
    • The acetyltransferase activity of the bacterial toxin YopJ of Yersinia is activated by eukaryotic host cell inositol hexakisphosphate
    • Mittal R, Peak-Chew SY, Sade RS, Vallis Y, McMahon HT. 2010. The acetyltransferase activity of the bacterial toxin YopJ of Yersinia is activated by eukaryotic host cell inositol hexakisphosphate. J Biol Chem 285:19927-19934. http://dx.doi.org/10.1074/jbc.M110.126581.
    • (2010) J Biol Chem , vol.285 , pp. 19927-19934
    • Mittal, R.1    Peak-Chew, S.Y.2    Sade, R.S.3    Vallis, Y.4    McMahon, H.T.5
  • 42
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • Mukherjee S, Keitany G, Li Y, Wang Y, Ball HL, Goldsmith EJ, Orth K. 2006. Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312:1211-1214. http://dx.doi.org/10.1126/science.1126867.
    • (2006) Science , vol.312 , pp. 1211-1214
    • Mukherjee, S.1    Keitany, G.2    Li, Y.3    Wang, Y.4    Ball, H.L.5    Goldsmith, E.J.6    Orth, K.7
  • 43
    • 84881027178 scopus 로고    scopus 로고
    • Cell death programs in Yersinia immunity and pathogenesis
    • Philip NH, Brodsky IE. 2012. Cell death programs in Yersinia immunity and pathogenesis. Front Cell Infect Microbiol 2:149. http://dx.doi.org/10.3389/fcimb.2012.00149.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 149
    • Philip, N.H.1    Brodsky, I.E.2
  • 47
    • 44949187452 scopus 로고    scopus 로고
    • Reduced secretion of YopJ by Yersinia limits in vivo cell death but enhances bacterial virulence
    • Brodsky IE, Medzhitov R. 2008. Reduced secretion of YopJ by Yersinia limits in vivo cell death but enhances bacterial virulence. PLoS Pathog 4:e1000067. http://dx.doi.org/10.1371/journal.ppat.1000067.
    • (2008) PLoS Pathog , vol.4
    • Brodsky, I.E.1    Medzhitov, R.2
  • 48
    • 84872385200 scopus 로고    scopus 로고
    • YopK controls both rate and fidelity of Yop translocation
    • Dewoody R, Merritt PM, Marketon MM. 2013. YopK controls both rate and fidelity of Yop translocation. Mol Microbiol 87:301-317. http://dx.doi.org/10.1111/mmi.12099.
    • (2013) Mol Microbiol , vol.87 , pp. 301-317
    • Dewoody, R.1    Merritt, P.M.2    Marketon, M.M.3
  • 49
    • 3342884252 scopus 로고    scopus 로고
    • The plague virulence protein YopM targets the innate immune response by causing a global depletion of NK cells
    • Kerschen EJ, Cohen DA, Kaplan AM, Straley SC. 2004. The plague virulence protein YopM targets the innate immune response by causing a global depletion of NK cells. Infect Immun 72:4589-4602. http://dx.doi.org/10.1128/IAI.72.8.4589-4602.2004.
    • (2004) Infect Immun , vol.72 , pp. 4589-4602
    • Kerschen, E.J.1    Cohen, D.A.2    Kaplan, A.M.3    Straley, S.C.4
  • 50
    • 0038719729 scopus 로고    scopus 로고
    • The Yersinia virulence factor YopM forms a novel protein complex with two cellular kinases
    • McDonald C, Vacratsis PO, Bliska JB, Dixon JE. 2003. The Yersinia virulence factor YopM forms a novel protein complex with two cellular kinases. J Biol Chem 278:18514-18523. http://dx.doi.org/10.1074/jbc.M301226200.
    • (2003) J Biol Chem , vol.278 , pp. 18514-18523
    • McDonald, C.1    Vacratsis, P.O.2    Bliska, J.B.3    Dixon, J.E.4
  • 51
    • 77952678232 scopus 로고    scopus 로고
    • The C-terminal tail of Yersinia pseudotuberculosis YopM is critical for interacting with RSK1 and for virulence
    • McCoy MW, Marre ML, Lesser CF, Mecsas J. 2010. The C-terminal tail of Yersinia pseudotuberculosis YopM is critical for interacting with RSK1 and for virulence. Infect Immun 78:2584-2598. http://dx.doi.org/10.1128/IAI.00141-10.
    • (2010) Infect Immun , vol.78 , pp. 2584-2598
    • McCoy, M.W.1    Marre, M.L.2    Lesser, C.F.3    Mecsas, J.4
  • 52
    • 77955293133 scopus 로고    scopus 로고
    • Delineation of regions of the Yersinia YopM protein required for interaction with the RSK1 and PRK2 host kinases and their requirement for interleukin-10 production and virulence
    • McPhee JB, Mena P, Bliska JB. 2010. Delineation of regions of the Yersinia YopM protein required for interaction with the RSK1 and PRK2 host kinases and their requirement for interleukin-10 production and virulence. Infect Immun 78:3529-3539. http://dx.doi.org/10.1128/IAI.00269-10.
    • (2010) Infect Immun , vol.78 , pp. 3529-3539
    • McPhee, J.B.1    Mena, P.2    Bliska, J.B.3
  • 53
    • 78049236063 scopus 로고    scopus 로고
    • Yersinia virulence factor YopM induces sustained RSK activation by interfering with dephosphorylation
    • Hentschke M, Berneking L, Belmar Campos C, Buck F, Ruckdeschel K, Aepfelbacher M. 2010. Yersinia virulence factor YopM induces sustained RSK activation by interfering with dephosphorylation. PLoS One 5:e13165. http://dx.doi.org/10.1371/journal.pone.0013165.
    • (2010) PLoS One , vol.5
    • Hentschke, M.1    Berneking, L.2    Belmar Campos, C.3    Buck, F.4    Ruckdeschel, K.5    Aepfelbacher, M.6
  • 54
    • 51949083412 scopus 로고    scopus 로고
    • Type III secretion decreases bacterial and host survival following phagocytosis of Yersinia pseudotuberculosis by macrophages
    • Zhang Y, Murtha J, Roberts MA, Siegel RM, Bliska JB. 2008. Type III secretion decreases bacterial and host survival following phagocytosis of Yersinia pseudotuberculosis by macrophages. Infect Immun 76:4299-4310. http://dx.doi.org/10.1128/IAI.00183-08.
    • (2008) Infect Immun , vol.76 , pp. 4299-4310
    • Zhang, Y.1    Murtha, J.2    Roberts, M.A.3    Siegel, R.M.4    Bliska, J.B.5
  • 55
    • 33748192535 scopus 로고    scopus 로고
    • Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors
    • Prehna G, Ivanov MI, Bliska JB, Stebbins CE. 2006. Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell 126:869-880. http://dx.doi.org/10.1016/j.cell.2006.06.056.
    • (2006) Cell , vol.126 , pp. 869-880
    • Prehna, G.1    Ivanov, M.I.2    Bliska, J.B.3    Stebbins, C.E.4
  • 56
    • 0021183978 scopus 로고
    • Evidence for a gamma-interferon receptor that regulates macrophage tumoricidal activity
    • Celada A, Gray PW, Rinderknecht E, Schreiber RD. 1984. Evidence for a gamma-interferon receptor that regulates macrophage tumoricidal activity. J Exp Med 160:55-74. http://dx.doi.org/10.1084/jem.160.1.55.
    • (1984) J Exp Med , vol.160 , pp. 55-74
    • Celada, A.1    Gray, P.W.2    Rinderknecht, E.3    Schreiber, R.D.4
  • 57
    • 77951221762 scopus 로고    scopus 로고
    • 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
    • Zhang Y, Bliska JB. 2010. 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. http://dx.doi.org/10.1128/IAI.00094-10.
    • (2010) Infect Immun , vol.78 , pp. 2329-2341
    • Zhang, Y.1    Bliska, J.B.2
  • 58
    • 70350714459 scopus 로고    scopus 로고
    • Innate immune response during Yersinia infection: critical modulation of cell death mechanisms through phagocyte activation
    • Bergsbaken T, Cookson BT. 2009. Innate immune response during Yersinia infection: critical modulation of cell death mechanisms through phagocyte activation. J Leukoc Biol 86:1153-1158. http://dx.doi.org/10.1189/jlb.0309146.
    • (2009) J Leukoc Biol , vol.86 , pp. 1153-1158
    • Bergsbaken, T.1    Cookson, B.T.2
  • 60
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py BF, Kim MS, Vakifahmetoglu-Norberg H, Yuan J. 2013. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol Cell 49:331-338. http://dx.doi.org/10.1016/j.molcel.2012.11.009.
    • (2013) Mol Cell , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 61
    • 84876518121 scopus 로고    scopus 로고
    • Ribotoxic stress through p38 mitogen-activated protein kinase activates in vitro the human pyrin inflammasome
    • Yu JW, Farias A, Hwang I, Fernandes-Alnemri T, Alnemri ES. 2013. Ribotoxic stress through p38 mitogen-activated protein kinase activates in vitro the human pyrin inflammasome. J Biol Chem 288:11378-11383. http://dx.doi.org/10.1074/jbc.M112.448795.
    • (2013) J Biol Chem , vol.288 , pp. 11378-11383
    • Yu, J.W.1    Farias, A.2    Hwang, I.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5
  • 62
    • 84906075102 scopus 로고    scopus 로고
    • Integrin-mediated first signal for inflammasome activation in intestinal epithelial cells
    • Thinwa J, Segovia JA, Bose S, Dube PH. 2014. Integrin-mediated first signal for inflammasome activation in intestinal epithelial cells. J Immunol 193:1373-1382. http://dx.doi.org/10.4049/jimmunol.1400145.
    • (2014) J Immunol , vol.193 , pp. 1373-1382
    • Thinwa, J.1    Segovia, J.A.2    Bose, S.3    Dube, P.H.4
  • 63
    • 0033861270 scopus 로고    scopus 로고
    • The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence
    • Black DS, Bliska JB. 2000. The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence. Mol Microbiol 37:515-527.
    • (2000) Mol Microbiol , vol.37 , pp. 515-527
    • Black, D.S.1    Bliska, J.B.2
  • 65
    • 0026674958 scopus 로고
    • Invasin expression in Yersinia pseudotuberculosis
    • Simonet M, Falkow S. 1992. Invasin expression in Yersinia pseudotuberculosis. Infect Immun 60:4414-4417.
    • (1992) Infect Immun , vol.60 , pp. 4414-4417
    • Simonet, M.1    Falkow, S.2


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