A humanized anti-VEGF rabbit monoclonal antibody inhibits angiogenesis and blocks tumor growth in xenograft models

PLoS ONE

Volumn 5, Issue 2, 2010, Pages

  Yu, Yanlan ^a   Lee, Pierre ^b   Ke, Yaohuang ^b   Zhang, Yongke ^b   Yu, Qiu ^b   Lee, Jonathan ^b   Li, Mingzhen ^c   Song, Jialiang ^c   Chen, Jungang ^c   Dai, Jihong ^c   Couto, Fernando Jose Rebelo Do ^b   An, Zhiqiang ^b   Zhu, Weimin ^b   Yu, Guo Liang ^b  

^a ZHEJIANG UNIVERSITY   (China)

^b Epitomics Inc   (United States)

^c Yikang Biotechnology Company   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BEVACIZUMAB; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY HUMANIZED VASCULAR ENDOTHELIAL GROWTH FACTOR RABBIT; UNCLASSIFIED DRUG; VASCULOTROPIN; VASCULOTROPIN A; VASCULOTROPIN RECEPTOR 2;

ANGIOGENESIS; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BIOLOGICAL ACTIVITY; HUMAN; HUMAN CELL; LUNG CARCINOMA; LUNG SARCOMA; MOUSE; NONHUMAN; RHABDOMYOSARCOMA; TUMOR GROWTH; TUMOR XENOGRAFT; AMINO ACID SEQUENCE; ANIMAL; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; BAGG ALBINO MOUSE; CELL LINE; CELL PROLIFERATION; DRUG EFFECT; DRUG SCREENING; EPITOPE MAPPING; FEMALE; GENETICS; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; NEOPLASM; NEOVASCULARIZATION (PATHOLOGY); NUDE MOUSE; PATHOLOGY; PHOSPHORYLATION; RABBIT; SEQUENCE HOMOLOGY; TUMOR CELL LINE; TUMOR VOLUME; VASCULARIZATION;

MUS; ORYCTOLAGUS CUNICULUS;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; CELL LINE; CELL LINE, TUMOR; CELL PROLIFERATION; EPITOPE MAPPING; FEMALE; HUMANS; MICE; MICE, INBRED BALB C; MICE, NUDE; MOLECULAR SEQUENCE DATA; NEOPLASMS; NEOVASCULARIZATION, PATHOLOGIC; PHOSPHORYLATION; RABBITS; SEQUENCE HOMOLOGY, AMINO ACID; TUMOR BURDEN; VASCULAR ENDOTHELIAL GROWTH FACTOR A; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR-2; XENOGRAFT MODEL ANTITUMOR ASSAYS;

EID: 77949407821     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009072     Document Type: Article

References (56)

1. Reichert JM, Valge-Archer VE (2007) Development trends for monoclonal antibody cancer therapeutics. Nat Rev Drug Discov 6: 349-356.
2. Oldham RK, Dillman RO (2008) Monoclonal antibodies in cancer therapy: 25 years of progress. J Clin Oncol 26: 1774-1777.
3. Carter PJ (2006) Potent antibody therapeutics by design. Nat Rev Immunol 6: 343-357.
4. Lonberg N (2005) Human antibodies from transgenic animals. Nat Biotechnol 23: 1117-1125.
5. Jakobovits A, Amado RG, Yang X, Roskos L, Schwab G (2007) From XenoMouse technology to panitumumab, the first fully human antibody product from transgenic mice. Nat Biotechnol 25: 1134-1143.
6. Hoogenboom HR (2005) Selecting and screening recombinant antibody libraries. Nat Biotechnol 23: 1105-1116.
7. Lee CM, Iorno N, Sierro F, Christ D (2007) Selection of human antibody fragments by phage display. Nat Protoc 2: 3001-3008.
8. Groves DJ, Morris BA (2000) Veterinary sources of nonrodent monoclonal antibodies: interspecific and intraspecific hybridomas. Hybridoma 19: 201-214.
9. Zhu W, Yu G-L (2009) Rabbit hybridoma. In: An Z, ed. Therapeutic Monoclonal Antibodies: from Bench to Clinic.. Hoboken, New Jersey: John Wiley & Sons 889.
10. Weller A, Meek J, Adamson ED (1987) Preparation and properties of monoclonal and polyclonal antibodies to mouse epidermal growth factor (EGF) receptors: evidence for cryptic EGF receptors in embryonal carcinoma cells. Development 100: 351-363.
11. Rossi S, Laurino L, Furlanetto A, Chinellato S, Orvieto E, et al. (2005) Rabbit monoclonal antibodies: a comparative study between a novel category of immunoreagents and the corresponding mouse monoclonal antibodies. Am J Clin Pathol 124: 295-302.
12. Huang Z, Zhu W, Meng Y, Xia H (2006) Development of new rabbit monoclonal antibody to progesterone receptor (Clone SP2): no heat pretreatment but effective for paraffin section immunohistochemistry. Appl Immunohistochem Mol Morphol 14: 229-233.
13. Tao GZ, Nakamichi I, Ku NO, Wang J, Frolkis M, et al. (2006) Bispecific and human disease-related anti-keratin rabbit monoclonal antibodies. Exp Cell Res 312: 411-422.
14. Spieker-Polet H, Sethupathi P, Yam PC, Knight KL (1995) Rabbit monoclonal antibodies: generating a fusion partner to produce rabbit-rabbit hybridomas. Proc Natl Acad Sci U S A 92: 9348-9352.
15. Pytela R, Zhu W, Ke Y, Qian Q, Au HC (2008) Fusion partner for production of monoclonal rabbit antibodies. United States patent: 7,429, 487.
16. Ferrara N, Gerber HP, LeCouter J (2003) The biology of VEGF and its receptors. Nat Med 9: 669-676.
17. Ferrara N (2004) Vascular endothelial growth factor: basic science and clinical progress. Endocr Rev 25: 581-611.
18. Aguayo A, Estey E, Kantarjian H, Mansouri T, Gidel C, et al. (1999) Cellular vascular endothelial growth factor is a predictor of outcome in patients with acute myeloid leukemia. Blood 94: 3717-3721.
19. Seo Y, Baba H, Fukuda T, Takashima M, Sugimachi K (2000) High expression of vascular endothelial growth factor is associated with liver metastasis and a poor prognosis for patients with ductal pancreatic adenocarcinoma. Cancer 88: 2239-2245.
20. Couto FJRD, Hendricks KB, Wallace SE, Yu G-L (2004) Methods for antibody engineering. US patent: 7,462,697.
21. Couto FJRD (2005) Methods for humanizing rabbit monoclonal antibodies. WO patent. pp 016950.
22. Hwang WY, Foote J (2005) Immunogenicity of engineered antibodies. Methods 36: 3-10.
23. Dougher M, Terman BI (1999) Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization. Oncogene 18: 1619-1627.
24. Retter I, Althaus HH, Munch R, Muller W (2005) VBASE2, an integrative V gene database. Nucleic Acids Res 33: D671-674.
25. Padlan EA (1994) Anatomy of the antibody molecule. Mol Immunol 31: 169-217.
26. Popkov M, Mage RG, Alexander CB, Thundivalappil S, Barbas CF 3rd, et al. (2003) Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: the impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display. J Mol Biol 325: 325-335.
27. Velders MP, van Rhijn CM, Oskam E, Fleuren GJ, Warnaar SO, et al. (1998) The impact of antigen density and antibody affinity on antibody-dependent cellular cytotoxicity: relevance for immunotherapy of carcinomas. Br J Cancer 78: 478-483.
28. Zhu Z, Hattori K, Zhang H, Jimenez X, Ludwig DL, et al. (2003) Inhibition of human leukemia in an animal model with human antibodies directed against vascular endothelial growth factor receptor 2. Correlation between antibody affinity and biological activity. Leukemia 17: 604-611.
29. Lu D, Shen J, Vil MD, Zhang H, Jimenez X, et al. (2003) Tailoring in vitro selection for a picomolar affinity human antibody directed against vascular endothelial growth factor receptor 2 for enhanced neutralizing activity. J Biol Chem 278: 43496-43507.
30. Witte L, Hicklin DJ, Zhu Z, Pytowski B, Kotanides H, et al. (1998) Monoclonal antibodies targeting the VEGF receptor-2 (Flk1/KDR) as an anti-angiogenic therapeutic strategy. Cancer Metastasis Rev 17: 155-161.
31. Liang WC, Wu X, Peale FV, Lee CV, Meng YG, et al. (2006) Cross-species vascular endothelial growth factor (VEGF)-blocking antibodies completely inhibit the growth of human tumor xenografts and measure the contribution of stromal VEGF. J Biol Chem 281: 951-961.
32. Bystryn JC, Jacobsen JS, Liu P, Heaney-Kieras J (1982) Comparison of cell-surface human melanoma-associated antigens identified by rabbit and murine antibodies. Hybridoma 1: 465-472.
33. Wu TT, Johnson G, Kabat EA (1993) Length distribution of CDRH3 in antibodies. Proteins 16: 1-7.
34. Heidmann O, Rougeon F (1984) Immunoglobulin kappa light-chain diversity in rabbit is based on the 39 length heterogeneity of germ-line variable genes. Nature 311: 74-76.
35. Sitnikova T, Su C (1998) Coevolution of immunoglobulin heavy- and light-chain variable-region gene families. Mol Biol Evol 15: 617-625.
36. Shamblott MJ, Litman GW (1989) Genomic organization and sequences of immunoglobulin light chain genes in a primitive vertebrate suggest coevolution of immunoglobulin gene organization. EMBO J 8: 3733-3739.
37. Jones PT, Dear PH, Foote J, Neuberger MS, Winter G (1986) Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321: 522-525.
38. Roguska MA, Pedersen JT, Keddy CA, Henry AH, Searle SJ, et al. (1994) Humanization of murine monoclonal antibodies through variable domain resurfacing. Proc Natl Acad Sci U S A 91: 969-973.
39. Kettleborough CA, Saldanha J, Heath VJ, Morrison CJ, Bendig MM (1991) Humanization of a mouse monoclonal antibody by CDR-grafting: the importance of framework residues on loop conformation. Protein Eng 4: 773-783.
40. Huang X, Gottstein C, Brekken RA, Thorpe PE (1998) Expression of soluble VEGF receptor 2 and characterization of its binding by surface plasmon resonance. Biochem Biophys Res Commun 252: 643-648.
41. Sugihara T, Wadhwa R, Kaul SC, Mitsui Y (1998) A novel alternatively spliced form of murine vascular endothelial growth factor, VEGF 115. J Biol Chem 273: 3033-3038.
42. Gerber HP, Kowalski J, Sherman D, Eberhard DA, Ferrara N (2000) Complete inhibition of rhabdomyosarcoma xenograft growth and neovascularization requires blockade of both tumor and host vascular endothelial growth factor. Cancer Res 60: 6253-6258.
43. Miller KD, Chap LI, Holmes FA, Cobleigh MA, Marcom PK, et al. (2005) Randomized phase III trial of capecitabine compared with bevacizumab plus capecitabine in patients with previously treated metastatic breast cancer. J Clin Oncol 23: 792-799.
44. Miller K, Wang M, Gralow J, Dickler M, Cobleigh M, et al. (2007) Paclitaxel plus bevacizumab versus paclitaxel alone for metastatic breast cancer. N Engl J Med 357: 2666-2676.
45. Bongartz T, Sutton AJ, Sweeting MJ, Buchan I, Matteson EL, et al. (2006) Anti-TNF antibody therapy in rheumatoid arthritis and the risk of serious infections and malignancies: systematic review and meta-analysis of rare harmful effects in randomized controlled trials. JAMA 295: 2275-2285.
46. Zhu X, Wu S, Dahut WL, Parikh CR (2007) Risks of proteinuria and hypertension with bevacizumab, an antibody against vascular endothelial growth factor: systematic review and meta-analysis. Am J Kidney Dis 49: 186-193.
47. High K, Meng Y, Washabaugh MW, Zhao Q (2005) Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with fluorescence detection. Anal Biochem 347: 159-161.
48. Muller YA, Christinger HW, Keyt BA, de Vos AM (1997) The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding. Structure 5: 1325-1338.
49. Muller YA, Li B, Christinger HW, Wells JA, Cunningham BC, et al. (1997) Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc Natl Acad Sci U S A 94: 7192-7197.
50. Muller YA, Chen Y, Christinger HW, Li B, Cunningham BC, et al. (1998) VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface. Structure 6: 1153-1167.
51. Fuh G, Wu P, Liang WC, Ultsch M, Lee CV, et al. (2006) Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin Fab. J Biol Chem 281: 6625-6631.
52. Johnsson B, Lofas S, Lindquist G (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal Biochem 198: 268-277.
53. Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948.
54. Weidner N, Folkman J, Pozza F, Bevilacqua P, Allred EN, et al. (1992) Tumor angiogenesis: a new significant and independent prognostic indicator in early-stage breast carcinoma. J Natl Cancer Inst 84: 1875-1887.
55. Al-Lazikani B, Lesk AM, Chothia C (1997) Standard conformations for the canonical structures of immunoglobulins. J Mol Biol 273: 927-948.
56. Kabat EA, National Institutes of H, Columbia U (1991) Sequences of proteins of immunological interest. Bethesda, MD: U.S. Dept. of Health and Human Services, Public Health Service, National Institutes of Health.