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Volumn 130, Issue 1-2, 2010, Pages 36-42

The same well-characterized T cell epitope SIINFEKL expressed in the context of a cytoplasmic or secreted protein in BCG induces different CD8+ T cell responses

Author keywords

Antigen location; CD8+ T cell responses; Mycobacterium

Indexed keywords

BCG VACCINE; CYTOPLASM PROTEIN; EPITOPE; GREEN FLUORESCENT PROTEIN; OCTAPEPTIDE; OVALBUMIN; SECRETORY PROTEIN; SERYLISOLEUCYLISOLEUCYLASPARAGINYLPHENYLALANYLGLUTAMYLLYSYLLEUCINE; UNCLASSIFIED DRUG;

EID: 77950927083     PISSN: 01652478     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imlet.2009.12.004     Document Type: Article
Times cited : (9)

References (49)
  • 1
    • 22944433876 scopus 로고    scopus 로고
    • The success and failure of BCG-implications for a novel tuberculosis vaccine
    • Andersen P., Doherty T.M. The success and failure of BCG-implications for a novel tuberculosis vaccine. Nat Rev Microbiol 2005, 3:656-662.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 656-662
    • Andersen, P.1    Doherty, T.M.2
  • 2
    • 77950932459 scopus 로고    scopus 로고
    • 2009 WR. Global tuberculosis control; 2009.
    • 2009 WR. Global tuberculosis control; 2009.
    • (2009)
  • 3
    • 0032730743 scopus 로고    scopus 로고
    • Cytolytic T-cell responses to human dendritic cells and macrophages infected with Mycobacterium bovis BCG and recombinant BCG secreting listeriolysin
    • Conradt P., Hess J., Kaufmann S.H. Cytolytic T-cell responses to human dendritic cells and macrophages infected with Mycobacterium bovis BCG and recombinant BCG secreting listeriolysin. Microbes Infect 1999, 1:753-764.
    • (1999) Microbes Infect , vol.1 , pp. 753-764
    • Conradt, P.1    Hess, J.2    Kaufmann, S.H.3
  • 4
    • 22344433382 scopus 로고    scopus 로고
    • Increased vaccine efficacy against tuberculosis of recombinant Mycobacterium bovis bacille Calmette-Guerin mutants that secrete listeriolysin
    • Grode L., Seiler P., Baumann S., Hess J., Brinkmann V., Eddine A.N., et al. Increased vaccine efficacy against tuberculosis of recombinant Mycobacterium bovis bacille Calmette-Guerin mutants that secrete listeriolysin. J Clin Invest 2005, 115:2472-2479.
    • (2005) J Clin Invest , vol.115 , pp. 2472-2479
    • Grode, L.1    Seiler, P.2    Baumann, S.3    Hess, J.4    Brinkmann, V.5    Eddine, A.N.6
  • 5
    • 0036604427 scopus 로고    scopus 로고
    • Multiple mechanisms compensate to enhance tumor-protective CD8(+) T cell response in the long-term despite poor CD8(+) T cell priming initially: comparison between an acute versus a chronic intracellular bacterium expressing a model antigen
    • Dudani R., Chapdelaine Y., Faassen Hv H., Smith D.K., Shen H., Krishnan L., et al. Multiple mechanisms compensate to enhance tumor-protective CD8(+) T cell response in the long-term despite poor CD8(+) T cell priming initially: comparison between an acute versus a chronic intracellular bacterium expressing a model antigen. J Immunol 2002, 168:5737-5745.
    • (2002) J Immunol , vol.168 , pp. 5737-5745
    • Dudani, R.1    Chapdelaine, Y.2    Faassen Hv, H.3    Smith, D.K.4    Shen, H.5    Krishnan, L.6
  • 6
    • 67449113507 scopus 로고    scopus 로고
    • Antigen load governs the differential priming of CD8 T cells in response to the bacille Calmette Guerin vaccine or Mycobacterium tuberculosis infection
    • Ryan A.A., Nambiar J.K., Wozniak T.M., Roediger B., Shklovskaya E., Britton W.J., et al. Antigen load governs the differential priming of CD8 T cells in response to the bacille Calmette Guerin vaccine or Mycobacterium tuberculosis infection. J Immunol 2009, 182:7172-7177.
    • (2009) J Immunol , vol.182 , pp. 7172-7177
    • Ryan, A.A.1    Nambiar, J.K.2    Wozniak, T.M.3    Roediger, B.4    Shklovskaya, E.5    Britton, W.J.6
  • 7
    • 17444361941 scopus 로고    scopus 로고
    • Epitope-tagging vectors for the expression and detection of recombinant proteins in mycobacteria
    • Spratt J.M., Ryan A.A., Britton W.J., Triccas J.A. Epitope-tagging vectors for the expression and detection of recombinant proteins in mycobacteria. Plasmid 2005, 53:269-273.
    • (2005) Plasmid , vol.53 , pp. 269-273
    • Spratt, J.M.1    Ryan, A.A.2    Britton, W.J.3    Triccas, J.A.4
  • 8
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody
    • Porgador A., Yewdell J.W., Deng Y., Bennink J.R., Germain R.N. Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity 1997, 6:715-726.
    • (1997) Immunity , vol.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 10
    • 0034443580 scopus 로고    scopus 로고
    • Identification of mycobacterial surface proteins released into subcellular compartments of infected macrophages
    • Beatty W.L., Russell D.G. Identification of mycobacterial surface proteins released into subcellular compartments of infected macrophages. Infect Immun 2000, 68:6997-7002.
    • (2000) Infect Immun , vol.68 , pp. 6997-7002
    • Beatty, W.L.1    Russell, D.G.2
  • 11
    • 0035132517 scopus 로고    scopus 로고
    • Mycobacterial surface moieties are released from infected macrophages by a constitutive exocytic event
    • Beatty W.L., Ullrich H.J., Russell D.G. Mycobacterial surface moieties are released from infected macrophages by a constitutive exocytic event. Eur J Cell Biol 2001, 80:31-40.
    • (2001) Eur J Cell Biol , vol.80 , pp. 31-40
    • Beatty, W.L.1    Ullrich, H.J.2    Russell, D.G.3
  • 12
    • 0028909199 scopus 로고
    • Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited
    • Clemens D.L., Horwitz M.A. Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited. J Exp Med 1995, 181:257-270.
    • (1995) J Exp Med , vol.181 , pp. 257-270
    • Clemens, D.L.1    Horwitz, M.A.2
  • 13
    • 33745318852 scopus 로고    scopus 로고
    • Secreted proteins from Mycobacterium tuberculosis gain access to the cytosolic MHC class-I antigen-processing pathway
    • Lewinsohn D.M., Grotzke J.E., Heinzel A.S., Zhu L., Ovendale P.J., Johnson M., et al. Secreted proteins from Mycobacterium tuberculosis gain access to the cytosolic MHC class-I antigen-processing pathway. J Immunol 2006, 177:437-442.
    • (2006) J Immunol , vol.177 , pp. 437-442
    • Lewinsohn, D.M.1    Grotzke, J.E.2    Heinzel, A.S.3    Zhu, L.4    Ovendale, P.J.5    Johnson, M.6
  • 14
    • 51949107482 scopus 로고    scopus 로고
    • Bacterial protein secretion is required for priming of CD8+ T cells specific for the Mycobacterium tuberculosis antigen CFP10
    • Woodworth J.S., Fortune S.M., Behar S.M. Bacterial protein secretion is required for priming of CD8+ T cells specific for the Mycobacterium tuberculosis antigen CFP10. Infect Immun 2008, 76:4199-4205.
    • (2008) Infect Immun , vol.76 , pp. 4199-4205
    • Woodworth, J.S.1    Fortune, S.M.2    Behar, S.M.3
  • 15
    • 1542514780 scopus 로고    scopus 로고
    • Prolonged antigen presentation, APC-, and CD8+ T cell turnover during mycobacterial infection: comparison with Listeria monocytogenes
    • van Faassen H., Dudani R., Krishnan L., Sad S. Prolonged antigen presentation, APC-, and CD8+ T cell turnover during mycobacterial infection: comparison with Listeria monocytogenes. J Immunol 2004, 172:3491-3500.
    • (2004) J Immunol , vol.172 , pp. 3491-3500
    • van Faassen, H.1    Dudani, R.2    Krishnan, L.3    Sad, S.4
  • 16
    • 0029907963 scopus 로고    scopus 로고
    • Major histocompatibility class I presentation of soluble antigen facilitated by Mycobacterium tuberculosis infection
    • Mazzaccaro R.J., Gedde M., Jensen E.R., van Santen H.M., Ploegh H.L., Rock K.L., et al. Major histocompatibility class I presentation of soluble antigen facilitated by Mycobacterium tuberculosis infection. Proc Natl Acad Sci USA 1996, 93:11786-11791.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11786-11791
    • Mazzaccaro, R.J.1    Gedde, M.2    Jensen, E.R.3    van Santen, H.M.4    Ploegh, H.L.5    Rock, K.L.6
  • 17
    • 2942751932 scopus 로고    scopus 로고
    • Alternative processing for MHC class I presentation by immature and CpG-activated dendritic cells
    • Chen L., Jondal M. Alternative processing for MHC class I presentation by immature and CpG-activated dendritic cells. Eur J Immunol 2004, 34:952-960.
    • (2004) Eur J Immunol , vol.34 , pp. 952-960
    • Chen, L.1    Jondal, M.2
  • 18
    • 0029906635 scopus 로고    scopus 로고
    • Major histocompatibility complex class I presentation of ovalbumin peptide 257-264 from exogenous sources: protein context influences the degree of TAP-independent presentation
    • Wick M.J., Pfeifer J.D. Major histocompatibility complex class I presentation of ovalbumin peptide 257-264 from exogenous sources: protein context influences the degree of TAP-independent presentation. Eur J Immunol 1996, 26:2790-2799.
    • (1996) Eur J Immunol , vol.26 , pp. 2790-2799
    • Wick, M.J.1    Pfeifer, J.D.2
  • 19
    • 4143146210 scopus 로고    scopus 로고
    • Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo
    • Shen L., Sigal L.J., Boes M., Rock K.L. Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo. Immunity 2004, 21:155-165.
    • (2004) Immunity , vol.21 , pp. 155-165
    • Shen, L.1    Sigal, L.J.2    Boes, M.3    Rock, K.L.4
  • 20
    • 0028910938 scopus 로고
    • A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules
    • Kovacsovics-Bankowski M., Rock K.L. A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules. Science 1995, 267:243-246.
    • (1995) Science , vol.267 , pp. 243-246
    • Kovacsovics-Bankowski, M.1    Rock, K.L.2
  • 21
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman A.L., Giodini A., Cresswell P. A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 2006, 25:607-617.
    • (2006) Immunity , vol.25 , pp. 607-617
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3
  • 22
    • 0242331619 scopus 로고    scopus 로고
    • Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens
    • Ackerman A.L., Kyritsis C., Tampe R., Cresswell P. Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens. Proc Natl Acad Sci USA 2003, 100:12889-12894.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12889-12894
    • Ackerman, A.L.1    Kyritsis, C.2    Tampe, R.3    Cresswell, P.4
  • 23
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • Guermonprez P., Saveanu L., Kleijmeer M., Davoust J., Van Endert P., Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 2003, 425:397-402.
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 24
    • 18344405138 scopus 로고    scopus 로고
    • Phagosomes are competent organelles for antigen cross-presentation
    • Houde M., Bertholet S., Gagnon E., Brunet S., Goyette G., Laplante A., et al. Phagosomes are competent organelles for antigen cross-presentation. Nature 2003, 425:402-406.
    • (2003) Nature , vol.425 , pp. 402-406
    • Houde, M.1    Bertholet, S.2    Gagnon, E.3    Brunet, S.4    Goyette, G.5    Laplante, A.6
  • 25
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann J.O., Albring J., Huter E., Bulbuc N., Spee P., Neefjes J., et al. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity 2000, 13:117-127.
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1    Albring, J.2    Huter, E.3    Bulbuc, N.4    Spee, P.5    Neefjes, J.6
  • 26
    • 33644956892 scopus 로고    scopus 로고
    • Identification of naturally processed peptides bound to the class I MHC molecule H-2Kd of normal and TAP-deficient cells
    • Suri A., Walters J.J., Levisetti M.G., Gross M.L., Unanue E.R. Identification of naturally processed peptides bound to the class I MHC molecule H-2Kd of normal and TAP-deficient cells. Eur J Immunol 2006, 36:544-557.
    • (2006) Eur J Immunol , vol.36 , pp. 544-557
    • Suri, A.1    Walters, J.J.2    Levisetti, M.G.3    Gross, M.L.4    Unanue, E.R.5
  • 27
    • 35348926889 scopus 로고    scopus 로고
    • Traffic of proteins and peptides across membranes for immunosurveillance by CD8(+) T lymphocytes: a topological challenge
    • Johnstone C., Del Val M. Traffic of proteins and peptides across membranes for immunosurveillance by CD8(+) T lymphocytes: a topological challenge. Traffic 2007, 8:1486-1494.
    • (2007) Traffic , vol.8 , pp. 1486-1494
    • Johnstone, C.1    Del Val, M.2
  • 29
    • 52449099804 scopus 로고    scopus 로고
    • MHC class I endosomal and lysosomal trafficking coincides with exogenous antigen loading in dendritic cells
    • Basha G., Lizee G., Reinicke A.T., Seipp R.P., Omilusik K.D., Jefferies W.A. MHC class I endosomal and lysosomal trafficking coincides with exogenous antigen loading in dendritic cells. PLoS One 2008, 3:e3247.
    • (2008) PLoS One , vol.3
    • Basha, G.1    Lizee, G.2    Reinicke, A.T.3    Seipp, R.P.4    Omilusik, K.D.5    Jefferies, W.A.6
  • 31
    • 0027511213 scopus 로고
    • Phagocytic processing of bacterial antigens for class I MHC presentation to T cells
    • Pfeifer J.D., Wick M.J., Roberts R.L., Findlay K., Normark S.J., Harding C.V. Phagocytic processing of bacterial antigens for class I MHC presentation to T cells. Nature 1993, 361:359-362.
    • (1993) Nature , vol.361 , pp. 359-362
    • Pfeifer, J.D.1    Wick, M.J.2    Roberts, R.L.3    Findlay, K.4    Normark, S.J.5    Harding, C.V.6
  • 32
    • 0033049945 scopus 로고    scopus 로고
    • Peptide-receptive class I major histocompatibility complex molecules on TAP-deficient and wild-type cells and their roles in the processing of exogenous antigens
    • Song R., Porgador A., Harding C.V. Peptide-receptive class I major histocompatibility complex molecules on TAP-deficient and wild-type cells and their roles in the processing of exogenous antigens. Immunology 1999, 97:316-324.
    • (1999) Immunology , vol.97 , pp. 316-324
    • Song, R.1    Porgador, A.2    Harding, C.V.3
  • 33
    • 0029993103 scopus 로고    scopus 로고
    • Roles of proteasomes, transporter for antigen presentation (TAP), and beta 2-microglobulin in the processing of bacterial or particulate antigens via an alternate class I MHC processing pathway
    • Song R., Harding C.V. Roles of proteasomes, transporter for antigen presentation (TAP), and beta 2-microglobulin in the processing of bacterial or particulate antigens via an alternate class I MHC processing pathway. J Immunol 1996, 156:4182-4190.
    • (1996) J Immunol , vol.156 , pp. 4182-4190
    • Song, R.1    Harding, C.V.2
  • 34
    • 0033976065 scopus 로고    scopus 로고
    • Bacterial proteins can be processed by macrophages in a transporter associated with antigen processing-independent, cysteine protease-dependent manner for presentation by MHC class I molecules
    • Campbell D.J., Serwold T., Shastri N. Bacterial proteins can be processed by macrophages in a transporter associated with antigen processing-independent, cysteine protease-dependent manner for presentation by MHC class I molecules. J Immunol 2000, 164:168-175.
    • (2000) J Immunol , vol.164 , pp. 168-175
    • Campbell, D.J.1    Serwold, T.2    Shastri, N.3
  • 36
    • 65449171187 scopus 로고    scopus 로고
    • Autophagy and its role in MHC-mediated antigen presentation
    • Crotzer V.L., Blum J.S. Autophagy and its role in MHC-mediated antigen presentation. J Immunol 2009, 182:3335-3341.
    • (2009) J Immunol , vol.182 , pp. 3335-3341
    • Crotzer, V.L.1    Blum, J.S.2
  • 37
    • 33846224369 scopus 로고    scopus 로고
    • Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes
    • Schmid D., Pypaert M., Munz C. Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes. Immunity 2007, 26:79-92.
    • (2007) Immunity , vol.26 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Munz, C.3
  • 38
    • 0032574807 scopus 로고    scopus 로고
    • Mycobacterium bovis Bacille Calmette-Guerin strains secreting listeriolysin of Listeria monocytogenes
    • Hess J., Miko D., Catic A., Lehmensiek V., Russell D.G., Kaufmann S.H. Mycobacterium bovis Bacille Calmette-Guerin strains secreting listeriolysin of Listeria monocytogenes. Proc Natl Acad Sci USA 1998, 95:5299-5304.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5299-5304
    • Hess, J.1    Miko, D.2    Catic, A.3    Lehmensiek, V.4    Russell, D.G.5    Kaufmann, S.H.6
  • 39
    • 0037067649 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
    • Gagnon E., Duclos S., Rondeau C., Chevet E., Cameron P.H., Steele-Mortimer O., et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell 2002, 110:119-131.
    • (2002) Cell , vol.110 , pp. 119-131
    • Gagnon, E.1    Duclos, S.2    Rondeau, C.3    Chevet, E.4    Cameron, P.H.5    Steele-Mortimer, O.6
  • 40
    • 26244461724 scopus 로고    scopus 로고
    • Quantitative and dynamic assessment of the contribution of the ER to phagosome formation
    • Touret N., Paroutis P., Terebiznik M., Harrison R.E., Trombetta S., Pypaert M., et al. Quantitative and dynamic assessment of the contribution of the ER to phagosome formation. Cell 2005, 123:157-170.
    • (2005) Cell , vol.123 , pp. 157-170
    • Touret, N.1    Paroutis, P.2    Terebiznik, M.3    Harrison, R.E.4    Trombetta, S.5    Pypaert, M.6
  • 42
    • 52049102433 scopus 로고    scopus 로고
    • Efficient cross-presentation depends on autophagy in tumor cells
    • Li Y., Wang L.X., Yang G., Hao F., Urba W.J., Hu H.M. Efficient cross-presentation depends on autophagy in tumor cells. Cancer Res 2008, 68:6889-6895.
    • (2008) Cancer Res , vol.68 , pp. 6889-6895
    • Li, Y.1    Wang, L.X.2    Yang, G.3    Hao, F.4    Urba, W.J.5    Hu, H.M.6
  • 43
    • 19344373577 scopus 로고    scopus 로고
    • Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens
    • Zhou D., Li P., Lin Y., Lott J.M., Hislop A.D., Canaday D.H., et al. Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity 2005, 22:571-581.
    • (2005) Immunity , vol.22 , pp. 571-581
    • Zhou, D.1    Li, P.2    Lin, Y.3    Lott, J.M.4    Hislop, A.D.5    Canaday, D.H.6
  • 44
    • 21244454544 scopus 로고    scopus 로고
    • Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
    • Wolters J.C., Abele R., Tampe R. Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9). J Biol Chem 2005, 280:23631-23636.
    • (2005) J Biol Chem , vol.280 , pp. 23631-23636
    • Wolters, J.C.1    Abele, R.2    Tampe, R.3
  • 45
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo A.M., Dice J.F. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996, 273:501-503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 46
    • 1842407159 scopus 로고    scopus 로고
    • Two novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing
    • Snyder H.L., Bacik I., Bennink J.R., Kearns G., Behrens T.W., Bachi T., et al. Two novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing. J Exp Med 1997, 186:1087-1098.
    • (1997) J Exp Med , vol.186 , pp. 1087-1098
    • Snyder, H.L.1    Bacik, I.2    Bennink, J.R.3    Kearns, G.4    Behrens, T.W.5    Bachi, T.6
  • 47
    • 33644758147 scopus 로고    scopus 로고
    • Role of phagosomes and major histocompatibility complex class II (MHC-II) compartment in MHC-II antigen processing of Mycobacterium tuberculosis in human macrophages
    • Torres M., Ramachandra L., Rojas R.E., Bobadilla K., Thomas J., Canaday D.H., et al. Role of phagosomes and major histocompatibility complex class II (MHC-II) compartment in MHC-II antigen processing of Mycobacterium tuberculosis in human macrophages. Infect Immun 2006, 74:1621-1630.
    • (2006) Infect Immun , vol.74 , pp. 1621-1630
    • Torres, M.1    Ramachandra, L.2    Rojas, R.E.3    Bobadilla, K.4    Thomas, J.5    Canaday, D.H.6
  • 48
    • 0028052101 scopus 로고
    • Phagocytic processing of exogenous particulate antigens by macrophages for presentation by class I MHC molecules
    • Harding C.V., Song R. Phagocytic processing of exogenous particulate antigens by macrophages for presentation by class I MHC molecules. J Immunol 1994, 153:4925-4933.
    • (1994) J Immunol , vol.153 , pp. 4925-4933
    • Harding, C.V.1    Song, R.2
  • 49
    • 0033559901 scopus 로고    scopus 로고
    • Phagosomes are fully competent antigen-processing organelles that mediate the formation of peptide:class II MHC complexes
    • Ramachandra L., Song R., Harding C.V. Phagosomes are fully competent antigen-processing organelles that mediate the formation of peptide:class II MHC complexes. J Immunol 1999, 162:3263-3272.
    • (1999) J Immunol , vol.162 , pp. 3263-3272
    • Ramachandra, L.1    Song, R.2    Harding, C.V.3


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