Refined structure of an intact IgG2a monoclonal antibody

Biochemistry

Volumn 36, Issue 7, 1997, Pages 1581-1597

  Harris, Lisa J ^a   Larson, Steven B ^a   Hasel, Karl W ^b   McPherson, Alexander ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b QED BioScience   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; IMMUNOGLOBULIN G2A; MONOCLONAL ANTIBODY;

ANTIBODY COMBINING SITE; ANTIGEN BINDING; ARTICLE; CONFORMATIONAL TRANSITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; CARBOHYDRATE CONFORMATION; CRYSTALLOGRAPHY, X-RAY; DOGS; IMMUNOGLOBULIN FAB FRAGMENTS; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; IMMUNOGLOBULIN VARIABLE REGION; LYMPHOMA; MICE; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY;

MURINAE;

EID: 0031017896     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962514+     Document Type: Article

References (88)

1. Amzel, L. M., & Poljak, R. J. (1979) Three-dimensional structure of immunoglobulins, Annu. Rev. Biochem. 48, 961-997.
2. Akerström, B., & Björck, L. (1989) Protein L: an immunoglobulin light chain binding protein. Characterization of binding and physiological properties, J. Biol. Chem. 264, 19740-19746.
3. Alzari, P. M., Lascombe, M.-B., & Poljak, R. J. (1988) Three-dimensional structure of antibodies, Annu. Rev. Immunol. 6, 555-580.
4. Arevalo, J. H., Taussig, M. J., & Wilson, I. A. (1993) Molecular basis of cross-reactivity and the limits of antibody-antigen complementarity, Nature 365, 859-863.
5. Arevalo, J. H., Hassig, C. A., Stura, E. A., Sims, M. J., Taussig, M. J., & Wilson, I.A. (1994) Structural analysis of antibody specificity. Detailed comparison of five Fab'-steroid complexes, J. Mol. Biol. 241, 663-690.
6. Ban, N., Escobar, C., Hasel, K. W., Day, J., Greenwood, A., & McPherson, A. (1995) Structure of an anti-idiotypic Fab against feline peritonitis virus-neutralizing antibody and a comparison with the complexed Fab, FASEB J. 9, 107-114.
7. Bernstein, F. C., Koetzle, T. F., William, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanonchi, T., & Tasumi, M. (1977) The protein databank: a computer-based archival file for macromolecular structures, J. Mol. Biol. 112, 535-542.
8. Brekke, O. H., Michaelsen, T. E., & Sandlie, I. (1995) The structural requirements for complement activation by IgG: does it hinge on the hinge?, Immunol. Today 16, 85-90.
9. Brünger, A. T. (1991) Simulated annealing in crystallography, Annu. Rev. Phys. Chem. 42, 197-223.
10. Burmeister, W. P., Huber, A. H., & Bjorkman, P. J. (1994) Crystal structure of the complex of rat neonatal Fc receptor with Fc, Nature 372, 379-383.
11. Burton, D. R. (1990) Antibody: the flexible adapter molecule, Trends Biochem. Sci. 15, 64-69.
12. Burton, D. R., & Woof, J. M. (1992) Human antibody effector function, Adv. Immunol. 51, 1-84.
13. Chothia, C., Lesk, A. M., Tramontano, A., Levitt, M., Smith-Gill, S. J., Air, G., Sheriff, S., Padlan, E. A., Davies, D., Tulip, W. R., Colman, P. M., Spinelli, S., Alzari, P. M., & Poljak, R. J. (1989) Conformations of immunoglobulin hypervariable regions, Nature 342, 877-883.
14. Coco-Martin, J. M., Brunink, F., van der Velden-de Groot, T. A. M., & Beuvery, E. C. (1992) Analysis of glycoforms present in two mouse IgG2a monoclonal antibody preparations, J. Immunol. Methods 155, 241-248.
15. Colman, P. M. (1988) Structure of antibody-antigen complexes: implications for immune recognition, Adv. Immunol. 43, 99-132.
16. Connolly, M. L. (1983) Analytical molecular surface calculation, J. Appl. Crystallogr. 16, 548-558.
17. Corper, A. L., Sohi, M. K., Jefferis, R., Steinitz, M., Feinstein, A., Beale, D., Taussig, M. J., & Sutton, B. J. (1996) Structure of a human IgM rheumatoid factor complexed with its autoantigen IgG Fc, International Union of Crystallography XVII Congress and General Assembly, Seattle, WA, Aug 8-17.
18. Crowther, R. A. (1972) The fast rotation function, In The Molecular Replacement Method (Rossman, M. G., Ed.) pp 173-178, Gordon & Breach, New York.
19. Cruse, J. M., & Lewis, R. E. (1995) Illustrated Dictionary of Immunology, pp 197-198, 263, CRC Press, Boca Raton, FL.
20. Dangl, J. L., Wensel, T. G., Morrison, S. L., Stryer, L., Herzenberg, L. A., & Oi, V. T. (1988) Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies, EMBO J. 7, 1989-1994.
21. Davies, D. R., & Chacko, S. (1993) Antibody structure, Acc. Chem. Res. 26, 421-427.
22. Davies, D. R., Padlan, E. A., & Sheriff, S. (1990) Antibody-antigen complexes, Annu. Rev. Biochem. 59, 439-473.
23. Deisenhofer, J. (1981) 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, 2361-2370.
24. Derrick, J. P., & Wigley, D. B. (1992) Crystal structure of a streptococcal protein G domain bound to an Fab fragment. Nature 359, 752-754.
25. Duncan, A. R. & Winter, G. (1988) The binding site for CIq on IgG, Nature 332, 738-740.
26. Duncan, A. R., Woof, J. M., Partridge, L. J., Burton, D. R., & Winter, G. (1988) Localization of the binding site for the human high-affinity Fc receptor on IgG, Nature 332, 563-564.
27. Edmundson, A. B., Wood, M. K., Schiffer, M., Hardman, K. D., Ainsworth, C. F., Ely, K. R., & Deutsch, H. F. (1970) A crystallographic investigation of a human IgG immunoglobulin, J. Biol. Chem. 245, 2763-2764.
28. Edmundson, A. B, Guddat, L. W., & Anderson, K. N. (1993) Crystal structures of intact IgG antibodies, ImmunoMethods 3, 197-210.
29. Edmundson, A. B., Guddat, L. W., Shan, L., & Fan, Z.-C. (1994) Structural aspects of conformational changes in ligand binding by antibody fragments, Res. Imnumol. 145, 56-61.
30. 2 fragment and the intact immunoglobulin, Biochemistry 17, 820-823.
31. Evans, S. V. (1993) SETOR: Hardware lighted three-dimensional solid model representations of macromolecules, J. Mol. Graphics 11, 134-138.
32. Fitzgerald, P. M. D. (1988) MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. Appl. Crystallogr. 21, 273-276.
33. Furukawa, K., & Kobata, A. (1991) IgG galactosylation-its biological significance and pathology, Mol. Immunol. 28, 1333-1340.
34. Ghetie, V., & Ward, E. S. (1995) Genetic manipulation of antibodies: from variable domains to constant regions, in The Antibodies (Zanetti, M., & Capra, J. D., Eds.) pp 169-211, Harwood Academic, Australia and United States.
35. Guddat, L. W., Herron, J. N., & Edmundson, A. B. (1993) Three-dimensional structure of a human immunoglobulin with a hinge deletion, Proc. Natl. Acad. Sci. U.S.A. 90, 4271-4275.
36. Guddat, L. W., Shan, L., Anchin, J. M., Linthicum, D. S., & Edmundson, A. B. (1994) Local and transmitted conformational changes on complexation of an anti-sweetener Fab, J. Mol. Biol. 263, 247-274.
37. Hamlin, R., Cork, C., Howard, A., Nielsen, C., Vernon, W., Mathews, D., & Xuong, N.-H. (1981) Characteristics of a flat multiwire area detector for protein crystallography, J. Appl. Crystallogr. 14, 85-89.
38. Harris, L. J., Larson, S. B., Hasel, K. W., Day, J., Greenwood, A., & McPherson, A. (1992) The three-dimensional structure of an intact monoclonal antibody for canine lymphoma, Nature 360, J 369-372.
39. Harris, L. J., Skaletsky, E., & McPherson, A. (1995) Crystallization of intact monoclonal antibodies, Proteins 23, 285-289.
40. Huber, R., Deisenhofer, J., Colman, P. M., & Matsushima, M. (1976) Crystallographic structure studies of an IgG molecule and an Fc fragment, Nature 264, 415-420.
41. Jeglum, K. A. (1989) Chemotherapy of Canine Lymphoma, Proceedings of the Seventh ACVIM Forum, San Diego, CA, pp 922-925.
42. Jones, T. A. (1978) A graphics model building and refinement system for macromolecules, J. Appl. Crystallogr. 11, 268-272.
43. Jones, T. A., & Kjeldgaard, M. (1994) O-The Manual, Uppsala University Press, Uppsala.
44. Kabat, E. A., Wu, T. T., Perry, H. M., Gottesman, K. S., & Foeller, C. (1991) in Sequences of Proteins of Immunological Interest, 5th ed., U.S. Public Health Service, NIH, Washington, DC.
45. Kastern, W., Hoist, E., Nielsen, E., Sjöbring, U., & Björck, L. (1990) Protein L, a bacterial immunoglobulin-binding protein is a possible virulence factor, Infect. Immun. 58, 1217-1222.
46. 13C nuclear magnetic resonance spectroscopy, J. Mol. Biol. 236, 300-309.
47. Kleywegt, G. J., & Jones, T. A. (1995) Where freedom is given, liberties are taken, Structure 3, 535-540.
48. Kleywegt, G. J., & Jones, T. A. (1996) Good model-building and refinement practice, Methods Enzymol. (in press).
49. Krotkiewski, H., Grönberg, G., Krotkiewska, B., Nilsson, B., & Svensson, S. (1990) The carbohydrate structures of a mouse monoclonal IgG antibody OKT3, J. Biol. Chem. 254, 20195-20201.
50. Larson, S., Day, J., Greenwood, A., Skaletsky, E., & McPherson, A. (1991) Characterization of crystals of an intact monoclonal antibody for canine lymphoma, J. Mol. Biol. 222, 17-19.
51. Lascombe, M.-B., Alzari, P. M., Boulot, G., Saludjian, P., Tougard, P., Berek, C., Haba, S., Rosen, E. M., Nisonoff, A., & Poljak, R. J. (1989) Three dimensional structure of Fab R 19.9, a monoclonal murine antibody specific for the P-azobenzenearsonate group, Proc. Natl. Acad. Sci. U.S.A. 86, 607-611.
52. Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) Procheck-a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
53. Leslie, A. G. W. (1992) Recent changes to the MOSFLM package for processing film and image plate data, Joint CCP4 and ESF-EACBM Newsletters on Protein Crystallography, Vol. 26.
54. Lund, J., Winter, G., Jones, P. T., Pound, J. D., Tanaka, T., Walker, M. R., Artymiuk, P. J., Arata, Y., Burton, D. R., Jefferis, R., & Woof, J. M. (1991) Human FcγRI and FcγRII interact with distinct but overlapping sites on human IgG, J. Immunol. 147, 2657-2662.
55. Marquart, M., Deisenhofer, J., Huber, R., & Palm, W. (1980) Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution, J. Mol. Biol. 141, 369-391.
56. Matsuda, H., Nakamura, S., Ichikawa, Y., Kozai, K., Takano, R., Nose, M., Endo, S., Nishimura, Y., & Arata, Y. (1990) Proton nuclear magnetic resonance studies of the structure of the Fc fragment of human immunoglobulin G1: comparisons of native and recombinant proteins, Mol. Imimmol. 27, 571-579.
57. Mian, I. S., Bradwell, A. R., & Olson, A. J. (1991) Structure, function and properties of antibody binding sites, J. Mol. Biol. 217, 133-151.
58. H2 domain of chimeric human IgG1 anti-HLA-DR is necessary for C1q, FcγRI and FcyRIII binding, Immunology 86, 319-324.
59. Nicholls, A., Sharp, K., & Honig, B. (1991) Protein folding and association-insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins: Struct., Funct., Genet. 4, 281-296.
60. Padlan, E. A. (1994) Anatomy of the antibody molecule, Mol. Imimmol. 31, 169-217.
61. Padlan, E. A., Silverton, E. W., Sheriff, S., Cohen, G. H., Smith-Gill, S. J., & Davies, D. R. (1989) Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fablysozyme complex, Proc. Natl. Acad. Sci. U.S.A. 86, 5938-5942.
62. Palm, W., & Colman, P. M. (1974) Preliminary X-ray data from well-ordered crystals of a human immunoglobulin G molecule, J. Mol. Biol. 82, 587-588.
63. Patel, T. P., Parekh, R. B., Moellering, B. J., & Prior, C. P. (1992) Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody, Biochem. J. 285, 839-845.
64. Poljak, R. J., Amzel, L. M., Chen, B. L., Phizackerley, R. P., & Saul, F. (1974) The three dimensional structure of the Fab fragment of a human myeloma immunoglobulin at 2.0 angström resolution, Proc. Natl. Acad. Sci. U.S.A. 71, 3440-3444.
65. Raeder, R., & Boyle, M. D. P. (1993) Association of type II immunoglobulin G-binding protein expression and survival of group A streptococci in human blood, Infect. Immun. 61, 3696-3702.
66. Rosales, C., Jeglum, K. A., Obrocka, M., & Steplewski, Z. (1988) Cytolytic activity of murine anti-dog lymphoma monoclonal antibodies with canine effector cells and complement, Cell Imimmol. 115, 420-428.
67. Rothman, R. J., Warren, L., Vliegenthart, J. F. G., & Härd, K. J. (1989) Clonal analysis of the glycosylation of immunoglobulin G secreted by murine hybridomas. Biochemistry 28, 1377-1384.
68. Roux, K. H. (1984) Direct demonstration of multiple VH allotopes on rabbit Ig molecules: allotope characteristics and Fab arm rotational flexibility revealed by immunoelectron microscopy, Eur. J. Imimmol. 14, 459-464.
69. Sarmay, G., Lund, J., Rozsnayay, Z., Gergely, J., & Jefferis, R. (1992) Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of human Fc receptors, Mol. Imimmol. 29, 633.
70. HIII subgroup, J. Imimmol. 142, 2778-2783.
71. Satow, Y., Cohen, G. H., Padlan, E. A., & Davies, D. R. (1986) Phosphocholine binding immunoglobulin Fab McPC603, J. Mol. Biol. 190, 593-604.
72. Sauer-Eriksson, A. E., Kleywegt, G. J., Uhlen, M., & Jones, T. A. (1995) Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG, Structure 3, 265-278.
73. Schneider, W. P., Wensel, T. G., Stryer, L., & Oi, V. T. (1988) Genetically engineered immunoglobulins reveal structural features controlling segmental flexibility, Proc. Natl. Acad. Sci. U.S.A. 85, 2509-2513.
74. Sheriff, S. (1993a) Antibody-protein complexes, ImmunoMethods 3, 222-227.
75. Sheriff, S. (1993b) Some methods for examining the interactions between two molecules, ImmunoMethods 3, 191-196.
76. Sheriff, S., Silverton, E. W., Padlan, E. A., Cohen, G. H., Smith-Gill, S. J., Finzel, B. C., & Davies, D. R. (1987) Three-dimensional structure of an antibody-antigen complex, Proc. Natl. Acad. Sci. U.S.A. 84, 8075-8079.
77. Silverton, E. W., Navia, M. A., & Davies, D. R. (1977) Three-dimensional structure of an intact human immunoglobulin, Proc. Natl. Acad. Sci. U.S.A. 74, 5140-5144.
78. Stanfield, R. L., Takimoto-Kamimura, Rini, J. M., Profy, A. T., & Wilson, I. A. (1993) Major antigen-induced domain rearrangements in an antibody, Structure 1, 83-93.
79. Steplewski, Z., Jeglum, K. A., Rosales, C., & Weintraub, N. (1987) Canine lymphoma-associated antigens defined by murine monoclonal antibodies, Cancer Immunol. Immunother. 24, 197-201.
80. Stura, E. A., Satterthwait, A. C., Calvo, J. C., Stefanko, R. S., Langeveld, J. P., & Kaslow, D. C. (1994) Crystallization of an intact monoclonal antibody (4B7) against Plasmodium falciparum malaria with peptides from the Pfs25 protein antigen, Acta Crystallogr. D50, 556-562.
81. Suh, S. W., Bhat, T. N., Navia, M. A., Cohen, G. H., Rao, D. N., Rudikoff, S., & Davies, D. R. (1986) The galactan-binding immunoglobulin Fab J539: an X-ray diffraction study at 2.6 Å resolution, Proteins 1, 74-80.
82. Terry, W. D., Matthews, B. W., & Davies, D. R. (1968) Crystallographic studies of a human immunoglobulin, Nature 220, 239-241.
83. Tsuchiya, N., Endo, T., Matsuta, K., Yoshinoya, S., Aikawa, T., Kosuge, E., Takeuchi, F., Miyamoto, T., & Kobata, A. (1989) Effects of galactose depletion from oligosaccharide chains on immunological activities of human IgG, J. Rheumatol. 16, 285-290.
84. Wade, R. H., Taveau, J. C., & Lamy, J. N. (1989) Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G, J. Mol. Biol. 206, 349-356.
85. Wilson, I. A., & Stanfield, R. L. (1994) Antibody-antigen interactions: new structures and new conformational changes, Curr. Opin. Stuct. Biol. 4, 857-867.
86. Wilson, I. A., Rini, J. M., Fremont, D. H., Fieser, G. G., & Stura, E. A. (1991) X-ray crystallographic analyses of free and antigen-complexed Fab fragments to investigate structural basis of immune recognition, Methods Enzymol. 203, 153-176.
87. Wrigley, N. G., Brown, E. B., & Skehel, J. J. (1983) Electron microscopic evidence for the axial rotation and inter-domain flexibility of the Fab regions of immunoglobulin G, J. Mol. Biol. 169, 771-774.
88. Xuong, N.-H., Nielsen, C., Hamlin, R., & Anderson, D. (1985) Strategy for data collection from protein crystals using a multiwire counter detector diffractometer, J. Appl. Crystallogr. 18, 342-360.