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5 - Role of dendritic cells in the innate response to bacteria

from II - Dendritic cells and innate immune responses to bacteria

Published online by Cambridge University Press:  12 August 2009

Maria Rescigno
Affiliation:
European Institute of Oncology, Milan
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Summary

INTRODUCTION

Innate immunity is an ancient and highly conserved system that provides the first line of defense upon encounter with pathogenic organisms. Activation of innate immune responses is a complex process involving multiple components and distinct steps. The cellular components of innate immunity include neutrophils, monocytes, macrophages and dendritic cells (DCs). These cells are capable of direct microbicidal activity that partially depends on inducible nitric synthase (iNOS) and NADPH oxidase complex that catalyze production of toxic anti-microbial compounds. Additionally, they secrete a vast array of pro-inflammatory mediators such as cytokines and chemokines and can recruit and activate other inflammatory cells, thus amplifying the immune cascade. Apart from their role in restricting microbial growth, innate immune responses also provide the inflammatory context in which adaptive T- and B-cell immune responses develop.

Dendritic cells are derived from hematopoietic progenitor cells in the bone marrow and are found in the peripheral circulation as well as in the lymphoid and non-lymphoid tissues. Dendritic cells can be subdivided into several subsets based on the expression of the cell surface markers and different subsets have been ascribed distinct functions during the immune response. Since their discovery, dendritic cells have been studied extensively with regard to their role as antigen-presenting cells. However, it is becoming increasingly clear that dendritic cells also play an important role during the innate immune responses to microbial pathogens.

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Publisher: Cambridge University Press
Print publication year: 2007

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References

Taylor, P. R.et al. (2005). Macrophage receptors and immune recognition. Annu. Rev. Immunol. 23, 901–44CrossRefGoogle ScholarPubMed
Segal, A. W. (2005). How neutrophils kill microbes. Annu. Rev. Immunol. 23, 197–223CrossRefGoogle ScholarPubMed
Shortman, K. and Liu, Y. J. (2002). Mouse and human dendritic cell subtypes. Nat. Rev. Immunol. 2(3), 151–61CrossRefGoogle ScholarPubMed
Steinman, R. M. (1991). The dendritic cell system and its role in immunogenicity. Annu. Rev. Immunol. 9, 271–96CrossRefGoogle ScholarPubMed
Carbone, F. R., Belz, G. T., and Heath, W. R. (2004). Transfer of antigen between migrating and lymph node-resident dendritic cells in peripheral T-cell tolerance and immunity. Trends Immunol. 25(12), 655–8CrossRefGoogle ScholarPubMed
Rescigno, M.et al. (2001). Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria. Nat. Immunol. 2(4), 361–7CrossRefGoogle ScholarPubMed
Lambrecht, B. N., Prins, J. B., and Hoogsteden, H. C. (2001). Lung dendritic cells and host immunity to infection. Eur. Respir. J. 18(4), 692–704Google ScholarPubMed
Vazquez-Torres, A.et al. (1999). Extraintestinal dissemination of Salmonella by CD18-expressing phagocytes. Nature 401(6755), 804–8Google ScholarPubMed
Gonzalez-Juarrero, M. and Orme, I. M. (2001). Characterization of murine lung dendritic cells infected with Mycobacterium tuberculosis. Infect. Immun. 69(2), 1127–33CrossRefGoogle ScholarPubMed
Pedroza-Gonzalez, A.et al. (2004). In situanalysis of lung antigen-presenting cells during murine pulmonary infection with virulentMycobacterium tuberculosis. Int. J. Exp. Pathol. 85(3), 135–45Google ScholarPubMed
Iwasaki, A. and Medzhitov, R. (2004). Toll-like receptor control of the adaptive immune responses. Nat. Immunol. 5(10), 987–95CrossRefGoogle ScholarPubMed
Fritz, J. H.et al. (2005). Synergistic stimulation of human monocytes and dendritic cells by Toll-like receptor 4 and nucleotide-binding oligomerization domain1- and nucleotide-binding oligomerization domain2-activating agonists. Eur. J. Immunol. 35(8), 2459–70CrossRefGoogle Scholar
Gutierrez, O.et al. (2002). Induction of Nod2 in myelomonocytic and intestinal epithelial cells via nuclear factor-kappa B activation. J. Biol. Chem. 277(44), 41701–5CrossRefGoogle ScholarPubMed
Gellin, B. G. and Broome, C. V. (1989). Listeriosis. JAMA 261(9), 1313–20PubMed
Gaillard, J. L.et al. (1991). Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci. Cell 65(7), 1127–41CrossRefGoogle ScholarPubMed
Dramsi, S.et al. (1995). Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family. Mol. Microbiol. 16(2), 251–61CrossRefGoogle ScholarPubMed
Braun, L., Ghebrehiwet, B., and Cossart, P. (2000). gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein ofListeria monocytogenes. EMBO J. 19(7), 1458–66CrossRefGoogle Scholar
Shen, Y.et al. (2000). InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103(3), 501–10CrossRefGoogle ScholarPubMed
Marino, M.et al. (2002). GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands. EMBO J. 21(21), 5623–34CrossRefGoogle ScholarPubMed
Jonquieres, R., Pizarro-Cerda, J., and Cossart, P. (2001). Synergy between the N- and C-terminal domains of InlB for efficient invasion of non-phagocytic cells by Listeria monocytogenes. Mol. Microbiol. 42(4), 955–65CrossRefGoogle Scholar
Dunne, D. W.et al. (1994). The type I macrophage scavenger receptor binds to Gram-positive bacteria and recognizes lipoteichoic acid. Proc. Natl Acad. Sci. U S A 91(5), 1863–7CrossRefGoogle ScholarPubMed
Drevets, D. A. and Campbell, P. A. (1991). Roles of complement and complement receptor type 3 in phagocytosis of Listeria monocytogenes by inflammatory mouse peritoneal macrophages. Infect. Immun. 59(8), 2645–52Google ScholarPubMed
Bielecki, J.et al. (1990). Bacillus subtilis expressing a haemolysin gene from Listeria monocytogenes can grow in mammalian cells. Nature 345(6271), 175–6CrossRefGoogle ScholarPubMed
O'Riordan, M.et al. (2002). Innate recognition of bacteria by a macrophage cytosolic surveillance pathway. Proc. Natl Acad. Sci. U S A 99(21), 13861–6CrossRefGoogle ScholarPubMed
Serbina, N. V.et al. (2003). Sequential MyD88-independent and -dependent activation of innate immune responses to intracellular bacterial infection. Immunity 19(6), 891–901CrossRefGoogle ScholarPubMed
Berche, P., Gaillard, J. L., and Sansonetti, P. J. (1987). Intracellular growth of Listeria monocytogenes as a prerequisite for in vivo induction of T cell-mediated immunity. J. Immunol. 138(7), 2266–71Google ScholarPubMed
Domann, E.et al. (1992). A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J. 11(5), 1981–90Google ScholarPubMed
Kocks, C.et al. (1992). L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68(3), 521–31CrossRefGoogle ScholarPubMed
Goossens, P. L. and Milon, G. (1992). Induction of protective CD8+ T lymphocytes by an attenuated Listeria monocytogenes actA mutant. Int. Immunol. 4(12), 1413–18CrossRefGoogle ScholarPubMed
Harty, J. T. and Bevan, M. J. (1996). CD8 T-cell recognition of macrophages and hepatocytes results in immunity to Listeria monocytogenes. Infect. Immun. 64(9), 3632–40Google ScholarPubMed
Bancroft, G. J., Schreiber, R. D., and Unanue, E. R. (1991). Natural immunity: a T-cell-independent pathway of macrophage activation, defined in the scid mouse. Immunol. Rev. 124, 5–24CrossRefGoogle ScholarPubMed
Stevenson, M. M., Kongshavn, P. A., and Skamene, E. (1981). Genetic linkage of resistance to Listeria monocytogenes with macrophage inflammatory responses. J. Immunol. 127(2), 402–7Google ScholarPubMed
Cheers, C. and McKenzie, I. F. (1978). Resistance and susceptibility of mice to bacterial infection: genetics of listeriosis. Infect. Immun. 19(3), 755–62Google ScholarPubMed
Boyartchuk, V.et al. (2004). The host resistance locus sst1 controls innate immunity to Listeria monocytogenes infection in immunodeficient mice. J. Immunol. 173(8), 5112–20CrossRefGoogle ScholarPubMed
Gervais, F., Desforges, C., and Skamene, E. (1989). The C5-sufficient A/J congenic mouse strain. Inflammatory response and resistance to Listeria monocytogenes. J. Immunol. 142(6), 2057–60Google ScholarPubMed
Gervais, F., Stevenson, M., and Skamene, E. (1984). Genetic control of resistance to Listeria monocytogenes: regulation of leukocyte inflammatory responses by the Hc locus. J. Immunol. 132(4), 2078–83Google ScholarPubMed
Unanue, E. R. (1997). Studies in listeriosis show the strong symbiosis between the innate cellular system and the T-cell response. Immunol. Rev. 158, 11–25CrossRefGoogle ScholarPubMed
Nickol, A. D. and Bonventre, P. F. (1977). Anomalous high native resistance to athymic mice to bacterial pathogens. Infect. Immun. 18(3), 636–45Google ScholarPubMed
Buchmeier, N. A. and Schreiber, R. D. (1985). Requirement of endogenous interferon-gamma production for resolution of Listeria monocytogenes infection. Proc. Natl Acad. Sci. U S A 82(21), 7404–8CrossRefGoogle ScholarPubMed
Havell, E. A. (1989). Evidence that tumor necrosis factor has an important role in antibacterial resistance. J. Immunol. 143(9), 2894–9Google ScholarPubMed
Pfeffer, K.et al. (1993). Mice deficient for the 55 kd tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection. Cell 73(3), 457–67CrossRefGoogle ScholarPubMed
Rothe, J.et al. (1993). Mice lacking the tumour necrosis factor receptor 1 are resistant to Tnuclear factor-mediated toxicity but highly susceptible to infection by Listeria monocytogenes. Nature 364(6440), 798–802CrossRefGoogle Scholar
Harty, J. T. and Bevan, M. J. (1995). Specific immunity to Listeria monocytogenes in the absence of interferon gamma. Immunity 3(1), 109–17CrossRefGoogle Scholar
Andersson, A.et al. (1998). Early interferon-gamma production and innate immunity during Listeria monocytogenes infection in the absence of natural killer cells. J. Immunol. 161(10), 5600–6Google Scholar
Xanthoulea, S.et al. (2004). Tumor necrosis factor (Tnuclear factor) receptor shedding controls thresholds of innate immune activation that balance opposing Tnuclear factor functions in infectious and inflammatory diseases. J. Exp. Med. 200(3), 367–76CrossRefGoogle ScholarPubMed
Tripp, C. S.et al. (1994). Neutralization of interleukin-12 decreases resistance to Listeria in SCID and C.B-17 mice. Reversal by interferon-gamma. J. Immunol. 152(4), 1883–7Google Scholar
Neighbors, M.et al. (2001). A critical role for interleukin 18 in primary and memory effector responses to Listeria monocytogenes that extends beyond its effects on interferon gamma production. J. Exp. Med. 194(3), 343–54CrossRefGoogle ScholarPubMed
Carrero, J. A., Calderon, B., and Unanue, E. R. (2004). Type I interferon sensitizes lymphocytes to apoptosis and reduces resistance to listeria infection. J. Exp. Med. 200(4), 535–40CrossRefGoogle ScholarPubMed
O'Connell, R. M.et al. (2004). Type I interferon production enhances susceptibility to Listeria monocytogenes infection. J. Exp. Med. 200(4), 437–45CrossRefGoogle ScholarPubMed
Auerbuch, V.et al. (2004). Mice lacking the type I interferon receptor are resistant to Listeria monocytogenes. J. Exp. Med. 200(4), 527–33CrossRefGoogle ScholarPubMed
Beckerman, K. P.et al. (1993). Release of nitric oxide during the T cell-independent pathway of macrophage activation. Its role in resistance to Listeria monocytogenes. J. Immunol. 150(3), 888–95Google Scholar
Conlan, J. W. and North, R. J. (1994). Neutrophils are essential for early anti-Listeria defense in the liver, but not in the spleen or peritoneal cavity, as revealed by a granulocyte-depleting monoclonal antibody. J. Exp. Med. 179(1), 259–68CrossRefGoogle ScholarPubMed
Rogers, H. W. and Unanue, E. R. (1993). Neutrophils are involved in acute, nonspecific resistance to Listeria monocytogenes in mice. Infect. Immun. 61(12), 5090–6Google ScholarPubMed
Czuprynski, C. J.et al. (1994). Administration of anti-granulocyte mAb RB6-8C5 impairs the resistance of mice to Listeria monocytogenes infection. J. Immunol. 152(4), 1836–46Google ScholarPubMed
Rosen, H., Gordon, S., and North, R. J. (1989). Exacerbation of murine listeriosis by a monoclonal antibody specific for the type 3 complement receptor of myelomonocytic cells. Absence of monocytes at infective foci allows Listeria to multiply in nonphagocytic cells. J. Exp. Med. 170(1), 27–37CrossRefGoogle ScholarPubMed
Fang, F. C. (2004). Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nat. Rev. Microbiol. 2(10), 820–32CrossRefGoogle ScholarPubMed
Amer, A. O. and Swanson, M. S. (2002). A phagosome of one's own: a microbial guide to life in the macrophage. Curr. Opin. Microbiol. 5(1), 56–61CrossRefGoogle ScholarPubMed
Shiloh, M. U.et al. (1999). Phenotype of mice and macrophages deficient in both phagocyte oxidase and inducible nitric oxide synthase. Immunity 10(1), 29–38CrossRefGoogle ScholarPubMed
Serbina, N. V.et al. (2003). Tnuclear factor/inducible nitric oxide synthase-producing dendritic cells mediate innate immune defense against bacterial infection. Immunity 19(1), 59–70CrossRefGoogle Scholar
Endres, R.et al. (1997). Listeriosis in p47(phox−/−) and TRp55−/− mice: protection despite absence of ROI and susceptibility despite presence of RNI. Immunity 7(3), 419–32CrossRefGoogle ScholarPubMed
Dinauer, M. C., Deck, M. B., and Unanue, E. R. (1997). Mice lacking reduced nicotinamide adenine dinucleotide phosphate oxidase activity show increased susceptibility to early infection with Listeria monocytogenes. J. Immunol. 158(12), 5581–3Google ScholarPubMed
Kuziel, W. A.et al. (1997). Severe reduction in leukocyte adhesion and monocyte extravasation in mice deficient in CC chemokine receptor 2. Proc. Natl Acad. Sci. U S A 94(22), 12053–8CrossRefGoogle ScholarPubMed
Kurihara, T.et al. (1997). Defects in macrophage recruitment and host defense in mice lacking the CCR2 chemokine receptor. J. Exp. Med. 186(10), 1757–62CrossRefGoogle ScholarPubMed
Sato, N.et al. (2000). CC chemokine receptor (CCR)2 is required for Langerhans cell migration and localization of T helper cell type 1 (Th1)-inducing dendritic cells. Absence of CCR2 shifts the Leishmania major-resistant phenotype to a susceptible state dominated by Th2 cytokines, b cell outgrowth, and sustained neutrophilic inflammation. J. Exp. Med. 192(2), 205–18CrossRefGoogle ScholarPubMed
Izikson, L.et al. (2000). Resistance to experimental autoimmune encephalomyelitis in mice lacking the CC chemokine receptor (CCR)2. J. Exp. Med. 192(7), 1075–80CrossRefGoogle ScholarPubMed
Vecchi, A.et al. (1999). Differential responsiveness to constitutive vs. inducible chemokines of immature and mature mouse dendritic cells. J. Leukoc. Biol. 66(3), 489–94CrossRefGoogle ScholarPubMed
Mack, M.et al. (2001). Expression and characterization of the chemokine receptors CCR2 and CCR5 in mice. J. Immunol. 166(7), 4697–704CrossRefGoogle ScholarPubMed
Merad, M.et al. (2002). Langerhans cells renew in the skin throughout life under steady-state conditions. Nat. Immunol. 3(12), 1135–41CrossRefGoogle ScholarPubMed
Geissmann, F., Jung, S., and Littman, D. R. (2003). Blood monocytes consist of two principal subsets with distinct migratory properties. Immunity 19(1), 71–82CrossRefGoogle ScholarPubMed
Peters, W.et al. (2004). CCR2-dependent trafficking of F4/80dim macrophages and CD11cdim/intermediate dendritic cells is crucial for T cell recruitment to lungs infected with Mycobacterium tuberculosis. J. Immunol. 172(12), 7647–53CrossRefGoogle Scholar
Kurihara, T. and Bravo, R. (1996). Cloning and functional expression of mCCR2, a murine receptor for the C–C chemokines JE and FIC. J. Biol. Chem. 271(20), 11603–7CrossRefGoogle ScholarPubMed
Sozzani, S.et al. (1997). Receptor expression and responsiveness of human dendritic cells to a defined set of CC and CXC chemokines. J. Immunol. 159(4), 1993–2000Google ScholarPubMed
Sheffler, L. A.et al. (1995). Exogenous nitric oxide regulates interferon-gamma plus lipopolysaccharide-induced nitric oxide synthase expression in mouse macrophages. J. Immunol. 155(2), 886–94Google ScholarPubMed
Lu, L.et al. (1996). Induction of nitric oxide synthase in mouse dendritic cells by interferon-gamma, endotoxin, and interaction with allogeneic T cells: nitric oxide production is associated with dendritic cell apoptosis. J. Immunol. 157(8), 3577–86Google ScholarPubMed
Albina, J. E. and Henry, W. L. Jr. (1991). Suppression of lymphocyte proliferation through the nitric oxide synthesizing pathway. J. Surg. Res. 50(4), 403–9CrossRefGoogle ScholarPubMed
Eriksson, S., Chambers, B. J., and Rhen, M. (2003). Nitric oxide produced by murine dendritic cells is cytotoxic for intracellular Salmonella enterica sv. Typhimurium. Scand. J. Immunol. 58(5), 493–502CrossRefGoogle ScholarPubMed
Cheminay, C., Mohlenbrink, A., and Hensel, M. (2005). Intracellular Salmonella inhibit antigen presentation by dendritic cells. J. Immunol. 174(5), 2892–9CrossRefGoogle ScholarPubMed
Fremond, C. M.et al. (2004). Fatal Mycobacterium tuberculosis infection despite adaptive immune response in the absence of MyD88. J. Clin. Invest. 114(12), 1790–9CrossRefGoogle ScholarPubMed
Bodnar, K. A., Serbina, N. V., and Flynn, J. L. (2001). Fate of Mycobacterium tuberculosis within murine dendritic cells. Infect. Immun. 69(2), 800–9CrossRefGoogle ScholarPubMed
Buettner, M.et al. (2005). Inverse correlation of maturity and antibacterial activity in human dendritic cells. J. Immunol. 174(7), 4203–9CrossRefGoogle ScholarPubMed
Kolb-Maurer, A.et al. (2000). Listeria monocytogenes-infected human dendritic cells: uptake and host cell response. Infect. Immun. 68(6), 3680–8CrossRefGoogle ScholarPubMed
Paschen, A.et al. (2000). Human dendritic cells infected by Listeria monocytogenes: induction of maturation, requirements for phagolysosomal escape and antigen presentation capacity. Eur. J. Immunol. 30(12), 3447–563.0.CO;2-M>CrossRefGoogle ScholarPubMed
Guzman, C. A.et al. (1995). Interaction of Listeria monocytogenes with mouse dendritic cells. Infect. Immun. 63(9), 3665–73Google ScholarPubMed
Neild, A. L. and Roy, C. R. (2003). Legionella reveal dendritic cell functions that facilitate selection of antigens for major histocompatibility complex class II presentation. Immunity 18(6), 813–23CrossRefGoogle Scholar
Macpherson, A. J. and Uhr, T. (2004). Induction of protective IgA by intestinal dendritic cells carrying commensal bacteria. Science 303(5664), 1662–5CrossRefGoogle ScholarPubMed
Hopkins, S. A.et al. (2000). A recombinant Salmonella typhimurium vaccine strain is taken up and survives within murine Peyer's patch dendritic cells. Cell Microbiol. 2(1), 59–68CrossRefGoogle ScholarPubMed
Brzoza, K. L., Rockel, A. B., and Hiltbold, E. M. (2004). Cytoplasmic entry of Listeria monocytogenes enhances dendritic cell maturation and T cell differentiation and function. J. Immunol. 173(4), 2641–51CrossRefGoogle Scholar
Feng, H.et al. (2005). Listeria-infected myeloid dendritic cells produce interferon-beta, priming T cell activation. J. Immunol. 175(1), 421–32CrossRefGoogle ScholarPubMed
Kolb-Maurer, A.et al. (2003). Production of interleukin-12 and interleukin-18 in human dendritic cells upon infection by Listeria monocytogenes. FEMS Immunol. Med. Microbiol. 35(3), 255–62CrossRefGoogle ScholarPubMed
Takeda, K. and Akira, S. (2004). Toll-like receptor signaling pathways. Semin. Immunol. 16(1), 3–9CrossRefGoogle Scholar
Seki, E.et al. (2002). Critical roles of myeloid differentiation factor 88-dependent proinflammatory cytokine release in early phase clearance of Listeria monocytogenes in mice. J. Immunol. 169(7), 3863–8CrossRefGoogle ScholarPubMed
Edelson, B. T. and Unanue, E. R. (2002). MyD88-dependent but Toll-like receptor 2-independent innate immunity to Listeria: no role for either in macrophage listericidal activity. J. Immunol. 169(7), 3869–75CrossRefGoogle ScholarPubMed
Adachi, O.et al. (1998). Targeted disruption of the MyD88 gene results in loss of interleukin-1- and interleukin-18-mediated function. Immunity 9(1), 143–50CrossRefGoogle Scholar
Tsuji, N. M.et al. (2004). Roles of caspase-1 in Listeria infection in mice. Int. Immunol. 16(2), 335–43CrossRefGoogle ScholarPubMed
Hayashi, F.et al. (2001). The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 410(6832), 1099–103CrossRefGoogle ScholarPubMed
Ito, S.et al. (2005). CpG oligodeoxynucleotides enhance neonatal resistance to Listeria infection. J. Immunol. 174(2), 777–82CrossRefGoogle ScholarPubMed
Inohara, N.et al. (2003). Host recognition of bacterial muramyl dipeptide mediated through nucleotide-binding oligomerization domain2. Implications for Crohn's disease. J. Biol. Chem. 278(8), 5509–12CrossRefGoogle Scholar
Girardin, S. E.et al. (2003). Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (muramyl dipeptide) detection. J. Biol. Chem. 278(11), 8869–72CrossRefGoogle ScholarPubMed
Li, J.et al. (2004). Regulation of interleukin-8 and interleukin-1beta expression in Crohn's disease associated nucleotide-binding oligomerization domain2/CARD15 mutations. Hum. Mol. Genet. 13(16), 1715–25CrossRefGoogle Scholar
Girardin, S. E.et al. (2003). Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 300(5625), 1584–7CrossRefGoogle ScholarPubMed
Kobayashi, K. S.et al. (2005). Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307(5710), 731–4CrossRefGoogle ScholarPubMed
Chin, A. I.et al. (2002). Involvement of receptor-interacting protein 2 in innate and adaptive immune responses. Nature 416(6877), 190–4CrossRefGoogle ScholarPubMed
Kobayashi, K.et al. (2002). Rip-like interacting caspase-like apoptosis-regulatory protein kinase/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature 416(6877), 194–9CrossRefGoogle Scholar
Hauf, N.et al. (1997). Listeria monocytogenes infection of P388D1 macrophages results in a biphasic nuclear factor-kappaB (RelA/p50) activation induced by lipoteichoic acid and bacterial phospholipases and mediated by IkappaBalpha and IkappaBbeta degradation. Proc. Natl Acad. Sci. U S A 94(17), 9394–9CrossRefGoogle Scholar
O'Connell, R. M.et al. (2005). Immune activation of type I interferons by Listeria monocytogenes occurs independently of Toll-like receptor4, Toll-like receptor2, and receptor interacting protein 2 but involves Tnuclear factorR-associated nuclear factor kappa B kinase-binding kinase 1. J. Immunol. 174(3), 1602–7CrossRefGoogle Scholar
Pron, B.et al. (2001). Dendritic cells are early cellular targets of Listeria monocytogenes after intestinal delivery and are involved in bacterial spread in the host. Cell Microbiol. 3(5), 331–40CrossRefGoogle Scholar
Vollstedt, S.et al. (2003). Flt3 ligand-treated neonatal mice have increased innate immunity against intracellular pathogens and efficiently control virus infections. J. Exp. Med. 197(5), 575–84CrossRefGoogle ScholarPubMed
Jung, S.et al. (2002). In vivo depletion of CD11c(+) dendritic cells abrogates priming of CD8(+) T cells by exogenous cell-associated antigens. Immunity 17(2), 211–20CrossRefGoogle ScholarPubMed
Kolb-Maurer, A.et al. (2003). Induction of interleukin-12 and interleukin-18 in human dendritic cells upon infection byListeria monocytogenes. FEMS Immunol. Med. Microbiol. 35(3), 255–62CrossRefGoogle Scholar
Alanir, R. C.et al. (2004). Increased dendritic cell numbers impair protective immunity to intracellular bacteria despite augmenting antigen-specific CD8+ T lymphocyte responses. J. Immunol. 172, 3725–35CrossRefGoogle Scholar

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