메뉴 건너뛰기




Volumn 169, Issue 9, 2002, Pages 5171-5180

Increasing the affinity of a human IgG1 for the neonatal Fc receptor: Biological consequences

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; FC RECEPTOR N; IMMUNOGLOBULIN G1; UNCLASSIFIED DRUG;

EID: 0036839457     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.169.9.5171     Document Type: Article
Times cited : (292)

References (48)
  • 1
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I-related receptor FcRn
    • Ghetie, V., and S. Ward. 2000. Multiple roles for the major histocompatibility complex class I-related receptor FcRn. Annu. Rev. Immunol. 18:739.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 739
    • Ghetie, V.1    Ward, S.2
  • 2
    • 0018836262 scopus 로고
    • Studies on the immunoglobulin-G Fc-fragment receptor from neonatal rat small intestine
    • Wallace, K. H., and A. R. Rees. 1980. Studies on the immunoglobulin-G Fc-fragment receptor from neonatal rat small intestine. Biochem. J. 188:9.
    • (1980) Biochem. J. , vol.188 , pp. 9
    • Wallace, K.H.1    Rees, A.R.2
  • 3
    • 0029842013 scopus 로고    scopus 로고
    • Localization of the site of the IgG that regulates maternofetal transmission in mice
    • Medesan, C., C. Radu, J. K. Kim, V. Ghetie, and S. Ward. 1996. Localization of the site of the IgG that regulates maternofetal transmission in mice. Eur. J. Immunol. 26:2533.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2533
    • Medesan, C.1    Radu, C.2    Kim, J.K.3    Ghetie, V.4    Ward, S.5
  • 4
    • 0032767535 scopus 로고    scopus 로고
    • Identification and function of neonatal Fc receptor in mammary gland of lactating mice
    • Cianga, P., C. Medesan, J. Richardson, V. Ghetie, and E. S. Ward. 1999. Identification and function of neonatal Fc receptor in mammary gland of lactating mice. Eur. J. Immunol. 29:2515.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2515
    • Cianga, P.1    Medesan, C.2    Richardson, J.3    Ghetie, V.4    Ward, E.S.5
  • 7
    • 0028061347 scopus 로고
    • A major histocompatibility complex class I-like Fc receptor cloned from human placenta: Possible role in transfer of immunoglobulin G from mother to fetus
    • Story, C. M., J. E. Mikulska, and N. E. Simister. 1994. A major histocompatibility complex class I-like Fc receptor cloned from human placenta: Possible role in transfer of immunoglobulin G from mother to fetus. J. Exp. Med. 180:2377.
    • (1994) J. Exp. Med. , vol.180 , pp. 2377
    • Story, C.M.1    Mikulska, J.E.2    Simister, N.E.3
  • 8
    • 0034879134 scopus 로고    scopus 로고
    • The MHC class I-related receptor, FcRn, plays an essential role in the matemofetal transfer of γ-globulin in humans
    • Firan, M., R. Bawdon, C. Radu, R. J. Ober, D. Eaken, F. Antohe, V. Ghetie, and S. Ward. 2001. The MHC class I-related receptor, FcRn, plays an essential role in the matemofetal transfer of γ-globulin in humans. Int. Immunol. 13:993.
    • (2001) Int. Immunol. , vol.13 , pp. 993
    • Firan, M.1    Bawdon, R.2    Radu, C.3    Ober, R.J.4    Eaken, D.5    Antohe, F.6    Ghetie, V.7    Ward, S.8
  • 12
    • 0033393536 scopus 로고    scopus 로고
    • Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn
    • Kim, J. K., M. Firan, C. Radu, C. H. Kim, V. Ghetie, and S. Ward. 1999. Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn. Eur. J. Immunol. 29:2819.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2819
    • Kim, J.K.1    Firan, M.2    Radu, C.3    Kim, C.H.4    Ghetie, V.5    Ward, S.6
  • 13
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • Simister, N. E., and K. E. Mostov. 1989. An Fc receptor structurally related to MHC class I antigens. Nature 337:184.
    • (1989) Nature , vol.337 , pp. 184
    • Simister, N.E.1    Mostov, K.E.2
  • 15
    • 0028051652 scopus 로고
    • Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor
    • Burmeister, W. P., L. N. Gastinel, N. E. Simister, M. L. Blum. and P. J. Bjorkman. 1994. Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor. Nature 372:336.
    • (1994) Nature , vol.372 , pp. 336
    • Burmeister, W.P.1    Gastinel, L.N.2    Simister, N.E.3    Blum, M.L.4    Bjorkman, P.J.5
  • 16
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister, W. P., A. H. Huber, and P. J. Bjorkman. 1994. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372:379.
    • (1994) Nature , vol.372 , pp. 379
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 17
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor
    • West, A. P., and P. J. Bjorkman. 2000. Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor. Biochemistry 39:9698.
    • (2000) Biochemistry , vol.39 , pp. 9698
    • West, A.P.1    Bjorkman, P.J.2
  • 18
    • 0017166982 scopus 로고
    • pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat
    • Rodewald, R. 1976. pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat. J. Cell Biol. 71:666.
    • (1976) J. Cell Biol. , vol.71 , pp. 666
    • Rodewald, R.1
  • 19
    • 0029947639 scopus 로고    scopus 로고
    • Co-localization of the neonatal Fcγ receptor and IgG in human placental term syncytiotrophoblasts
    • Kristoffersen, E. K., and R. Matre. 1996. Co-localization of the neonatal Fcγ receptor and IgG in human placental term syncytiotrophoblasts. Eur. J. Immunol. 26:1668.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1668
    • Kristoffersen, E.K.1    Matre, R.2
  • 22
    • 0028220297 scopus 로고
    • Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis
    • Kim, J. K., M. F. Tsen, V. Ghetie, and S. Ward. 1994. Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis. Eur. J. Immunol. 24:542.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 542
    • Kim, J.K.1    Tsen, M.F.2    Ghetie, V.3    Ward, S.4
  • 23
    • 0035012654 scopus 로고    scopus 로고
    • Crystal structure at 2.8Å of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding
    • Martin, W. L., A. P. West, L. Gan, and P. J. Bjorkman. 2001. Crystal structure at 2.8Å of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding. Mol. Cell 7:867.
    • (2001) Mol. Cell , vol.7 , pp. 867
    • Martin, W.L.1    West, A.P.2    Gan, L.3    Bjorkman, P.J.4
  • 24
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR
    • Shields, R. L., A. K. Namenuk, K. Hong, Y. G. Meng, J. Rae, J. Briggs, D. Xie, J. Lai, A. Stadlen, B. Li, et al. 2001. High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR. J. Biol. Chem. 276:6591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10
  • 25
    • 0028467948 scopus 로고
    • Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand
    • Raghavan, M., M. Y. Chen, L. N. Gastinel, and P. J. Bjorkman. 1994. Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand. Immunity 1:303.
    • (1994) Immunity , vol.1 , pp. 303
    • Raghavan, M.1    Chen, M.Y.2    Gastinel, L.N.3    Bjorkman, P.J.4
  • 28
    • 0028808880 scopus 로고
    • Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants
    • Raghavan, M., V. R. Bonagura, S. L. Morrison, and P. J. Bjorkman. 1995. Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants. Biochemistry 34:14649.
    • (1995) Biochemistry , vol.34 , pp. 14649
    • Raghavan, M.1    Bonagura, V.R.2    Morrison, S.L.3    Bjorkman, P.J.4
  • 29
    • 0030130749 scopus 로고    scopus 로고
    • The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn
    • Popov, S., J. G. Hubbard, J. Kim, B. Ober, V. Ghetie, and E. S. Ward. 1996. The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn. Mol. Immunol. 33:521.
    • (1996) Mol. Immunol. , vol.33 , pp. 521
    • Popov, S.1    Hubbard, J.G.2    Kim, J.3    Ober, B.4    Ghetie, V.5    Ward, E.S.6
  • 32
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection, Methods Enzymol. 154:367.
    • (1987) Methods Enzymol. , vol.154 , pp. 367
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 33
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Péase. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 15:51.
    • (1989) Gene , vol.15 , pp. 51
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Péase, L.R.5
  • 37
    • 0027932728 scopus 로고
    • Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59
    • Van der Merwe, P. A., A. N. Barclay, D. W. Mason, E. A. Davies. B. P. Morgan, M. Tone, A. K. C. Kilshnam, C. Ianelli, and S. J. Davis. 1994, Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59, Biochemistry 33:10149.
    • (1994) Biochemistry , vol.33 , pp. 10149
    • 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    Kilshnam, A.K.C.7    Ianelli, C.8    Davis, S.J.9
  • 38
    • 0027500841 scopus 로고
    • Affinity and kinetic analysis of the interaction of the cell adhesion molecules rat CD2 and CD48
    • Van der Merwe, P. A., M. H. Brown, S. J. Davis, and A. N. Barclay. 1993. Affinity and kinetic analysis of the interaction of the cell adhesion molecules rat CD2 and CD48. EMBO J. 12:4945.
    • (1993) EMBO J. , vol.12 , pp. 4945
    • Van der Merwe, P.A.1    Brown, M.H.2    Davis, S.J.3    Barclay, A.N.4
  • 39
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., S. Lofas, and G. Lindquist. 1991. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198:268.
    • (1991) Anal. Biochem. , vol.198 , pp. 268
    • Johnsson, B.1    Lofas, S.2    Lindquist, G.3
  • 40
    • 0029764534 scopus 로고    scopus 로고
    • A mutational analysis of the binding of two different proteins to the same antibody
    • Dall'Acqua, W., E. R. Goldman, E. Eisenstein, and R. A. Mariuzza. 1996. A mutational analysis of the binding of two different proteins to the same antibody. Biochemistry 35:9667.
    • (1996) Biochemistry , vol.35 , pp. 9667
    • Dall'Acqua, W.1    Goldman, E.R.2    Eisenstein, E.3    Mariuzza, R.A.4
  • 41
    • 34547383713 scopus 로고
    • Preparation of iodine-131 labelled human growth hormone of high specific activity
    • Hunter, W. M., and F. C. Greenwood. 1962. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature 194:495.
    • (1962) Nature , vol.194 , pp. 495
    • Hunter, W.M.1    Greenwood, F.C.2
  • 42
    • 0025336478 scopus 로고
    • Autoradiography using storage phosphor technology
    • Johnston, R. F., S. C. Pickett, and D. L. Barker. 1990. Autoradiography using storage phosphor technology. Electrophoresis 11:355.
    • (1990) Electrophoresis , vol.11 , pp. 355
    • Johnston, R.F.1    Pickett, S.C.2    Barker, D.L.3
  • 43
    • 0039643451 scopus 로고    scopus 로고
    • Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand
    • Sanchez, L. M., D. M. Penny, and P. J. Bjorkman. 1999. Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand. Biochemistry 38:9471.
    • (1999) Biochemistry , vol.38 , pp. 9471
    • Sanchez, L.M.1    Penny, D.M.2    Bjorkman, P.J.3
  • 44
    • 0033613146 scopus 로고    scopus 로고
    • Characterization of the 2:1 complex between the class I-related Fc receptor and its Fc ligand in solution
    • Martin, W. L., and P. J. Bjorkman. 1999. Characterization of the 2:1 complex between the class I-related Fc receptor and its Fc ligand in solution. Biochemistry 38:12639.
    • (1999) Biochemistry , vol.38 , pp. 12639
    • Martin, W.L.1    Bjorkman, P.J.2
  • 45
    • 0030806484 scopus 로고    scopus 로고
    • High affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization
    • Vaughn, D. E., and P. J. Bjorkman. 1997. High affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization. Biochemistry 36:9374.
    • (1997) Biochemistry , vol.36 , pp. 9374
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 46
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. 1994. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389.
    • (1994) Nature , vol.370 , pp. 389
    • Stemmer, W.P.1
  • 47
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution
    • Deisenhofer, J. 198 I. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 20:2361.
    • (1981) Biochemistry , vol.20 , pp. 2361
    • Deisenhofer, J.1
  • 48
    • 0031473847 scopus 로고    scopus 로고
    • Swiss model and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. Swiss model and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18:2714.
    • (1997) Electrophoresis , vol.18 , pp. 2714
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.