메뉴 건너뛰기




Volumn 284, Issue 1, 1998, Pages 85-99

Crystal structures of a rat anti-CD52 (CAMPATH-1) therapeutic antibody Fab fragment and its humanized counterpart

Author keywords

Antibody humanization; CD52; Molecular replacement; Protein crystallography; Therapeutic antibodies

Indexed keywords

ALEMTUZUMAB; DIMER; IMMUNOGLOBULIN F(AB) FRAGMENT;

EID: 0032553334     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2157     Document Type: Article
Times cited : (30)

References (65)
  • 1
    • 0025119206 scopus 로고
    • Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: The role of somatic mutation and heavy/light chain pairing in the maturation of an immune response
    • Alzari P. M. ., Spinelli S., Mariuzza R. A., Boulot G., Poljak R. A., Jarvis J. M., Milstein C. Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: the role of somatic mutation and heavy/light chain pairing in the maturation of an immune response. EMBO J. 9:1990;3807-3814.
    • (1990) EMBO J. , vol.9 , pp. 3807-3814
    • Alzari, P.M.1    Spinelli, S.2    Mariuzza, R.A.3    Boulot, G.4    Poljak, R.A.5    Jarvis, J.M.6    Milstein, C.7
  • 3
    • 0023691376 scopus 로고
    • Importance of antigen specificity for complement mediated lysis by monoclonal antibodies
    • Bindon C. I., Hale G., Waldmann H. Importance of antigen specificity for complement mediated lysis by monoclonal antibodies. Eur. J. Immunol. 18:1988;1507-1514.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 1507-1514
    • Bindon, C.I.1    Hale, G.2    Waldmann, H.3
  • 4
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new strategy based on Patterson correlation refinement
    • Brunger A. T. Extension of molecular replacement: a new strategy based on Patterson correlation refinement. Acta Crystallog. sect. A. 46:1990;46-57.
    • (1990) Acta Crystallog. Sect. A , vol.46 , pp. 46-57
    • Brunger, A.T.1
  • 6
    • 0026597444 scopus 로고
    • Free R -value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger A. T. Free R -value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992b;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 9
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C., Lesk A. M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196:1987;901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 15
    • 0026518375 scopus 로고
    • Humanized monoclonal antibody CAMPATH-1H: Myeloma cell expression of genomic constructs, nucleotide sequence of cDNA constructs and comparison of effector mechanisms of myeloma and Chinese hamster ovary cell derived material
    • Crowe J. S., Hall V. S., Smith M. A., Cooper H. J., Tite J. P. Humanized monoclonal antibody CAMPATH-1H: myeloma cell expression of genomic constructs, nucleotide sequence of cDNA constructs and comparison of effector mechanisms of myeloma and Chinese hamster ovary cell derived material. Clin. Expt. Immunol. 87:1992;105-110.
    • (1992) Clin. Expt. Immunol. , vol.87 , pp. 105-110
    • Crowe, J.S.1    Hall, V.S.2    Smith, M.A.3    Cooper, H.J.4    Tite, J.P.5
  • 17
    • 0026802451 scopus 로고
    • Crystal structure of a streptococcal protein G domain bound to an Fab fragment
    • Derrick J. P., Wigley D. B. Crystal structure of a streptococcal protein G domain bound to an Fab fragment. Nature. 359:1992;752-754.
    • (1992) Nature , vol.359 , pp. 752-754
    • Derrick, J.P.1    Wigley, D.B.2
  • 18
    • 0024566393 scopus 로고
    • Effects of CAMPATH-1 antibodies in vivo in patients with lymphoid malignancies: Influence of antibody isotype
    • Dyer M. J. S., Hale G., Hayhoe F. G. J., Waldmann H. Effects of CAMPATH-1 antibodies in vivo in patients with lymphoid malignancies: influence of antibody isotype. Blood. 73:1989;1431-1439.
    • (1989) Blood , vol.73 , pp. 1431-1439
    • Dyer, M.J.S.1    Hale, G.2    Hayhoe, F.G.J.3    Waldmann, H.4
  • 19
    • 0027467623 scopus 로고
    • X-ray structures of the antigen-binding domains from 3 variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modelling
    • Eigenbrot C., Randal M., Presta L., Carter P., Kossiakoff A. A. X-ray structures of the antigen-binding domains from 3 variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modelling. J. Mol. Biol. 229:1993;969-995.
    • (1993) J. Mol. Biol. , vol.229 , pp. 969-995
    • Eigenbrot, C.1    Randal, M.2    Presta, L.3    Carter, P.4    Kossiakoff, A.A.5
  • 20
    • 0027955736 scopus 로고
    • X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody-structural indications of the key role of VH residues 59 to 65
    • Eigenbrot C., Gonzalez T., Mayeda J., Carter P., Werther W., Hotaling T., Fox J., Kessler J. X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody-structural indications of the key role of VH residues 59 to 65. Proteins: Struct. Funct. Genet. 18:1994;49-62.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 49-62
    • Eigenbrot, C.1    Gonzalez, T.2    Mayeda, J.3    Carter, P.4    Werther, W.5    Hotaling, T.6    Fox, J.7    Kessler, J.8
  • 21
    • 0016804680 scopus 로고
    • The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein/REI refined at 2.0 Å resolution
    • Epp O., Lattmann E. E., Colman P., Fehlhammer H., Bode W., Schiffer M., Huber R., Palm W. The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein/REI refined at 2.0 Å resolution. Biochemistry. 14:1975;4943-4952.
    • (1975) Biochemistry , vol.14 , pp. 4943-4952
    • Epp, O.1    Lattmann, E.E.2    Colman, P.3    Fehlhammer, H.4    Bode, W.5    Schiffer, M.6    Huber, R.7    Palm, W.8
  • 22
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosylphosphatidylinositol structures
    • Ferguson M. A. J., Williams A. F. Cell-surface anchoring of proteins via glycosylphosphatidylinositol structures. Annu. Rev. Biochem. 57:1988;285-320.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 25
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J., Winter G. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224:1992;487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 26
    • 0029583823 scopus 로고
    • Synthetic peptide mimotope of the CAMPATH-1 (CD52) antigen, a small glycosylphosphatidylinositol-anchored glycoprotein
    • Hale G. Synthetic peptide mimotope of the CAMPATH-1 (CD52) antigen, a small glycosylphosphatidylinositol-anchored glycoprotein. Immunotechnology. 1:1995;175-187.
    • (1995) Immunotechnology , vol.1 , pp. 175-187
    • Hale, G.1
  • 27
    • 0028791093 scopus 로고
    • Clinical trials with CAMPATH-1 and other monoclonal antibodies
    • Hale G., Phillips J. M. Clinical trials with CAMPATH-1 and other monoclonal antibodies. Biochem. Soc. Trans. 23:1995;1057-1063.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 1057-1063
    • Hale, G.1    Phillips, J.M.2
  • 28
    • 0021813140 scopus 로고
    • Reactivity of rat monoclonal antibody CAMPATH-1 with human leukaemia cell and its possible application for autologous bone marrow transplantation
    • Hale G., Swirsky D., Waldmann H., Chan L. C. Reactivity of rat monoclonal antibody CAMPATH-1 with human leukaemia cell and its possible application for autologous bone marrow transplantation. Brit. J. Haematol. 60:1985;41-48.
    • (1985) Brit. J. Haematol. , vol.60 , pp. 41-48
    • Hale, G.1    Swirsky, D.2    Waldmann, H.3    Chan, L.C.4
  • 29
    • 0023924847 scopus 로고
    • T cell depletion with CAMPATH-1 in allogeneic bone marrow transplantation
    • Hale G., Cobbold S., Waldmann H. T cell depletion with CAMPATH-1 in allogeneic bone marrow transplantation. Transplantation. 45:1988a;753-759.
    • (1988) Transplantation , vol.45 , pp. 753-759
    • Hale, G.1    Cobbold, S.2    Waldmann, H.3
  • 31
    • 0028556362 scopus 로고
    • Comparison of crystal structures of two homologous proteins: Structural origin of altered domain interactions in immunoglobulin light-chain dimers
    • Huang D. B., Chang C. H., Ainsworth C., Brunger A. T., Eulitz M., Solomon A., Stevens F. J., Schiffer M. Comparison of crystal structures of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers. Biochemistry. 33:1994;14848-14857.
    • (1994) Biochemistry , vol.33 , pp. 14848-14857
    • Huang, D.B.1    Chang, C.H.2    Ainsworth, C.3    Brunger, A.T.4    Eulitz, M.5    Solomon, A.6    Stevens, F.J.7    Schiffer, M.8
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 256:1975;495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 39
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. M. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.M.1
  • 41
    • 0025964038 scopus 로고
    • Structure, function and properties of antibody binding sites
    • Mian I. S., Bradwell A. R., Olson A. J. Structure, function and properties of antibody binding sites. J. Mol. Biol. 217:1991;133-151.
    • (1991) J. Mol. Biol. , vol.217 , pp. 133-151
    • Mian, I.S.1    Bradwell, A.R.2    Olson, A.J.3
  • 42
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hypervariable region in the VH domain of immunoglobulins
    • Morea V., Tramontano A., Rustici M., Chothia C., Lesk A. M. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J. Mol. Biol. 275:1998;269-294.
    • (1998) J. Mol. Biol. , vol.275 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 43
    • 0028346432 scopus 로고
    • Preliminary evidence from magnetic resonance imaging for reduction in disease activity after lymphocyte depletion in multiple sclerosis
    • Moreau T., Thorpe J., Miller D., Mosele I., Hale G., Waldmann H., Clayton D., Wing M., Scolding N., Compston A. Preliminary evidence from magnetic resonance imaging for reduction in disease activity after lymphocyte depletion in multiple sclerosis. Lancet. 344:1994;298-301.
    • (1994) Lancet , vol.344 , pp. 298-301
    • Moreau, T.1    Thorpe, J.2    Miller, D.3    Mosele, I.4    Hale, G.5    Waldmann, H.6    Clayton, D.7    Wing, M.8    Scolding, N.9    Compston, A.10
  • 44
    • 84920325457 scopus 로고
    • AMORE: An automated package for molecular replacement
    • Navaza J. AMORE: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 45
    • 84986486656 scopus 로고
    • GRASP: A program for the graphical representation and analysis of surface properties
    • Nicholl A., Honig B. J. GRASP: a program for the graphical representation and analysis of surface properties. J. Comput. Chem. 12:1991;435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholl, A.1    Honig, B.J.2
  • 48
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 50
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini J. M., Schultze-Garmen U., Wilson I. A. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science. 255:1992;959-969.
    • (1992) Science , vol.255 , pp. 959-969
    • Rini, J.M.1    Schultze-Garmen, U.2    Wilson, I.A.3
  • 51
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McP603: An X-ray diffraction study at 2.7 Å
    • Satow Y., Cohen G. H., Padlan E. A., Davies D. R. Phosphocholine binding immunoglobulin Fab McP603: an X-ray diffraction study at 2.7 Å J. Mol. Biol. 190:1986;539-604.
    • (1986) J. Mol. Biol. , vol.190 , pp. 539-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 52
    • 0017855552 scopus 로고
    • Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin NEW at 2.0 Å resolution
    • Saul F. A., Amzel L. M., Poljak R. J. Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin NEW at 2.0 Å resolution. J. Biol. Chem. 253:1978;585-597.
    • (1978) J. Biol. Chem. , vol.253 , pp. 585-597
    • Saul, F.A.1    Amzel, L.M.2    Poljak, R.J.3
  • 53
    • 0022429703 scopus 로고
    • Formation of an infinite β-sheet arrangement dominates the crystallization behaviour of λ-type antibody light chains
    • Schiffer M., Chang C.-H., Stevens F. J. Formation of an infinite β-sheet arrangement dominates the crystallization behaviour of λ-type antibody light chains. J. Mol. Biol. 186:1985;475-478.
    • (1985) J. Mol. Biol. , vol.186 , pp. 475-478
    • Schiffer, M.1    Chang, C.-H.2    Stevens, F.J.3
  • 55
    • 0030577371 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 in antibodies
    • Shirai H., Kidera A., Nakamura H. Structural classification of CDR-H3 in antibodies. FEBS Letters. 399:1996;1-8.
    • (1996) FEBS Letters , vol.399 , pp. 1-8
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 56
    • 0010348361 scopus 로고
    • The effect of CAMPATH-1H monoclonal-antibody therapy on the T-cell receptor (TCR) repertoire of patients with rheumatoid arthritis
    • Sundy J. S., Denning S. M., Jacobs M. R., St. Clair E. W. The effect of CAMPATH-1H monoclonal-antibody therapy on the T-cell receptor (TCR) repertoire of patients with rheumatoid arthritis. Arthrit. Rheumat. 36:1993;S40.
    • (1993) Arthrit. Rheumat. , vol.36 , pp. 40
    • Sundy, J.S.1    Denning, S.M.2    Jacobs, M.R.3    St. Clair, E.W.4
  • 57
    • 0027109248 scopus 로고
    • Strategies in the crystallization of glycoproteins and protein complexes
    • Stura E. A., Nemerow G. R., Wilson I. A. Strategies in the crystallization of glycoproteins and protein complexes. J. Cryst. Growth. 122:1992;273-285.
    • (1992) J. Cryst. Growth , vol.122 , pp. 273-285
    • Stura, E.A.1    Nemerow, G.R.2    Wilson, I.A.3
  • 59
    • 0026451628 scopus 로고
    • Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences
    • Turnell W. G., Finch J. T. Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. J. Mol. Biol. 227:1992;1205-1223.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1205-1223
    • Turnell, W.G.1    Finch, J.T.2
  • 60
    • 0010304849 scopus 로고
    • Single-dose subcutaneous CAMPATH-1H in the treatment of rheumatoid-arthritis
    • Watts R. A., Manna V., Hazleman B. L. Single-dose subcutaneous CAMPATH-1H in the treatment of rheumatoid-arthritis. Brit. J. Rheumatol. 32:1993;21.
    • (1993) Brit. J. Rheumatol. , vol.32 , pp. 21
    • Watts, R.A.1    Manna, V.2    Hazleman, B.L.3
  • 62
    • 0025878925 scopus 로고
    • Characterization of the CAMPATH-1 (CD52) antigen: Biochemical analysis and cDNA cloning reveal an unusually small peptide backbone
    • Xia M., Tone M., Packman L., Hale G., Waldmann H. Characterization of the CAMPATH-1 (CD52) antigen: biochemical analysis and cDNA cloning reveal an unusually small peptide backbone. Eur. J. Immunol. 21:1991;1677-1684.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1677-1684
    • Xia, M.1    Tone, M.2    Packman, L.3    Hale, G.4    Waldmann, H.5
  • 63
    • 0027194472 scopus 로고
    • Structure of the CAMPATH-1 antigen, a glycosylphosphatidylinositol-anchored glycoprotein which is an exceptionally good target for complement lysis
    • Xia M., Hale G., Lifely M. R., Ferguson M. A. J., Campbell D., Packman L., Waldmann H. Structure of the CAMPATH-1 antigen, a glycosylphosphatidylinositol-anchored glycoprotein which is an exceptionally good target for complement lysis. Biochem. J. 293:1993a;633-640.
    • (1993) Biochem. J. , vol.293 , pp. 633-640
    • Xia, M.1    Hale, G.2    Lifely, M.R.3    Ferguson, M.A.J.4    Campbell, D.5    Packman, L.6    Waldmann, H.7
  • 64
    • 0027283918 scopus 로고
    • Efficient complement-mediated lysis of cells containing the CAMPATH-1 (CDw52) Antigen
    • Xia M.-Q., Hale G., Waldmann H. Efficient complement-mediated lysis of cells containing the CAMPATH-1 (CDw52) Antigen. Mol. Immunol. 30:1993b;1089-1096.
    • (1993) Mol. Immunol. , vol.30 , pp. 1089-1096
    • Xia, M.-Q.1    Hale, G.2    Waldmann, H.3
  • 65
    • 85030343373 scopus 로고
    • The refinement and structure of MCG Bence-Jones dimer at 2.3 Ångstroms resolution
    • Xu Z. B., Schiffer M. The refinement and structure of MCG Bence-Jones dimer at 2.3 Ångstroms resolution. Am. Cryst. Assoc. 16:1988;74.
    • (1988) Am. Cryst. Assoc. , vol.16 , pp. 74
    • Xu, Z.B.1    Schiffer, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.