메뉴 건너뛰기




Volumn 33, Issue 25, 2015, Pages 2887-2896

Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120

Author keywords

Antigen presentation; Antigen processing; Cellular immune response; Disulfide; Lymphocyte; Protein conformation; Protein denaturation; T helper

Indexed keywords

EPITOPE; GAMMA INTERFERON; GAMMA INTERFERON INDUCIBLE LYSOSOMAL THIOREDUCTASE; GLYCOPROTEIN GP 120; UNCLASSIFIED DRUG; DISULFIDE; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; IFI30 PROTEIN, MOUSE; OXIDOREDUCTASE;

EID: 84929515864     PISSN: 0264410X     EISSN: 18732518     Source Type: Journal    
DOI: 10.1016/j.vaccine.2015.04.082     Document Type: Article
Times cited : (12)

References (54)
  • 1
    • 84857751302 scopus 로고    scopus 로고
    • HIV-specific cytolytic CD4 T cell responses during acute HIV infection predict disease outcome
    • Soghoian D.Z., Jessen H., Flanders M., Sierra-Davidson K., Cutler S., Pertel T., et al. HIV-specific cytolytic CD4 T cell responses during acute HIV infection predict disease outcome. Sci Transl Med 2012, 4:123ra25.
    • (2012) Sci Transl Med , vol.4 , pp. 123-125
    • Soghoian, D.Z.1    Jessen, H.2    Flanders, M.3    Sierra-Davidson, K.4    Cutler, S.5    Pertel, T.6
  • 2
    • 84880286540 scopus 로고    scopus 로고
    • Association of HLA-DRB1-restricted CD4(+) T cell responses with HIV immune control
    • Ranasinghe S., Cutler S., Davis I., Lu R., Soghoian D.Z., Qi Y., et al. Association of HLA-DRB1-restricted CD4(+) T cell responses with HIV immune control. Nat Med 2013, 19:930-933.
    • (2013) Nat Med , vol.19 , pp. 930-933
    • Ranasinghe, S.1    Cutler, S.2    Davis, I.3    Lu, R.4    Soghoian, D.Z.5    Qi, Y.6
  • 3
    • 0035834732 scopus 로고    scopus 로고
    • Allocation of helper T-cell epitope immunodominance according to three-dimensional structure in the human immunodeficiency virus type I envelope glycoprotein gp120
    • Dai G., Steede N.K., Landry S.J. Allocation of helper T-cell epitope immunodominance according to three-dimensional structure in the human immunodeficiency virus type I envelope glycoprotein gp120. J Biol Chem 2001, 276:41913-41920.
    • (2001) J Biol Chem , vol.276 , pp. 41913-41920
    • Dai, G.1    Steede, N.K.2    Landry, S.J.3
  • 5
    • 42949139524 scopus 로고    scopus 로고
    • A systematic assessment of MHC class II peptide binding predictions and evaluation of a consensus approach
    • Wang P., Sidney J., Dow C., Mothe B., Sette A., Peters B. A systematic assessment of MHC class II peptide binding predictions and evaluation of a consensus approach. PLoS Comput Biol 2008, 4:e1000048.
    • (2008) PLoS Comput Biol , vol.4 , pp. e1000048
    • Wang, P.1    Sidney, J.2    Dow, C.3    Mothe, B.4    Sette, A.5    Peters, B.6
  • 6
    • 84904685791 scopus 로고    scopus 로고
    • Specificities of human CD4+ T cell responses to an inactivated flavivirus vaccine and infection: correlation with structure and epitope prediction
    • Schwaiger J., Aberle J.H., Stiasny K., Knapp B., Schreiner W., Fae I., et al. Specificities of human CD4+ T cell responses to an inactivated flavivirus vaccine and infection: correlation with structure and epitope prediction. J Virol 2014, 88:7828-7842.
    • (2014) J Virol , vol.88 , pp. 7828-7842
    • Schwaiger, J.1    Aberle, J.H.2    Stiasny, K.3    Knapp, B.4    Schreiner, W.5    Fae, I.6
  • 7
    • 33748475526 scopus 로고    scopus 로고
    • Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    • Delamarre L., Couture R., Mellman I., Trombetta E.S. Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis. J Exp Med 2006, 203:2049-2055.
    • (2006) J Exp Med , vol.203 , pp. 2049-2055
    • Delamarre, L.1    Couture, R.2    Mellman, I.3    Trombetta, E.S.4
  • 10
    • 0037016734 scopus 로고    scopus 로고
    • Proteolytic sensitivity and helper T-cell epitope immunodominance associated with the mobile loop in Hsp10s
    • Carmicle S., Dai G., Steede N.K., Landry S.J. Proteolytic sensitivity and helper T-cell epitope immunodominance associated with the mobile loop in Hsp10s. J Biol Chem 2002, 277:155-160.
    • (2002) J Biol Chem , vol.277 , pp. 155-160
    • Carmicle, S.1    Dai, G.2    Steede, N.K.3    Landry, S.J.4
  • 11
    • 0037016774 scopus 로고    scopus 로고
    • Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10: role of disordered loops
    • Dai G., Carmicle S., Steede N.K., Landry S.J. Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10: role of disordered loops. J Biol Chem 2002, 277:161-168.
    • (2002) J Biol Chem , vol.277 , pp. 161-168
    • Dai, G.1    Carmicle, S.2    Steede, N.K.3    Landry, S.J.4
  • 12
    • 20144363711 scopus 로고    scopus 로고
    • T cell epitope hotspots on the HIV Type 1 gp120 envelope protein overlap with tryptic fragments displayed by mass spectrometry
    • Brown S.A., Lockey T.D., Slaughter C., Slobod K.S., Surman S., Zirkel A., et al. T cell epitope hotspots on the HIV Type 1 gp120 envelope protein overlap with tryptic fragments displayed by mass spectrometry. AIDS Res Hum Retroviruses 2005, 21:165-170.
    • (2005) AIDS Res Hum Retroviruses , vol.21 , pp. 165-170
    • Brown, S.A.1    Lockey, T.D.2    Slaughter, C.3    Slobod, K.S.4    Surman, S.5    Zirkel, A.6
  • 13
    • 33748784872 scopus 로고    scopus 로고
    • Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes
    • Carmicle S., Steede N.K., Landry S.J. Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes. Mol Immunol 2007, 44:1159-1168.
    • (2007) Mol Immunol , vol.44 , pp. 1159-1168
    • Carmicle, S.1    Steede, N.K.2    Landry, S.J.3
  • 14
    • 77949345227 scopus 로고    scopus 로고
    • Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120
    • Mirano-Bascos D., Steede N.K., Robinson J.E., Landry S.J. Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120. J Virol 2010, 84:3303-3311.
    • (2010) J Virol , vol.84 , pp. 3303-3311
    • Mirano-Bascos, D.1    Steede, N.K.2    Robinson, J.E.3    Landry, S.J.4
  • 15
    • 57349153146 scopus 로고    scopus 로고
    • Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein
    • vanAnken E., Sanders R.W., Liscaljet I.M., Land A., Bontjer I., Tillemans S., et al. Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein. Mol Biol Cell 2008, 19:4298-4309.
    • (2008) Mol Biol Cell , vol.19 , pp. 4298-4309
    • vanAnken, E.1    Sanders, R.W.2    Liscaljet, I.M.3    Land, A.4    Bontjer, I.5    Tillemans, S.6
  • 16
    • 0029794529 scopus 로고    scopus 로고
    • A chimeric simian/human immunodeficiency virus expressing a primary patient human immunodeficiency virus type 1 isolate Env causes an AIDS-like disease after in vivo passage in rhesus monkeys
    • Reimann K.A., Li J.T., Veazey R., Halloran M., Park I.W., Karlsson G.B., et al. A chimeric simian/human immunodeficiency virus expressing a primary patient human immunodeficiency virus type 1 isolate Env causes an AIDS-like disease after in vivo passage in rhesus monkeys. J Virol 1996, 70:6922-6928.
    • (1996) J Virol , vol.70 , pp. 6922-6928
    • Reimann, K.A.1    Li, J.T.2    Veazey, R.3    Halloran, M.4    Park, I.W.5    Karlsson, G.B.6
  • 17
    • 15844388931 scopus 로고    scopus 로고
    • Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection
    • Liu R., Paxton W.A., Choe S., Ceradini D., Martin S.R., Horuk R., et al. Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection. Cell 1996, 86:367-377.
    • (1996) Cell , vol.86 , pp. 367-377
    • Liu, R.1    Paxton, W.A.2    Choe, S.3    Ceradini, D.4    Martin, S.R.5    Horuk, R.6
  • 18
    • 77954722964 scopus 로고    scopus 로고
    • Magnitude and breadth of a nonprotective neutralizing antibody response in an efficacy trial of a candidate HIV-1 gp120 vaccine
    • Gilbert P., Wang M., Wrin T., Petropoulos C., Gurwith M., Sinangil F., et al. Magnitude and breadth of a nonprotective neutralizing antibody response in an efficacy trial of a candidate HIV-1 gp120 vaccine. J Infect Dis 2010, 202:595-605.
    • (2010) J Infect Dis , vol.202 , pp. 595-605
    • Gilbert, P.1    Wang, M.2    Wrin, T.3    Petropoulos, C.4    Gurwith, M.5    Sinangil, F.6
  • 20
    • 84872228952 scopus 로고    scopus 로고
    • MHC class II-restricted presentation of the major house dust mite allergen Der p 1 Is GILT-dependent: implications for allergic asthma
    • West L.C., Grotzke J.E., Cresswell P. MHC class II-restricted presentation of the major house dust mite allergen Der p 1 Is GILT-dependent: implications for allergic asthma. PLoS ONE 2013, 8:e51343.
    • (2013) PLoS ONE , vol.8 , pp. e51343
    • West, L.C.1    Grotzke, J.E.2    Cresswell, P.3
  • 21
    • 0037141017 scopus 로고    scopus 로고
    • Absence of gamma-interferon-inducible lysosomal thiol reductase in melanomas disrupts T cell recognition of select immunodominant epitopes
    • Haque M.A., Li P., Jackson S.K., Zarour H.M., Hawes J.W., Phan U.T., et al. Absence of gamma-interferon-inducible lysosomal thiol reductase in melanomas disrupts T cell recognition of select immunodominant epitopes. J Exp Med 2002, 195:1267-1277.
    • (2002) J Exp Med , vol.195 , pp. 1267-1277
    • Haque, M.A.1    Li, P.2    Jackson, S.K.3    Zarour, H.M.4    Hawes, J.W.5    Phan, U.T.6
  • 22
    • 0036721601 scopus 로고    scopus 로고
    • Role of disulfide bonds in regulating antigen processing and epitope selection
    • Li P., Haque M.A., Blum J.S. Role of disulfide bonds in regulating antigen processing and epitope selection. J Immunol 2002, 169:2444-2450.
    • (2002) J Immunol , vol.169 , pp. 2444-2450
    • Li, P.1    Haque, M.A.2    Blum, J.S.3
  • 23
    • 2442696568 scopus 로고    scopus 로고
    • Differential requirements for endosomal reduction in the presentation of two H2-E(d)-restricted epitopes from influenza hemagglutinin
    • Sinnathamby G., Maric M., Cresswell P., Eisenlohr L.C. Differential requirements for endosomal reduction in the presentation of two H2-E(d)-restricted epitopes from influenza hemagglutinin. J Immunol 2004, 172:6607-6614.
    • (2004) J Immunol , vol.172 , pp. 6607-6614
    • Sinnathamby, G.1    Maric, M.2    Cresswell, P.3    Eisenlohr, L.C.4
  • 25
    • 84862612083 scopus 로고    scopus 로고
    • A switch in pathogenic mechanism in myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis in IFN-(-inducible lysosomal thiol reductase-free mice
    • Bergman C.M., Marta C.B., Maric M., Pfeiffer S.E., Cresswell P., Ruddle N.H. A switch in pathogenic mechanism in myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis in IFN-(-inducible lysosomal thiol reductase-free mice. J Immunol 2012, 188:6001-6009.
    • (2012) J Immunol , vol.188 , pp. 6001-6009
    • Bergman, C.M.1    Marta, C.B.2    Maric, M.3    Pfeiffer, S.E.4    Cresswell, P.5    Ruddle, N.H.6
  • 26
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • Moore J.P., Sodroski J. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J Virol 1996, 70:1863-1872.
    • (1996) J Virol , vol.70 , pp. 1863-1872
    • Moore, J.P.1    Sodroski, J.2
  • 27
    • 0026801056 scopus 로고
    • Discontinuous, conserved neutralization epitopes overlapping the CD4-binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein
    • Thali M., Furman C., Ho D.D., Robinson J., Tilley S., Pinter A., et al. Discontinuous, conserved neutralization epitopes overlapping the CD4-binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein. J Virol 1992, 66:5635-5641.
    • (1992) J Virol , vol.66 , pp. 5635-5641
    • Thali, M.1    Furman, C.2    Ho, D.D.3    Robinson, J.4    Tilley, S.5    Pinter, A.6
  • 28
    • 0242270786 scopus 로고    scopus 로고
    • Epitope mapping and characterization of a novel CD4-induced human monoclonal antibody capable of neutralizing primary HIV-1 strains
    • Xiang S.H., Wang L., Abreu M., Huang C.C., Kwong P.D., Rosenberg E., et al. Epitope mapping and characterization of a novel CD4-induced human monoclonal antibody capable of neutralizing primary HIV-1 strains. Virology 2003, 315:124-134.
    • (2003) Virology , vol.315 , pp. 124-134
    • Xiang, S.H.1    Wang, L.2    Abreu, M.3    Huang, C.C.4    Kwong, P.D.5    Rosenberg, E.6
  • 29
    • 0033587495 scopus 로고    scopus 로고
    • Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements
    • Manyusa S., Whitford D. Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements. Biochemistry 1999, 38:9533-9540.
    • (1999) Biochemistry , vol.38 , pp. 9533-9540
    • Manyusa, S.1    Whitford, D.2
  • 30
    • 79954535010 scopus 로고    scopus 로고
    • Characterization of a mutant Escherichia coli heat-labile toxin, LT(R192G/L211A), as a safe and effective oral adjuvant
    • Norton E.B., Lawson L.B., Freytag L.C., Clements J.D. Characterization of a mutant Escherichia coli heat-labile toxin, LT(R192G/L211A), as a safe and effective oral adjuvant. Clin Vaccine Immunol 2011, 18:546-551.
    • (2011) Clin Vaccine Immunol , vol.18 , pp. 546-551
    • Norton, E.B.1    Lawson, L.B.2    Freytag, L.C.3    Clements, J.D.4
  • 31
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996, 14:51-55. 29-32.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 32
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 1999, 41:95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 34
    • 84861173075 scopus 로고    scopus 로고
    • The Thai phase III trial (RV144) vaccine regimen induces T cell responses that preferentially target epitopes within the V2 region of HIV-1 envelope
    • de Souza M.S., Ratto-Kim S., Chuenarom W., Schuetz A., Chantakulkij S., Nuntapinit B., et al. The Thai phase III trial (RV144) vaccine regimen induces T cell responses that preferentially target epitopes within the V2 region of HIV-1 envelope. J Immunol 2012, 188:5166-5176.
    • (2012) J Immunol , vol.188 , pp. 5166-5176
    • de Souza, M.S.1    Ratto-Kim, S.2    Chuenarom, W.3    Schuetz, A.4    Chantakulkij, S.5    Nuntapinit, B.6
  • 35
    • 84855927062 scopus 로고    scopus 로고
    • HIV-specific CD4 T cell responses to different viral proteins have discordant associations with viral load and clinical outcome
    • Ranasinghe S., Flanders M., Cutler S., Soghoian D.Z., Ghebremichael M., Davis I., et al. HIV-specific CD4 T cell responses to different viral proteins have discordant associations with viral load and clinical outcome. J Virol 2012, 86:277-283.
    • (2012) J Virol , vol.86 , pp. 277-283
    • Ranasinghe, S.1    Flanders, M.2    Cutler, S.3    Soghoian, D.Z.4    Ghebremichael, M.5    Davis, I.6
  • 36
    • 47049114120 scopus 로고    scopus 로고
    • Antigen structure influences helper T-cell epitope dominance in the human immune response to HIV envelope glycoprotein gp120
    • Mirano-Bascos D., Tary-Lehmann M., Landry S.J. Antigen structure influences helper T-cell epitope dominance in the human immune response to HIV envelope glycoprotein gp120. Eur J Immunol 2008, 38:1231-1237.
    • (2008) Eur J Immunol , vol.38 , pp. 1231-1237
    • Mirano-Bascos, D.1    Tary-Lehmann, M.2    Landry, S.J.3
  • 37
    • 84864707126 scopus 로고    scopus 로고
    • HIV-1 envelope resistance to proteasomal cleavage: implications for vaccine induced immune responses
    • Steers N.J., Ratto-Kim S., de Souza M.S., Currier J.R., Kim J.H., Michael N.L., et al. HIV-1 envelope resistance to proteasomal cleavage: implications for vaccine induced immune responses. PLoS ONE 2012, 7:e42579.
    • (2012) PLoS ONE , vol.7 , pp. e42579
    • Steers, N.J.1    Ratto-Kim, S.2    de Souza, M.S.3    Currier, J.R.4    Kim, J.H.5    Michael, N.L.6
  • 38
    • 0027508349 scopus 로고
    • Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system
    • Yeh J.C., Seals J.R., Murphy C.I., van Halbeek H., Cummings R.D. Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system. Biochemistry 1993, 32:11087-11099.
    • (1993) Biochemistry , vol.32 , pp. 11087-11099
    • Yeh, J.C.1    Seals, J.R.2    Murphy, C.I.3    van Halbeek, H.4    Cummings, R.D.5
  • 39
    • 44849108137 scopus 로고    scopus 로고
    • Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes
    • Li H., Chien P.C.Jr., Tuen M., Visciano M.L., Cohen S., Blais S., et al. Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes. J Immunol 2008, 180:4011-4021.
    • (2008) J Immunol , vol.180 , pp. 4011-4021
    • Li, H.1    Chien, P.2    Tuen, M.3    Visciano, M.L.4    Cohen, S.5    Blais, S.6
  • 41
    • 70449359806 scopus 로고    scopus 로고
    • NN-align: An artificial neural network-based alignment algorithm for MHC class II peptide binding prediction
    • Nielsen M., Lund O., NN-align. An artificial neural network-based alignment algorithm for MHC class II peptide binding prediction. BMC Bioinf 2009, 10:296.
    • (2009) BMC Bioinf , vol.10 , pp. 296
    • Nielsen, M.1    Lund, O.2
  • 42
    • 84872498812 scopus 로고    scopus 로고
    • GILT expression in B cells diminishes cathepsin S steady-state protein expression and activity
    • Phipps-Yonas H., Semik V., Hastings K.T.G.I.L.T. expression in B cells diminishes cathepsin S steady-state protein expression and activity. Eur J Immunol 2013, 43:65-74.
    • (2013) Eur J Immunol , vol.43 , pp. 65-74
    • Phipps-Yonas, H.1    Semik, V.2    Hastings, K.T.3
  • 43
    • 48149111341 scopus 로고    scopus 로고
    • Gamma-IFN-inducible-lysosomal thiol reductase modulates acidic proteases and HLA class II antigen processing in melanoma
    • Goldstein O.G., Hajiaghamohseni L.M., Amria S., Sundaram K., Reddy S.V., Haque A. Gamma-IFN-inducible-lysosomal thiol reductase modulates acidic proteases and HLA class II antigen processing in melanoma. Cancer Immunol Immunother 2008, 57:1461-1470.
    • (2008) Cancer Immunol Immunother , vol.57 , pp. 1461-1470
    • Goldstein, O.G.1    Hajiaghamohseni, L.M.2    Amria, S.3    Sundaram, K.4    Reddy, S.V.5    Haque, A.6
  • 44
    • 0031265431 scopus 로고    scopus 로고
    • Local protein instability predictive of helper T-cell epitopes
    • Landry S.J. Local protein instability predictive of helper T-cell epitopes. Immunol Today 1997, 18:527-532.
    • (1997) Immunol Today , vol.18 , pp. 527-532
    • Landry, S.J.1
  • 45
    • 0033696962 scopus 로고    scopus 로고
    • Control of antigen presentation by a single protease cleavage site
    • Antoniou A.N., Blackwood S.L., Mazzeo D., Watts C. Control of antigen presentation by a single protease cleavage site. Immunity 2000, 12:391-398.
    • (2000) Immunity , vol.12 , pp. 391-398
    • Antoniou, A.N.1    Blackwood, S.L.2    Mazzeo, D.3    Watts, C.4
  • 46
    • 77949265993 scopus 로고    scopus 로고
    • Naturally processed T cell-activating peptides of the major birch pollen allergen
    • 8 e1-8 e2
    • Mutschlechner S., Egger M., Briza P., Wallner M., Lackner P., Karle A., et al. Naturally processed T cell-activating peptides of the major birch pollen allergen. J Allergy Clin Immunol 2010, 125:711-718. 8 e1-8 e2.
    • (2010) J Allergy Clin Immunol , vol.125 , pp. 711-718
    • Mutschlechner, S.1    Egger, M.2    Briza, P.3    Wallner, M.4    Lackner, P.5    Karle, A.6
  • 47
    • 0031931326 scopus 로고    scopus 로고
    • Six unrelated HLA-DR-matched adults recognize identical CD4(+) T cell epitopes from influenza A haemagglutinin that are not simply peptides with high HLA-DR binding affinities
    • Gelder C., Davenport M., Barnardo M., Bourne T., Lamb J., Askonas B., et al. Six unrelated HLA-DR-matched adults recognize identical CD4(+) T cell epitopes from influenza A haemagglutinin that are not simply peptides with high HLA-DR binding affinities. Int Immunol 1998, 10:211-222.
    • (1998) Int Immunol , vol.10 , pp. 211-222
    • Gelder, C.1    Davenport, M.2    Barnardo, M.3    Bourne, T.4    Lamb, J.5    Askonas, B.6
  • 48
    • 0031178878 scopus 로고    scopus 로고
    • Determinants of T cell reactivity to the Mycobacterium leprae GroES homologue
    • Kim J., Sette A., Rodda S., Southwood S., Sieling P.A., Mehra V., et al. Determinants of T cell reactivity to the Mycobacterium leprae GroES homologue. J Immunol 1997, 159:335-343.
    • (1997) J Immunol , vol.159 , pp. 335-343
    • Kim, J.1    Sette, A.2    Rodda, S.3    Southwood, S.4    Sieling, P.A.5    Mehra, V.6
  • 50
    • 0032496213 scopus 로고    scopus 로고
    • Presentation of the Goodpasture autoantigen to CD4 T cells is influenced more by processing constraints than by HLA class II peptide binding preferences
    • Phelps R.G., Jones V.L., Coughlan M., Turner A.N., Rees A.J. Presentation of the Goodpasture autoantigen to CD4 T cells is influenced more by processing constraints than by HLA class II peptide binding preferences. J Biol Chem 1998, 273:11440-11447.
    • (1998) J Biol Chem , vol.273 , pp. 11440-11447
    • Phelps, R.G.1    Jones, V.L.2    Coughlan, M.3    Turner, A.N.4    Rees, A.J.5
  • 51
    • 84903788684 scopus 로고    scopus 로고
    • Proteome-wide analysis of HIV-specific naive and memory CD4(+) T cells in unexposed blood donors
    • Campion S.L., Brodie T.M., Fischer W., Korber B.T., Rossetti A., Goonetilleke N., et al. Proteome-wide analysis of HIV-specific naive and memory CD4(+) T cells in unexposed blood donors. J Exp Med 2014, 211:1273-1280.
    • (2014) J Exp Med , vol.211 , pp. 1273-1280
    • Campion, S.L.1    Brodie, T.M.2    Fischer, W.3    Korber, B.T.4    Rossetti, A.5    Goonetilleke, N.6
  • 52
    • 38349165050 scopus 로고    scopus 로고
    • + T-cell epitope dominance in influenza virus hemagglutinin
    • + T-cell epitope dominance in influenza virus hemagglutinin. J Virol 2008, 82:1238-1248.
    • (2008) J Virol , vol.82 , pp. 1238-1248
    • Landry, S.J.1
  • 54
    • 84921278229 scopus 로고    scopus 로고
    • T cell receptor cross-reactivity between similar foreign and self peptides influences naive cell population size and autoimmunity
    • Nelson R.W., Beisang D., Tubo N.J., Dileepan T., Wiesner D.L., Nielsen K., et al. T cell receptor cross-reactivity between similar foreign and self peptides influences naive cell population size and autoimmunity. Immunity 2015, 42:95-107.
    • (2015) Immunity , vol.42 , pp. 95-107
    • Nelson, R.W.1    Beisang, D.2    Tubo, N.J.3    Dileepan, T.4    Wiesner, D.L.5    Nielsen, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.