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Volumn 48, Issue 1, 2010, Pages 42-52

Deletion of Braun lipoprotein gene (lpp) attenuates Yersinia pestis KIM/D27 strain: Role of Lpp in modulating host immune response, NF-κB activation and cell death

Author keywords

Apoptosis; Braun lipoprotein; Host immune response; Mouse model of infection; NF B; Yersinia pestis

Indexed keywords

BACTERIAL ANTIGEN; BACTERIAL VACCINE; BACTERIUM ANTIBODY; BRAUN LIPOPROTEIN; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 12; LIPOPROTEIN; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN E;

EID: 72149091437     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2009.09.002     Document Type: Article
Times cited : (15)

References (68)
  • 1
    • 0031029062 scopus 로고    scopus 로고
    • Yersinia pestis - etiologic agent of plague
    • Perry R.D., and Fetherston J.D. Yersinia pestis - etiologic agent of plague. Clin Microbiol Rev 10 (1997) 35-66
    • (1997) Clin Microbiol Rev , vol.10 , pp. 35-66
    • Perry, R.D.1    Fetherston, J.D.2
  • 2
    • 0034600229 scopus 로고    scopus 로고
    • Plague as a biological weapon: medical and public health management. Working Group on Civilian Biodefense
    • Inglesby T.V., Dennis D.T., Henderson D.A., Bartlett J.G., Ascher M.S., Eitzen E., et al. Plague as a biological weapon: medical and public health management. Working Group on Civilian Biodefense. JAMA 283 (2000) 2281-2290
    • (2000) JAMA , vol.283 , pp. 2281-2290
    • Inglesby, T.V.1    Dennis, D.T.2    Henderson, D.A.3    Bartlett, J.G.4    Ascher, M.S.5    Eitzen, E.6
  • 3
    • 0345700249 scopus 로고    scopus 로고
    • Synergistic protection of mice against plague with monoclonal antibodies specific for the F1 and V antigens of Yersinia pestis
    • Hill J., Copse C., Leary S., Stagg A.J., Williamson E.D., and Titball R.W. Synergistic protection of mice against plague with monoclonal antibodies specific for the F1 and V antigens of Yersinia pestis. Infect Immun 71 (2003) 2234-2238
    • (2003) Infect Immun , vol.71 , pp. 2234-2238
    • Hill, J.1    Copse, C.2    Leary, S.3    Stagg, A.J.4    Williamson, E.D.5    Titball, R.W.6
  • 4
    • 33645788354 scopus 로고    scopus 로고
    • Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague
    • Sebbane F., Jarrett C.O., Gardner D., Long D., and Hinnebusch B.J. Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague. Proc Natl Acad Sci 103 (2006) 5526-5530
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 5526-5530
    • Sebbane, F.1    Jarrett, C.O.2    Gardner, D.3    Long, D.4    Hinnebusch, B.J.5
  • 6
    • 0029134671 scopus 로고
    • Environmental modulation of gene expression and pathogenesis in Yersinia
    • Straley S.C., and Perry R.D. Environmental modulation of gene expression and pathogenesis in Yersinia. Trends Microbiol 3 (1995) 310-317
    • (1995) Trends Microbiol , vol.3 , pp. 310-317
    • Straley, S.C.1    Perry, R.D.2
  • 8
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells
    • Cornelis G.R., and Wolf-Watz H. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol 23 (1997) 861-867
    • (1997) Mol Microbiol , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 10
    • 0015611501 scopus 로고
    • Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane
    • Hantke K., and Braun V. Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane. Eur J Biochem 34 (1973) 284-296
    • (1973) Eur J Biochem , vol.34 , pp. 284-296
    • Hantke, K.1    Braun, V.2
  • 11
    • 0036091972 scopus 로고    scopus 로고
    • DOLOP - database of bacterial lipoproteins
    • Madan Babu M., and Sankaran K. DOLOP - database of bacterial lipoproteins. Bioinformatics 18 (2002) 641-643
    • (2002) Bioinformatics , vol.18 , pp. 641-643
    • Madan Babu, M.1    Sankaran, K.2
  • 12
    • 0034719341 scopus 로고    scopus 로고
    • The lipid component of lipoproteins from Borrelia burgdorferi: structural analysis, antigenicity, and presentation via human dendritic cells
    • Beermann C., Lochnit G., Geyer R., Groscurth P., and Filgueira L. The lipid component of lipoproteins from Borrelia burgdorferi: structural analysis, antigenicity, and presentation via human dendritic cells. Biochem Biophys Res Commun 267 (2000) 897-905
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 897-905
    • Beermann, C.1    Lochnit, G.2    Geyer, R.3    Groscurth, P.4    Filgueira, L.5
  • 13
    • 0025264283 scopus 로고
    • Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins
    • Brandt M.E., Riley B.S., Radolf J.D., and Norgard M.V. Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins. Infect Immun 58 (1990) 983-991
    • (1990) Infect Immun , vol.58 , pp. 983-991
    • Brandt, M.E.1    Riley, B.S.2    Radolf, J.D.3    Norgard, M.V.4
  • 14
    • 0033863073 scopus 로고    scopus 로고
    • Attachment of Borrelia burgdorferi within Ixodes scapularis mediated by outer surface protein A
    • Pal U., de Silva A.M., Montgomery R.R., Fish D., Anguita J., Anderson J.F., et al. Attachment of Borrelia burgdorferi within Ixodes scapularis mediated by outer surface protein A. J Clin Invest 106 (2000) 561-569
    • (2000) J Clin Invest , vol.106 , pp. 561-569
    • Pal, U.1    de Silva, A.M.2    Montgomery, R.R.3    Fish, D.4    Anguita, J.5    Anderson, J.F.6
  • 15
  • 16
    • 0033618630 scopus 로고    scopus 로고
    • Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2
    • Aliprantis A.O., Yang R.B., Mark M.R., Suggett S., Devaux B., Radolf J.D., et al. Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2. Science 285 (1999) 736-739
    • (1999) Science , vol.285 , pp. 736-739
    • Aliprantis, A.O.1    Yang, R.B.2    Mark, M.R.3    Suggett, S.4    Devaux, B.5    Radolf, J.D.6
  • 17
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., Uematsu S., and Takeuchi O. Pathogen recognition and innate immunity. Cell 124 (2006) 783-801
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 18
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden M.S., and Ghosh S. Signaling to NF-kappaB. Genes Dev 18 (2004) 2195-2224
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 19
    • 0033996762 scopus 로고    scopus 로고
    • The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling
    • Karin M., and Delhase M. The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling. Semin Immunol 12 (2000) 85-98
    • (2000) Semin Immunol , vol.12 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 20
    • 34848831208 scopus 로고    scopus 로고
    • YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction
    • Sweet C.R., Conlon J., Golenbock D.T., Goguen J., and Silverman N. YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction. Cell Microbiol 9 (2007) 2700-2715
    • (2007) Cell Microbiol , vol.9 , pp. 2700-2715
    • Sweet, C.R.1    Conlon, J.2    Golenbock, D.T.3    Goguen, J.4    Silverman, N.5
  • 21
    • 0036546501 scopus 로고    scopus 로고
    • NF-kappaB in cancer: from innocent bystander to major culprit
    • Karin M., Cao Y., Greten F.R., and Li Z.W. NF-kappaB in cancer: from innocent bystander to major culprit. Nat Rev Cancer 2 (2002) 301-310
    • (2002) Nat Rev Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.W.4
  • 22
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin M., and Lin A. NF-kappaB at the crossroads of life and death. Nat Immunol 3 (2002) 221-227
    • (2002) Nat Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 23
    • 4844226351 scopus 로고    scopus 로고
    • Chlamydia and apoptosis: life and death decisions of an intracellular pathogen
    • Byrne G.I., and Ojcius D.M. Chlamydia and apoptosis: life and death decisions of an intracellular pathogen. Nat Rev Microbiol 2 (2004) 802-808
    • (2004) Nat Rev Microbiol , vol.2 , pp. 802-808
    • Byrne, G.I.1    Ojcius, D.M.2
  • 24
    • 0037229178 scopus 로고    scopus 로고
    • Endogenous human papillomavirus E6 and E7 proteins differentially regulate proliferation, senescence, and apoptosis in HeLa cervical carcinoma cells
    • DeFilippis R.A., Goodwin E.C., Wu L., and DiMaio D. Endogenous human papillomavirus E6 and E7 proteins differentially regulate proliferation, senescence, and apoptosis in HeLa cervical carcinoma cells. J Virol 77 (2003) 1551-1563
    • (2003) J Virol , vol.77 , pp. 1551-1563
    • DeFilippis, R.A.1    Goodwin, E.C.2    Wu, L.3    DiMaio, D.4
  • 25
    • 0033857980 scopus 로고    scopus 로고
    • Pathogen-induced apoptosis of macrophages: a common end for different pathogenic strategies
    • Navarre W.W., and Zychlinsky A. Pathogen-induced apoptosis of macrophages: a common end for different pathogenic strategies. Cell Microbiol 2 (2000) 265-273
    • (2000) Cell Microbiol , vol.2 , pp. 265-273
    • Navarre, W.W.1    Zychlinsky, A.2
  • 26
    • 0030780833 scopus 로고    scopus 로고
    • Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis
    • Ruckdeschel K., Roggenkamp A., Lafont V., Mangeat P., Heesemann J., and Rouot B. Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis. Infect Immun 65 (1997) 4813-4821
    • (1997) Infect Immun , vol.65 , pp. 4813-4821
    • Ruckdeschel, K.1    Roggenkamp, A.2    Lafont, V.3    Mangeat, P.4    Heesemann, J.5    Rouot, B.6
  • 27
    • 0030985415 scopus 로고    scopus 로고
    • Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death
    • Monack D.M., Mecsas J., Ghori N., and Falkow S. Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death. Proc Natl Acad Sci U S A 94 (1997) 10385-10390
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10385-10390
    • Monack, D.M.1    Mecsas, J.2    Ghori, N.3    Falkow, S.4
  • 28
    • 0030730859 scopus 로고    scopus 로고
    • Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms and involving YopP, presumably acting as an effector protein
    • Mills S.D., Boland A., Sory M.P., van der Smissen P., Kerbourch C., Finlay B.B., et al. Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms and involving YopP, presumably acting as an effector protein. Proc Natl Acad Sci U S A 94 (1997) 12638-12643
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12638-12643
    • Mills, S.D.1    Boland, A.2    Sory, M.P.3    van der Smissen, P.4    Kerbourch, C.5    Finlay, B.B.6
  • 29
    • 33748045153 scopus 로고    scopus 로고
    • Yersinia pestis YopJ suppresses tumor necrosis factor alpha induction and contributes to apoptosis of immune cells in the lymph node but is not required for virulence in a rat model of bubonic plague
    • Lemaitre N., Sebbane F., Long D., and Hinnebusch B.J. Yersinia pestis YopJ suppresses tumor necrosis factor alpha induction and contributes to apoptosis of immune cells in the lymph node but is not required for virulence in a rat model of bubonic plague. Infect Immun 74 (2006) 5126-5131
    • (2006) Infect Immun , vol.74 , pp. 5126-5131
    • Lemaitre, N.1    Sebbane, F.2    Long, D.3    Hinnebusch, B.J.4
  • 30
    • 42149163014 scopus 로고    scopus 로고
    • Braun lipoprotein (Lpp) contributes to the virulence of yersiniae: potential role of Lpp in inducing bubonic and pneumonic plague
    • Sha J., Agar S.L., Baze W.B., Olano J.P., Fadl A.A., Erova T.E., et al. Braun lipoprotein (Lpp) contributes to the virulence of yersiniae: potential role of Lpp in inducing bubonic and pneumonic plague. Infect Immun 76 (2008) 1390-1409
    • (2008) Infect Immun , vol.76 , pp. 1390-1409
    • Sha, J.1    Agar, S.L.2    Baze, W.B.3    Olano, J.P.4    Fadl, A.A.5    Erova, T.E.6
  • 31
    • 51149099737 scopus 로고    scopus 로고
    • Characterization of a mouse model of plague after aerosolization of Yersinia pestis CO92
    • Agar S.L., Sha J., Foltz S.M., Erova T.E., Walberg K.G., Parham T.E., et al. Characterization of a mouse model of plague after aerosolization of Yersinia pestis CO92. Microbiology 154 (2008) 1939-1948
    • (2008) Microbiology , vol.154 , pp. 1939-1948
    • Agar, S.L.1    Sha, J.2    Foltz, S.M.3    Erova, T.E.4    Walberg, K.G.5    Parham, T.E.6
  • 33
    • 0027054511 scopus 로고
    • In vivo neutralization of tumor necrosis factor-alpha and interferon-gamma abrogates resistance to Yersinia enterocolitica infection in mice
    • Autenrieth I.B., and Heesemann J. In vivo neutralization of tumor necrosis factor-alpha and interferon-gamma abrogates resistance to Yersinia enterocolitica infection in mice. Med Microbiol Immunol 181 (1992) 333-338
    • (1992) Med Microbiol Immunol , vol.181 , pp. 333-338
    • Autenrieth, I.B.1    Heesemann, J.2
  • 34
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins: new discoveries and insights
    • Baldwin Jr. A.S. The NF-kappa B and I kappa B proteins: new discoveries and insights. Annu Rev Immunol 14 (1996) 649-683
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 35
    • 20444413447 scopus 로고    scopus 로고
    • Inhibition of MAPK and NF-kappa B pathways is necessary for rapid apoptosis in macrophages infected with Yersinia
    • Zhang Y., Ting A.T., Marcu K.B., and Bliska J.B. Inhibition of MAPK and NF-kappa B pathways is necessary for rapid apoptosis in macrophages infected with Yersinia. J Immunol 174 (2005) 7939-7949
    • (2005) J Immunol , vol.174 , pp. 7939-7949
    • Zhang, Y.1    Ting, A.T.2    Marcu, K.B.3    Bliska, J.B.4
  • 38
    • 33845586870 scopus 로고    scopus 로고
    • Kinetics of the immune response to the (F1 + V) vaccine in models of bubonic and pneumonic plague
    • Williamson E.D., Stagg A.J., Eley S.M., Taylor R., Green M., Jones S.M., et al. Kinetics of the immune response to the (F1 + V) vaccine in models of bubonic and pneumonic plague. Vaccine 25 (2007) 1142-1148
    • (2007) Vaccine , vol.25 , pp. 1142-1148
    • Williamson, E.D.1    Stagg, A.J.2    Eley, S.M.3    Taylor, R.4    Green, M.5    Jones, S.M.6
  • 39
    • 33746612813 scopus 로고    scopus 로고
    • Immunogenicity and protective immunity against bubonic plague and pneumonic plague by immunization of mice with the recombinant V10 antigen, a variant of LcrV
    • DeBord K.L., Anderson D.M., Marketon M.M., Overheim K.A., DePaolo R.W., Ciletti N.A., et al. Immunogenicity and protective immunity against bubonic plague and pneumonic plague by immunization of mice with the recombinant V10 antigen, a variant of LcrV. Infect Immun 74 (2006) 4910-4914
    • (2006) Infect Immun , vol.74 , pp. 4910-4914
    • DeBord, K.L.1    Anderson, D.M.2    Marketon, M.M.3    Overheim, K.A.4    DePaolo, R.W.5    Ciletti, N.A.6
  • 40
    • 33846209218 scopus 로고    scopus 로고
    • Oral vaccination with salmonella simultaneously expressing Yersinia pestis F1 and V antigens protects against bubonic and pneumonic plague
    • Yang X., Hinnebusch B.J., Trunkle T., Bosio C.M., Suo Z., Tighe M., et al. Oral vaccination with salmonella simultaneously expressing Yersinia pestis F1 and V antigens protects against bubonic and pneumonic plague. J Immunol 178 (2007) 1059-1067
    • (2007) J Immunol , vol.178 , pp. 1059-1067
    • Yang, X.1    Hinnebusch, B.J.2    Trunkle, T.3    Bosio, C.M.4    Suo, Z.5    Tighe, M.6
  • 41
    • 1842484204 scopus 로고    scopus 로고
    • Flea-borne transmission model to evaluate vaccine efficacy against naturally acquired bubonic plague
    • Jarrett C.O., Sebbane F., Adamovicz J.J., Andrews G.P., and Hinnebusch B.J. Flea-borne transmission model to evaluate vaccine efficacy against naturally acquired bubonic plague. Infect Immun 72 (2004) 2052-2056
    • (2004) Infect Immun , vol.72 , pp. 2052-2056
    • Jarrett, C.O.1    Sebbane, F.2    Adamovicz, J.J.3    Andrews, G.P.4    Hinnebusch, B.J.5
  • 42
    • 33846786590 scopus 로고    scopus 로고
    • Vaccination with live Yersinia pestis primes CD4 and CD8 T cells that synergistically protect against lethal pulmonary Y. pestis infection
    • Philipovskiy A.V., and Smiley S.T. Vaccination with live Yersinia pestis primes CD4 and CD8 T cells that synergistically protect against lethal pulmonary Y. pestis infection. Infect Immun 75 (2007) 878-885
    • (2007) Infect Immun , vol.75 , pp. 878-885
    • Philipovskiy, A.V.1    Smiley, S.T.2
  • 43
    • 35148895218 scopus 로고    scopus 로고
    • A Yersinia pestis lpxM-mutant live vaccine induces enhanced immunity against bubonic plague in mice and guinea pigs
    • Feodorova V.A., Pan'kina L.N., Savostina E.P., Sayapina L.V., Motin V.L., Dentovskaya S.V., et al. A Yersinia pestis lpxM-mutant live vaccine induces enhanced immunity against bubonic plague in mice and guinea pigs. Vaccine 25 (2007) 7620-7628
    • (2007) Vaccine , vol.25 , pp. 7620-7628
    • Feodorova, V.A.1    Pan'kina, L.N.2    Savostina, E.P.3    Sayapina, L.V.4    Motin, V.L.5    Dentovskaya, S.V.6
  • 45
    • 0031573217 scopus 로고    scopus 로고
    • Bacterial lipoprotein and lipopolysaccharide act synergistically to induce lethal shock and proinflammatory cytokine production
    • Zhang H., Peterson J.W., Niesel D.W., and Klimpel G.R. Bacterial lipoprotein and lipopolysaccharide act synergistically to induce lethal shock and proinflammatory cytokine production. J Immunol 159 (1997) 4868-4878
    • (1997) J Immunol , vol.159 , pp. 4868-4878
    • Zhang, H.1    Peterson, J.W.2    Niesel, D.W.3    Klimpel, G.R.4
  • 47
    • 56949084010 scopus 로고    scopus 로고
    • An IL-12 DNA vaccine co-expressing Yersinia pestis antigens protects against pneumonic plague
    • Yamanaka H., Hoyt T., Bowen R., Yang X., Crist K., Golden S., et al. An IL-12 DNA vaccine co-expressing Yersinia pestis antigens protects against pneumonic plague. Vaccine 27 (2009) 80-87
    • (2009) Vaccine , vol.27 , pp. 80-87
    • Yamanaka, H.1    Hoyt, T.2    Bowen, R.3    Yang, X.4    Crist, K.5    Golden, S.6
  • 48
    • 71049153268 scopus 로고    scopus 로고
    • Deletion of Braun lipoprotein gene (lpp) and curing of plasmid pPCP1 dramatically alter the virulence of Yersinia pestis CO92 in a mouse model of pneumonic plague
    • Agar S.L., Sha J., Baze W.B., Erova T.E., Foltz S.M., Suarez G., et al. Deletion of Braun lipoprotein gene (lpp) and curing of plasmid pPCP1 dramatically alter the virulence of Yersinia pestis CO92 in a mouse model of pneumonic plague. Microbiology 155 (2009) 3247-3259
    • (2009) Microbiology , vol.155 , pp. 3247-3259
    • Agar, S.L.1    Sha, J.2    Baze, W.B.3    Erova, T.E.4    Foltz, S.M.5    Suarez, G.6
  • 49
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62 (1998) 379-433
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 50
    • 0031744367 scopus 로고    scopus 로고
    • Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice
    • Monack D.M., Mecsas J., Bouley D., and Falkow S. Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice. J Exp Med 188 (1998) 2127-2137
    • (1998) J Exp Med , vol.188 , pp. 2127-2137
    • Monack, D.M.1    Mecsas, J.2    Bouley, D.3    Falkow, S.4
  • 51
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth K., Palmer L.E., Bao Z.Q., Stewart S., Rudolph A.E., Bliska J.B., et al. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science 285 (1999) 1920-1923
    • (1999) Science , vol.285 , pp. 1920-1923
    • Orth, K.1    Palmer, L.E.2    Bao, Z.Q.3    Stewart, S.4    Rudolph, A.E.5    Bliska, J.B.6
  • 52
    • 0037372795 scopus 로고    scopus 로고
    • Role of Toll-like receptor signaling in the apoptotic response of macrophages to Yersinia infection
    • Zhang Y., and Bliska J.B. Role of Toll-like receptor signaling in the apoptotic response of macrophages to Yersinia infection. Infect Immun 71 (2003) 1513-1519
    • (2003) Infect Immun , vol.71 , pp. 1513-1519
    • Zhang, Y.1    Bliska, J.B.2
  • 53
    • 0141923688 scopus 로고    scopus 로고
    • A dominant role of Toll-like receptor 4 in the signaling of apoptosis in bacteria-faced macrophages
    • Haase R., Kirschning C.J., Sing A., Schrottner P., Fukase K., Kusumoto S., et al. A dominant role of Toll-like receptor 4 in the signaling of apoptosis in bacteria-faced macrophages. J Immunol 171 (2003) 4294-4303
    • (2003) J Immunol , vol.171 , pp. 4294-4303
    • Haase, R.1    Kirschning, C.J.2    Sing, A.3    Schrottner, P.4    Fukase, K.5    Kusumoto, S.6
  • 54
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., et al. Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312 (2006) 1211-1214
    • (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
  • 55
    • 34248218099 scopus 로고    scopus 로고
    • The Yersinia effector protein YpkA induces apoptosis independently of actin depolymerization
    • Park H., Teja K., O'Shea J.J., and Siegel R.M. The Yersinia effector protein YpkA induces apoptosis independently of actin depolymerization. J Immunol 178 (2007) 6426-6434
    • (2007) J Immunol , vol.178 , pp. 6426-6434
    • Park, H.1    Teja, K.2    O'Shea, J.J.3    Siegel, R.M.4
  • 56
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R., Preston-Hurlburt P., and Janeway Jr. C.A. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388 (1997) 394-397
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 59
    • 25444505635 scopus 로고    scopus 로고
    • A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-kappa B through TLR1, TLR2, and TLR6
    • Shimizu T., Kida Y., and Kuwano K. A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-kappa B through TLR1, TLR2, and TLR6. J Immunol 175 (2005) 4641-4646
    • (2005) J Immunol , vol.175 , pp. 4641-4646
    • Shimizu, T.1    Kida, Y.2    Kuwano, K.3
  • 60
    • 0034292425 scopus 로고    scopus 로고
    • Activation of toll-like receptor 2 on human dendritic cells triggers induction of IL-12, but not IL-10
    • Thoma-Uszynski S., Kiertscher S.M., Ochoa M.T., Bouis D.A., Norgard M.V., Miyake K., et al. Activation of toll-like receptor 2 on human dendritic cells triggers induction of IL-12, but not IL-10. J Immunol 165 (2000) 3804-3810
    • (2000) J Immunol , vol.165 , pp. 3804-3810
    • Thoma-Uszynski, S.1    Kiertscher, S.M.2    Ochoa, M.T.3    Bouis, D.A.4    Norgard, M.V.5    Miyake, K.6
  • 62
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenicity revisited
    • Finlay B.B., and Falkow S. Common themes in microbial pathogenicity revisited. Microbiol Mol Biol Rev 61 (1997) 136-169
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 63
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi D.G., and Hultgren S.J. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr Opin Cell Biol 12 (2000) 420-430
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 65
    • 0034139491 scopus 로고    scopus 로고
    • Redirection of host vesicle trafficking pathways by intracellular parasites
    • Hackstadt T. Redirection of host vesicle trafficking pathways by intracellular parasites. Traffic 1 (2000) 93-99
    • (2000) Traffic , vol.1 , pp. 93-99
    • Hackstadt, T.1
  • 66
    • 33749341240 scopus 로고    scopus 로고
    • Current trends in plague research: from genomics to virulence
    • Huang X.Z., Nikolich M.P., and Lindler L.E. Current trends in plague research: from genomics to virulence. Clin Med Res 4 (2006) 189-199
    • (2006) Clin Med Res , vol.4 , pp. 189-199
    • Huang, X.Z.1    Nikolich, M.P.2    Lindler, L.E.3
  • 68
    • 12844250743 scopus 로고    scopus 로고
    • Murein lipoprotein is a critical outer membrane component involved in Salmonella enterica serovar Typhimurium systemic infection
    • Fadl A.A., Sha J., Klimpel G.R., Olano J.P., Niesel D.W., and Chopra A.K. Murein lipoprotein is a critical outer membrane component involved in Salmonella enterica serovar Typhimurium systemic infection. Infect Immun 73 (2005) 1081-1096
    • (2005) Infect Immun , vol.73 , pp. 1081-1096
    • Fadl, A.A.1    Sha, J.2    Klimpel, G.R.3    Olano, J.P.4    Niesel, D.W.5    Chopra, A.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.