메뉴 건너뛰기




Volumn 34, Issue 6, 1997, Pages 493-503

Affinity and kinetics of the interactions between an αβ T-cell receptor and its superantigen and class II-MHC/peptide ligands

Author keywords

Binding constants; Leucine zipper; MHC; SPR; Superantigens; TCR

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; SUPERANTIGEN;

EID: 18744436304     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(97)00044-8     Document Type: Article
Times cited : (19)

References (58)
  • 1
    • 0025233576 scopus 로고
    • Genetic and mutational analysis of the T-cell antigen receptor
    • Ashwell J. D. and Klausner R. D. (1990) Genetic and mutational analysis of the T-cell antigen receptor. A. Rev. Immun. 8, 139-167.
    • (1990) A. Rev. Immun. , vol.8 , pp. 139-167
    • Ashwell, J.D.1    Klausner, R.D.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the protein-dye binding. Analyt. Biochem. 72, 248-254.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0028053838 scopus 로고
    • Evidence for a functional interaction between the β chain of major histocompatibility complex class II and the T cell receptor α chain during recognition of a bacterial superantigen
    • Deckhut A. M., Chien Y.-H., Blackman M. A. and Woodland D. L. (1994) Evidence for a functional interaction between the β chain of major histocompatibility complex class II and the T cell receptor α chain during recognition of a bacterial superantigen. J. Exp. Med. 180, 1931-1935.
    • (1994) J. Exp. Med. , vol.180 , pp. 1931-1935
    • Deckhut, A.M.1    Chien, Y.-H.2    Blackman, M.A.3    Woodland, D.L.4
  • 9
    • 0026750669 scopus 로고
    • High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers
    • Engel I., Ottenhoff M. and Klausner R. D. (1992) High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers. Science 256, 1318-1321.
    • (1992) Science , vol.256 , pp. 1318-1321
    • Engel, I.1    Ottenhoff, M.2    Klausner, R.D.3
  • 10
    • 0029883778 scopus 로고    scopus 로고
    • Biophysical studies of T-cell receptors and their ligands
    • Fremont D. H., Rees W. A. and Kozono H. (1996) Biophysical studies of T-cell receptors and their ligands. Curr. Opin. Immun. 8, 93-100.
    • (1996) Curr. Opin. Immun. , vol.8 , pp. 93-100
    • Fremont, D.H.1    Rees, W.A.2    Kozono, H.3
  • 14
    • 0028577182 scopus 로고
    • Binding of soluble natural ligands to a soluble human T-cell receptor fragment produced in Escherichia coli
    • Hilyard K. L., Reyburn H., Chung S., Bell J. I. and Strominger J. L. (1994) Binding of soluble natural ligands to a soluble human T-cell receptor fragment produced in Escherichia coli. Proc. natn. Acad. Sci. U.S.A. 91, 9057-9061.
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.91 , pp. 9057-9061
    • Hilyard, K.L.1    Reyburn, H.2    Chung, S.3    Bell, J.I.4    Strominger, J.L.5
  • 15
    • 0029923425 scopus 로고    scopus 로고
    • Different superantigens interact with distinct sites in the V β domain of a single T cell receptor
    • Hong S.-C., Waterbury G., Janeway C. A. Jr. (1996) Different superantigens interact with distinct sites in the V β domain of a single T cell receptor. J. Exp. Med. 183, 1437-1446.
    • (1996) J. Exp. Med. , vol.183 , pp. 1437-1446
    • Hong, S.-C.1    Waterbury, G.2    Janeway C.A., Jr.3
  • 17
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson B., Lofas S. and Lindqvist G. (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Analyt. Biochem. 198, 268-277.
    • (1991) Analyt. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Lofas, S.2    Lindqvist, G.3
  • 18
    • 0024837614 scopus 로고
    • Antibody-mediated activation of T-cell clones as a method for screening hybridomas producing antibodies to the T cell receptor
    • Kanagawa O. (1989) Antibody-mediated activation of T-cell clones as a method for screening hybridomas producing antibodies to the T cell receptor. J. Exp. Med. 170, 1513-1519.
    • (1989) J. Exp. Med. , vol.170 , pp. 1513-1519
    • Kanagawa, O.1
  • 19
    • 0028168571 scopus 로고
    • Binding of a soluble αβ T-cell receptor to superantigen/major histocompatibility complex ligands
    • Kappler J., White J., Kozono H., Clements J. and Marrack P. (1994) Binding of a soluble αβ T-cell receptor to superantigen/major histocompatibility complex ligands. Proc. natn. Acad. Sci. U.S.A. 91, 8462-8466.
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.91 , pp. 8462-8466
    • Kappler, J.1    White, J.2    Kozono, H.3    Clements, J.4    Marrack, P.5
  • 20
    • 0020602877 scopus 로고
    • Both a monoclonal antibody and antisera specific for determinants unique to individual cloned helper T cell lines can substitute for antigen and antigen-presenting cells in the activation of T cells
    • Kaye J., Porcelli S., Tite J., Jones B. and Janeway C. A. Jr. (1983) Both a monoclonal antibody and antisera specific for determinants unique to individual cloned helper T cell lines can substitute for antigen and antigen-presenting cells in the activation of T cells. J. Exp. Med. 158, 836-856.
    • (1983) J. Exp. Med. , vol.158 , pp. 836-856
    • Kaye, J.1    Porcelli, S.2    Tite, J.3    Jones, B.4    Janeway C.A., Jr.5
  • 21
    • 0027728318 scopus 로고
    • A simple and rapid method for the purification of GroEL, an Escherichia coli homolog of the heat shock protein 60 family of molecular chaperonins
    • Khandekar S. S., Bettencourt B. M., Kelley K. C. and Recny M. A. (1993) A simple and rapid method for the purification of GroEL, an Escherichia coli homolog of the heat shock protein 60 family of molecular chaperonins. Protein Expression and Purification 4, 580-584.
    • (1993) Protein Expression and Purification , vol.4 , pp. 580-584
    • Khandekar, S.S.1    Bettencourt, B.M.2    Kelley, K.C.3    Recny, M.A.4
  • 22
    • 0029153035 scopus 로고
    • Multiple binding sites for bacterial superantigens on soluble class II molecules
    • Kozono H., Parker D., White J., Marrack P. and Kappler J. (1995) Multiple binding sites for bacterial superantigens on soluble class II molecules. Immunity 3, 187-196.
    • (1995) Immunity , vol.3 , pp. 187-196
    • Kozono, H.1    Parker, D.2    White, J.3    Marrack, P.4    Kappler, J.5
  • 23
    • 0028233838 scopus 로고
    • Production of soluble MHC class II proteins with covalently bound single peptides
    • Kozono H., White J., Clements J., Marrack P. and Kappler J. (1994) Production of soluble MHC class II proteins with covalently bound single peptides. Nature 369, 151-154.
    • (1994) Nature , vol.369 , pp. 151-154
    • Kozono, H.1    White, J.2    Clements, J.3    Marrack, P.4    Kappler, J.5
  • 24
    • 0024535530 scopus 로고
    • Characterization of a monoclonal antibody which detects all murine αβ T cell receptors
    • Kubo R. T., Born W., Kappler J. W., Marrack P. and Pigeon M. (1989) Characterization of a monoclonal antibody which detects all murine αβ T cell receptors. J. Immun. 142, 2736-2742.
    • (1989) J. Immun. , vol.142 , pp. 2736-2742
    • Kubo, R.T.1    Born, W.2    Kappler, J.W.3    Marrack, P.4    Pigeon, M.5
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277, 680-682.
    • (1970) Nature , vol.277 , pp. 680-682
    • Laemmli, U.K.1
  • 26
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons D. S., Lieberman S. A., Hampl J., Boniface J. J., Chien Y.-H., Berg L. J. and Davis M. M. (1996) A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 5, 53-61.
    • (1996) Immunity , vol.5 , pp. 53-61
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.-H.5    Berg, L.J.6    Davis, M.M.7
  • 28
    • 0027286137 scopus 로고
    • Surface plasmon resonance for detection and measurement of antibody-antigen affinity and kinetics
    • Malmqvist M. (1993) Surface plasmon resonance for detection and measurement of antibody-antigen affinity and kinetics. Curr. Biol. 5, 282-286.
    • (1993) Curr. Biol. , vol.5 , pp. 282-286
    • Malmqvist, M.1
  • 29
    • 0030582113 scopus 로고    scopus 로고
    • An affinity for learning
    • Margulies D. H. (1996) An affinity for learning. Nature 381, 558-559.
    • (1996) Nature , vol.381 , pp. 558-559
    • Margulies, D.H.1
  • 30
    • 37049178741 scopus 로고
    • The Staphylococcal enterotoxins and their relatives
    • Marrack P. and Kappler J. (1990) The Staphylococcal enterotoxins and their relatives. Science 248, 705-711.
    • (1990) Science , vol.248 , pp. 705-711
    • Marrack, P.1    Kappler, J.2
  • 32
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 33
    • 0026345967 scopus 로고
    • Low affinity interaction of peptide-MHC complexes with T cell receptors
    • Matsui K., Boniface J. J., Reay P. A., Schild H., Groth F. and Davis M. M. (1991) Low affinity interaction of peptide-MHC complexes with T cell receptors. Science 254, 1788-1791.
    • (1991) Science , vol.254 , pp. 1788-1791
    • Matsui, K.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Groth, F.5    Davis, M.M.6
  • 35
    • 10544232275 scopus 로고    scopus 로고
    • Immunization with soluble BDC2.5 T cell receptor-immunoglobulin (TCR-IgG1) chimeric protein: Antibody specificity and protection of non obese diabetic (NOD) mice against adoptive transfer of diabetes by maternal immunization
    • McKeever U., Khandekar S., Newcomb J., Naylor J., Gregory P., Brauer P., Jesson M., Bettencourt B., Burke E., Alderson A., Banerji J., Haskins K. and Jones B. (1996) Immunization with soluble BDC2.5 T cell receptor-immunoglobulin (TCR-IgG1) chimeric protein: antibody specificity and protection of non obese diabetic (NOD) mice against adoptive transfer of diabetes by maternal immunization. J. Exp. Med. 184, 1755-1768.
    • (1996) J. Exp. Med. , vol.184 , pp. 1755-1768
    • McKeever, U.1    Khandekar, S.2    Newcomb, J.3    Naylor, J.4    Gregory, P.5    Brauer, P.6    Jesson, M.7    Bettencourt, B.8    Burke, E.9    Alderson, A.10    Banerji, J.11    Haskins, K.12    Jones, B.13
  • 36
    • 0027932728 scopus 로고
    • Human cell-adhesion molecule CD2 bind CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59
    • Merwe P. A. van der, Barclay A. N., Mason D. W., Davies E. A., Morgan B. P., Tone M., Krishnan A. K. C., Lanelli C. and Davis S. J. (1994) Human cell-adhesion molecule CD2 bind CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59. Biochemistry 33, 10149-10160.
    • (1994) Biochemistry , vol.33 , pp. 10149-10160
    • Van Der Merwe, P.A.1    Barclay, A.N.2    Mason, D.W.3    Davies, E.A.4    Morgan, B.P.5    Tone, M.6    Krishnan, A.K.C.7    Lanelli, C.8    Davis, S.J.9
  • 38
    • 0026650992 scopus 로고
    • The human immunodeficiency virus gp120 binding site on CD4: Delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure
    • Moebius U., Clayton L. K., Abraham S., Harrison S. C. and Reinherz E. L. (1992) The human immunodeficiency virus gp120 binding site on CD4: delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure. J. Exp. Med. 176, 507-517.
    • (1992) J. Exp. Med. , vol.176 , pp. 507-517
    • Moebius, U.1    Clayton, L.K.2    Abraham, S.3    Harrison, S.C.4    Reinherz, E.L.5
  • 42
    • 0028157937 scopus 로고
    • Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: A critique of the surface plasmon resonance literature
    • O'Shannessy D. J. (1994) Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature. Curr. Biol. 5, 65-71.
    • (1994) Curr. Biol. , vol.5 , pp. 65-71
    • O'Shannessy, D.J.1
  • 43
    • 0000236570 scopus 로고
    • Peptide "Velcro": Design of a heterodimeric coiled coil
    • O'Shea E. K., Lumb K. L. and Kim P. S. (1993) Peptide "Velcro": design of a heterodimeric coiled coil. Curr. Biol. 3, 658-667.
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.L.2    Kim, P.S.3
  • 44
    • 0025788111 scopus 로고
    • Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli
    • Pantoliano M. W., Bird R. E., Johnson S., Asel E. D., Dodd S. W., Wood J. F. and Hardman K. D. (1991) Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli. Biochemistry 30, 10117-10125.
    • (1991) Biochemistry , vol.30 , pp. 10117-10125
    • Pantoliano, M.W.1    Bird, R.E.2    Johnson, S.3    Asel, E.D.4    Dodd, S.W.5    Wood, J.F.6    Hardman, K.D.7
  • 46
    • 0027330886 scopus 로고
    • A comparison of large-scale Sf9 insect cell growth and protein production: Stirred vessel vs. airlift
    • Rice J. W., Rankl N. B., Gurganus T. M., Marr C. M., Barna J. B., Walters M. M. and Burns D. J. (1993) A comparison of large-scale Sf9 insect cell growth and protein production: stirred vessel vs. airlift. Biotechniques 15, 1015-1059.
    • (1993) Biotechniques , vol.15 , pp. 1015-1059
    • Rice, J.W.1    Rankl, N.B.2    Gurganus, T.M.3    Marr, C.M.4    Barna, J.B.5    Walters, M.M.6    Burns, D.J.7
  • 47
    • 0025870669 scopus 로고
    • A role for peptide in determining MHC class II structure
    • 0
    • Sadegh-Nasseri S. and Germain R. N. (1991) A role for peptide in determining MHC class II structure. Nature 0, 167-170.
    • (1991) Nature , pp. 167-170
    • Sadegh-Nasseri, S.1    Germain, R.N.2
  • 48
    • 0024549388 scopus 로고
    • Structural and binding analysis of a two domain extracellular CD2 molecule
    • Sayre P. H., Hussey R. E., Chang H.-C., Ciardelli T. L. and Reinherz E. L. (1989) Structural and binding analysis of a two domain extracellular CD2 molecule. J. Exp. Med. 169, 995-1009.
    • (1989) J. Exp. Med. , vol.169 , pp. 995-1009
    • Sayre, P.H.1    Hussey, R.E.2    Chang, H.-C.3    Ciardelli, T.L.4    Reinherz, E.L.5
  • 49
    • 0029979998 scopus 로고    scopus 로고
    • Role of chain pairing for the productivity of functional soluble IA major histocompatibility complex class II molecules
    • Scott C. A., Garcia K. C., Carbone F. R., Wilson I. A. and Teyton E. (1996) Role of chain pairing for the productivity of functional soluble IA major histocompatibility complex class II molecules. J. Exp. Med. 183, 2087-2095.
    • (1996) J. Exp. Med. , vol.183 , pp. 2087-2095
    • Scott, C.A.1    Garcia, K.C.2    Carbone, F.R.3    Wilson, I.A.4    Teyton, E.5
  • 51
    • 0026571278 scopus 로고
    • The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide
    • Stern L. J. and Wiley D. C. (1992) The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide. Cell 68, 465-477.
    • (1992) Cell , vol.68 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 52
    • 0028773294 scopus 로고
    • Antigenic peptide binding by class I and class II histocompatibility proteins
    • Stern L. J. and Wiley D. C. (1994) Antigenic peptide binding by class I and class II histocompatibility proteins. Curr. Biol. 2, 245-251.
    • (1994) Curr. Biol. , vol.2 , pp. 245-251
    • Stern, L.J.1    Wiley, D.C.2
  • 53
    • 0001962451 scopus 로고
    • A manual of methods for baculovirus vectors and insect cell culture procedures
    • Summers M. D. and Smith G. E. (1988) A manual of methods for baculovirus vectors and insect cell culture procedures. Texas Agriculatural Experimental Station Bulletin 1555, 10-39.
    • (1988) Texas Agriculatural Experimental Station Bulletin , vol.1555 , pp. 10-39
    • Summers, M.D.1    Smith, G.E.2
  • 54
    • 0028410566 scopus 로고
    • Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexes
    • Sykulev Y., Brunmark A., Jackson M., Cohen R. J., Peterson P. and Eisen H. N. (1994) Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexes. Immunity 1, 15-22.
    • (1994) Immunity , vol.1 , pp. 15-22
    • Sykulev, Y.1    Brunmark, A.2    Jackson, M.3    Cohen, R.J.4    Peterson, P.5    Eisen, H.N.6
  • 55
    • 0028104782 scopus 로고
    • High-affinity reactions between antigen-specific T-cell receptors and peptides associated with allogeneic and syngeneic major histocompatibility complex class I proteins
    • Sykulev Y., Brunmark A., Tsomides T. J., Kageyama S., Jackson M., Peterson P. and Eisen H. N. (1994) High-affinity reactions between antigen-specific T-cell receptors and peptides associated with allogeneic and syngeneic major histocompatibility complex class I proteins. Proc. natn. Acad. Sci. U.S.A. 91, 11487-11491.
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.91 , pp. 11487-11491
    • Sykulev, Y.1    Brunmark, A.2    Tsomides, T.J.3    Kageyama, S.4    Jackson, M.5    Peterson, P.6    Eisen, H.N.7
  • 56
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • Valitutti S., Muller S., Cella M., Padovan E. and Lanzavecchia A. (1995) Serial triggering of many T-cell receptors by a few peptide-MHC complexes. Nature 375, 148-151.
    • (1995) Nature , vol.375 , pp. 148-151
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Padovan, E.4    Lanzavecchia, A.5
  • 57
    • 0026553367 scopus 로고
    • Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor
    • Weber S., Traunecker A., Oliveri F., Gerhard W. and Karjalainen K. (1992) Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor. Nature 356, 793-796.
    • (1992) Nature , vol.356 , pp. 793-796
    • Weber, S.1    Traunecker, A.2    Oliveri, F.3    Gerhard, W.4    Karjalainen, K.5
  • 58
    • 0027229409 scopus 로고
    • How do T-cell receptors, MHC molecules and superantigens get together?
    • Woodland D. L. and Blackman M. A. (1993) How do T-cell receptors, MHC molecules and superantigens get together? Immun. Today 14, 208-211.
    • (1993) Immun. Today , vol.14 , pp. 208-211
    • Woodland, D.L.1    Blackman, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.