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Mediators of Inflammation
Volume 2015, Article ID 460264, 11 pages
http://dx.doi.org/10.1155/2015/460264
Research Article

Construction, Expression, and Characterization of a Recombinant Immunotoxin Targeting EpCAM

1Department of Clinical Immunology, Xijing Hospital, Fourth Military Medical University, Xi’an 710032, China
2Department of Neurology, Chinese Navy General Hospital, Beijing 100048, China
3Department of Geriatric Gastroenterology, Chinese People’s Liberation Army General Hospital, Beijing 100853, China
4Department of Immunology, Fourth Military Medical University, Xi’an 710032, China

Received 17 October 2014; Accepted 4 December 2014

Academic Editor: Lijun Xin

Copyright © 2015 Minghua Lv et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. G. Jurcic, D. A. Scheinberg, and A. N. Houghton, “Monoclonal antibody therapy of cancer.,” Cancer chemotherapy and biological response modifiers, vol. 15, pp. 152–175, 1994. View at Google Scholar · View at Scopus
  2. G. A. Leget and M. S. Czuczman, “Use of rituximab, the new FDA-approved antibody,” Current Opinion in Oncology, vol. 10, no. 6, pp. 548–551, 1998. View at Publisher · View at Google Scholar · View at Scopus
  3. T. Yamaguchi and T. Takahashi, “Application of monoclonal antibody for cancer therapy,” Gan to Kagaku Ryoho, vol. 21, no. 2, pp. 157–162, 1994. View at Google Scholar
  4. B. E. Bejcek, D. Wang, E. Berven et al., “Development and characterization of three recombinant single chain antibody fragments (scFvs) directed against the CD19 antigen,” Cancer Research, vol. 55, no. 11, pp. 2346–2351, 1995. View at Google Scholar · View at Scopus
  5. D. Flieger, P. Kufer, I. Beier, T. Sauerbruch, and I. G. H. Schmidt-Wolf, “A bispecific single-chain antibody directed against EpCAM/CD3 in combination with the cytokines interferon α and interleukin-2 efficiently retargets T and CD3+CD56+ natural-killer-like T lymphocytes to EpCAM-expressing tumor cells,” Cancer Immunology Immunotherapy, vol. 49, no. 8, pp. 441–448, 2000. View at Publisher · View at Google Scholar · View at Scopus
  6. A. S. Wayne, R. J. Kreitman, H. W. Findley et al., “Anti-CD22 immunotoxin RFB4(dsFv)-PE38 (BL22) for CD22-positive hematologic malignancies of childhood: preclinical studies and phase I clinical trial,” Clinical Cancer Research, vol. 16, no. 6, pp. 1894–1903, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. R. J. Kreitman, M. S. Tallman, T. Robak et al., “Phase I trial of anti-CD22 recombinant immunotoxin moxetumomab pasudotox (CAT-8015 or HA22) in patients with hairy cell leukemia,” Journal of Clinical Oncology, vol. 30, no. 15, pp. 1822–1828, 2012. View at Publisher · View at Google Scholar · View at Scopus
  8. P. Piascik, “FDA approves fusion protein for treatment of lymphoma,” Journal of the American Pharmaceutical Association, vol. 39, no. 4, pp. 571–572, 1999. View at Google Scholar · View at Scopus
  9. U. Schnell, V. Cirulli, and B. N. G. Giepmans, “EpCAM: structure and function in health and disease,” Biochimica et Biophysica Acta, vol. 1828, no. 8, pp. 1989–2001, 2013. View at Publisher · View at Google Scholar · View at Scopus
  10. P. A. Baeuerle and O. Gires, “EpCAM (CD326) finding its role in cancer,” British Journal of Cancer, vol. 96, no. 3, pp. 417–423, 2007. View at Publisher · View at Google Scholar · View at Scopus
  11. P. Went, M. Vasei, L. Bubendorf et al., “Frequent high-level expression of the immunotherapeutic target Ep-CAM in colon, stomach, prostate and lung cancers,” British Journal of Cancer, vol. 94, no. 1, pp. 128–135, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. G. Riethmüller, E. Holz, G. Schlimok et al., “Monoclonal antibody therapy for resected Dukes' C colerectal cancer: seven-year outcome of a multicenter randomized trial,” Journal of Clinical Oncology, vol. 16, no. 5, pp. 1788–1794, 1998. View at Google Scholar · View at Scopus
  13. E. M. Kirchner, R. Gerhards, and R. Voigtmann, “Sequential immunochemotherapy and edrecolomab in the adjuvant therapy of breast cancer: Reduction of 17-1A-positive disseminated tumour cells,” Annals of Oncology, vol. 13, no. 7, pp. 1044–1048, 2002. View at Publisher · View at Google Scholar · View at Scopus
  14. M. Mack, G. Riethmuller, and P. Kufer, “A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 15, pp. 7021–7025, 1995. View at Publisher · View at Google Scholar · View at Scopus
  15. A. Burges, P. Wimberger, C. Kümper et al., “Effective relief of malignant ascites in patients with advanced ovarian cancer by a trifunctional anti-EpCAM x anti-CD3 antibody: a phase I/II study,” Clinical Cancer Research, vol. 13, no. 13, pp. 3899–3905, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. D. A. Vallera, B. Zhang, M. K. Gleason et al., “Heterodimeric bispecific single-chain variable-fragment antibodies against EpCAM and CD16 induce effective antibody-dependent cellular cytotoxicity against human carcinoma cells,” Cancer Biotherapy & Radiopharmaceuticals, vol. 28, no. 4, pp. 274–282, 2013. View at Publisher · View at Google Scholar · View at Scopus
  17. N. Shirasu, H. Yamada, H. Shibaguchi, and M. Kuroki, “Molecular characterization of a fully human chimeric T-cell antigen receptor for tumor-associated antigen EpCAM,” Journal of Biomedicine and Biotechnology, vol. 2012, Article ID 853879, 7 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  18. C. Di Paolo, J. Willuda, S. Kubetzko et al., “A recombinant immunotoxin derived from a humanized epithelial cell adhesion molecule-specific single-chain antibody fragment has potent and selective antitumor activity,” Clinical Cancer Research, vol. 9, no. 7, pp. 2837–2848, 2003. View at Google Scholar · View at Scopus
  19. M. Simon, N. Stefan, L. Borsig, A. Pleuckthun, and U. Zangemeister-Wittke, “Increasing the antitumor effect of an EpCAM-targeting fusion toxin by facile click PEgylation,” Molecular Cancer Therapeutics, vol. 13, no. 2, pp. 375–385, 2014. View at Publisher · View at Google Scholar · View at Scopus
  20. X. Xie, C. Y. Wang, Y. X. Cao et al., “Expression pattern of epithelial cell adhesion molecule on normal and malignant colon tissues,” World Journal of Gastroenterology, vol. 11, no. 3, pp. 344–347, 2005. View at Publisher · View at Google Scholar · View at Scopus
  21. P. A. Baeuerle and O. Gires, “EpCAM (CD326) finding its role in cancer,” British Journal of Cancer, vol. 96, no. 3, pp. 417–423, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. D. Seimetz, H. Lindhofer, and C. Bokemeyer, “Development and approval of the trifunctional antibody catumaxomab (anti-EpCAM×anti-CD3) as a targeted cancer immunotherapy,” Cancer Treatment Reviews, vol. 36, no. 6, pp. 458–467, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. K. Ogawa, S. Tanaka, S. Matsumura et al., “EpCAM-targeted therapy for human hepatocellular carcinoma,” Annals of Surgical Oncology, vol. 21, no. 4, pp. 1314–1322, 2014. View at Publisher · View at Google Scholar
  24. C. Bokemeyer, “Catumaxomab trifunctional anti-EpCAM antibody used to treat malignant ascites,” Expert Opinion on Biological Therapy, vol. 10, no. 8, pp. 1259–1269, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. A. Premsukh, J. M. Lavoie, J. Cizeau, J. Entwistle, and G. C. MacDonald, “Development of a GMP Phase III purification process for VB4-845, an immunotoxin expressed in E. coli using high cell density fermentation,” Protein Expression and Purification, vol. 78, no. 1, pp. 27–37, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. H. Zola and B. Swart, “The human leucocyte differentiation antigens (HLDA) workshops: the evolving role of antibodies in research, diagnosis and therapy,” Cell Research, vol. 15, no. 9, pp. 691–694, 2005. View at Publisher · View at Google Scholar · View at Scopus
  27. J. Posey, M. Khazaeli, and M. Saleh, “Phase I trial testing multiple doses of humanized monoclonal antibody (Mab) 3622W94,” ASCO Annual Meeting, vol. 17, p. 436, 1998. View at Google Scholar
  28. J. S. de Bono, A. W. Tolcher, A. Forero et al., “ING-1, a monoclonal antibody targeting Ep-CAM in patients with advanced adenocarcinomas,” Clinical Cancer Research, vol. 10, no. 22, pp. 7555–7565, 2004. View at Publisher · View at Google Scholar · View at Scopus
  29. S. Naundorf, S. Preithner, P. Mayer et al., “In vitro and in vivo activity of MT201, a fully human monoclonal antibody for pancarcinoma treatment,” International Journal of Cancer, vol. 100, no. 1, pp. 101–110, 2002. View at Publisher · View at Google Scholar · View at Scopus
  30. W. Xiang, P. Wimberger, T. Dreier et al., “Cytotoxic activity of novel human monoclonal antibody MT201 against primary ovarian tumor cells,” Journal of Cancer Research and Clinical Oncology, vol. 129, no. 6, pp. 341–348, 2003. View at Publisher · View at Google Scholar · View at Scopus
  31. N. Prang, S. Preithner, K. Brischwein et al., “Cellular and complement-dependent cytotoxicity of Ep-CAM-specific monoclonal antibody MT201 against breast cancer cell lines,” British Journal of Cancer, vol. 92, no. 2, pp. 342–349, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. U. C. Wargalla and R. A. Reisfeld, “Rate of internalization of an immunotoxin correlates with cytotoxic activity against human tumor cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 13, pp. 5146–5150, 1989. View at Publisher · View at Google Scholar · View at Scopus
  33. K. Yamamoto, H. Hamada, H. Shinkai, Y. Kohno, H. Koseki, and T. Aoe, “The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen-activated protein kinase signaling cascades,” Journal of Biological Chemistry, vol. 278, no. 36, pp. 34525–34532, 2003. View at Publisher · View at Google Scholar · View at Scopus
  34. M. Capitani and M. Sallese, “The KDEL receptor: new functions for an old protein,” FEBS Letters, vol. 583, no. 23, pp. 3863–3871, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. S. Song, J. Xue, K. Fan et al., “Preparation and characterization of fusion protein truncated Pseudomonas Exotoxin A (PE38KDEL) in Escherichia coli,” Protein Expression and Purification, vol. 44, no. 1, pp. 52–57, 2005. View at Publisher · View at Google Scholar · View at Scopus
  36. L. M. Thomas, P. J. Huntington, L. J. Mead, D. L. Wingate, B. A. Rogerson, and A. M. Lew, “A soluble recombinant fusion protein of the transmembrane envelop protein of equine infectious anaemia virus for ELISA,” Veterinary Microbiology, vol. 31, no. 2-3, pp. 127–137, 1992. View at Publisher · View at Google Scholar · View at Scopus
  37. Y.-Q. Luo, L.-H. Wang, Q. Yi, and B.-H. Jiao, “Expression of soluble, biologically active recombinant human tumstatin in Escherichia coli,” Clinical and Experimental Medicine, vol. 8, no. 1, pp. 37–42, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. H. Wang, J. Dai, B. Li et al., “Expression, purification, and characterization of an immunotoxin containing a humanized anti-CD25 single-chain fragment variable antibody fused to a modified truncated Pseudomonas exotoxin A,” Protein Expression and Purification, vol. 58, no. 1, pp. 140–147, 2008. View at Publisher · View at Google Scholar · View at Scopus