Molecular Basis of Recognition of Human Osteopontin by 23C3, a Potential Therapeutic Antibody for Treatment of Rheumatoid Arthritis

Journal of Molecular Biology

Volumn 382, Issue 4, 2008, Pages 835-842

  Du, Jiamu ^a,b   Hou, Sheng ^c   Zhong, Chen ^a   Lai, Zheng ^a   Yang, Hui ^a,b   Dai, Jianxin ^c   Zhang, Dapeng ^c   Wang, Hao ^c   Guo, Yajun ^c   Ding, Jianping ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c SECOND MILITARY MEDICAL UNIVERSITY   (China)

Author keywords

23C3; antibody structure; epitope; osteopontin; rheumatoid arthritis

Indexed keywords

EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 23C3; OSTEOPONTIN; UNCLASSIFIED DRUG;

ANTIGEN ANTIBODY REACTION; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DRUG STRUCTURE; HUMAN; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; RHEUMATOID ARTHRITIS;

MURINAE;

EID: 51249102953     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.07.075     Document Type: Article

References (36)

1. Boers M. Rheumatoid arthritis. Treatment of early disease. Rheum. Dis. Clin. North. Am. 27 (2001) 405-414
2. Holmdahl R., Bockermann R., Backlund J., and Yamada H. The molecular pathogenesis of collagen-induced arthritis in mice-a model for rheumatoid arthritis. Ageing Res. Rev. 1 (2002) 135-147
3. Salmon M., and Gaston J.S. The role of T-lymphocytes in rheumatoid arthritis. Br. Med. Bull. 51 (1995) 332-345
4. Genovese M.C., Bathon J.M., Martin R.W., Fleischmann R.M., Tesser J.R., Schiff M.H., et al. Etanercept versus methotrexate in patients with early rheumatoid arthritis: two-year radiographic and clinical outcomes. Arthritis Rheum. 46 (2002) 1443-1450
5. Lipsky P.E., van der Heijde D.M., St Clair E.W., Furst D.E., Breedveld F.C., Kalden J.R., et al. Infliximab and methotrexate in the treatment of rheumatoid arthritis. Anti-Tumor Necrosis Factor Trial in Rheumatoid Arthritis with Concomitant Therapy Study Group. N. Engl. J. Med. 343 (2000) 1594-1602
6. Campion G.V., Lebsack M.E., Lookabaugh J., Gordon G., and Catalano M. Dose-range and dose-frequency study of recombinant human interleukin-1 receptor antagonist in patients with rheumatoid arthritis. The IL-1Ra Arthritis Study Group. Arthritis Rheum. 39 (1996) 1092-1101
7. Denhardt D.T., Noda M., O'Regan A.W., Pavlin D., and Berman J.S. Osteopontin as a means to cope with environmental insults: regulation of inflammation, tissue remodeling, and cell survival. J. Clin. Invest. 107 (2001) 1055-1061
8. 3 potentiate bone resorption. J. Biol. Chem. 268 (1993) 9901-9907
9. 5. J. Biol. Chem. 270 (1995) 26232-26238
10. 1 and potential roles for this integrin-ligand interaction in kidney morphogenesis. Mol. Biol. Cell 9 (1998) 1425-1435
11. Yokosaki Y., Matsuura N., Sasaki T., Murakami I., Schneider H., Higashiyama S., et al. The integrin a9b1 binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin. J. Biol. Chem. 274 (1999) 36328-36334
12. 1 integrin-osteopontin interaction. Exp. Cell Res. 258 (2000) 342-351
13. 4 integrins. FEBS Lett. 503 (2001) 75-79
14. 1-containing integrins to permit cells to bind to osteopontin independently of arginine-glycine-aspartic acid, thereby stimulating cell motility and chemotaxis. Cancer Res. 59 (1999) 219-226
15. Denhardt D.T., and Guo X. Osteopontin: a protein with diverse functions. FASEB J. 7 (1993) 1475-1482
16. Ashkar S., Weber G.F., Panoutsakopoulou V., Sanchirico M.E., Jansson M., Zawaideh S., et al. Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. Science 287 (2000) 860-864
17. Xanthou G., Alissafi T., Semitekolou M., Simoes D.C., Economidou E., Gaga M., et al. Osteopontin has a crucial role in allergic airway disease through regulation of dendritic cell subsets. Nat. Med. 13 (2007) 570-578
18. Diao H., Kon S., Iwabuchi K., Kimura C., Morimoto J., Ito D., et al. Osteopontin as a mediator of NKT cell function in T cell-mediated liver diseases. Immunity 21 (2004) 539-550
19. Burdo T.H., Wood M.R., and Fox H.S. Osteopontin prevents monocyte recirculation and apoptosis. J. Leukoc. Biol. 81 (2007) 1504-1511
20. Zhu B., Suzuki K., Goldberg H.A., Rittling S.R., Denhardt D.T., McCulloch C.A., and Sodek J. Osteopontin modulates CD44-dependent chemotaxis of peritoneal macrophages through G-protein-coupled receptors: evidence of a role for an intracellular form of osteopontin. J. Cell. Physiol. 198 (2004) 155-167
21. Xu G., Nie H., Li N., Zheng W., Zhang D., Feng G., et al. Role of osteopontin in amplification and perpetuation of rheumatoid synovitis. J. Clin. Invest. 115 (2005) 1060-1067
22. Petrow P.K., Hummel K.M., Schedel J., Franz J.K., Klein C.L., Muller-Ladner U., et al. Expression of osteopontin messenger RNA and protein in rheumatoid arthritis: effects of osteopontin on the release of collagenase 1 from articular chondrocytes and synovial fibroblasts. Arthritis Rheum. 43 (2000) 1597-1605
23. Yamamoto N., Nakashima T., Torikai M., Naruse T., Morimoto J., Kon S., et al. Successful treatment of collagen-induced arthritis in non-human primates by chimeric anti-osteopontin antibody. Int. Immunopharmacol. 7 (2007) 1460-1470
24. Yamamoto N., Sakai F., Kon S., Morimoto J., Kimura C., Yamazaki H., et al. Essential role of the cryptic epitope SLAYGLR within osteopontin in a murine model of rheumatoid arthritis. J. Clin. Invest. 112 (2003) 181-188
25. Fan K., Dai J., Wang H., Wei H., Cao Z., Hou S., et al. Treatment of collagen-induced arthritis with an anti-osteopontin monoclonal antibody through promotion of apoptosis of both murine and human activated T cells. Arthritis Rheum. 58 (2008) 2041-2052
26. Stanfield R.L., Zemla A., Wilson I.A., and Rupp B. Antibody elbow angles are influenced by their light chain class. J. Mol. Biol. 357 (2006) 1566-1574
27. Al-Lazikani B., Lesk A.M., and Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273 (1997) 927-948
28. Wu T.T., Johnson G., and Kabat E.A. Length distribution of CDRH3 in antibodies. Proteins 16 (1993) 1-7
29. Bell C.H., Pantophlet R., Schiefner A., Cavacini L.A., Stanfield R.L., Burton D.R., and Wilson I.A. Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization. J. Mol. Biol. 375 (2008) 969-978
30. Stanfield R.L., Fieser T.M., Lerner R.A., and Wilson I.A. Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å. Science 248 (1990) 712-719
31. Wallick S.C., Kabat E.A., and Morrison S.L. Glycosylation of a VH residue of a monoclonal antibody against alpha (1-6) dextran increases its affinity for antigen. J. Exp. Med. 168 (1988) 1099-1109
32. Wilson I.A., and Stanfield R.L. Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4 (1994) 857-867
33. Wilson I.A., Stanfield R.L., Rini J.M., Arevalo J.H., Schulze-Gahmen U., Fremont D.H., and Stura E.A. Structural aspects of antibodies and antibody-antigen complexes. Ciba Found. Symp. 159 (1991) 13-28
34. Stanfield R.L., and Wilson I.A. Protein-peptide interactions. Curr. Opin. Struct. Biol. 5 (1995) 103-113
35. Lawrence M.C., and Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234 (1993) 946-950
36. Cardoso R.M., Brunel F.M., Ferguson S., Zwick M., Burton D.R., Dawson P.E., and Wilson I.A. Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10. J. Mol. Biol. 365 (2007) 1533-1544