Immuno-targeting the multifunctional CD38 using nanobody

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Li, Ting ^a   Qi, Shali ^b   Unger, Mandy ^c   Hou, Yun Nan ^a   Deng, Qi Wen ^a   Liu, Jun ^a   Lam, Connie M C ^b   Wang, Xian Wang ^d   Xin, Du ^e   Zhang, Peng ^f   Koch Nolte, Friedrich ^c   Hao, Quan ^b   Zhang, Hongmin ^g   Lee, Hon Cheung ^a   Zhao, Yong Juan ^a  

^a PEKING UNIVERSITY   (China)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

^c UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

^d YANGTZE UNIVERSITY   (China)

^e THE FIRST AFFILIATED HOSPITAL OF SHENZHEN UNIVERSITY   (China)

^f HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^g SOUTHERN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADP RIBOSYL CYCLASE/CYCLIC ADP RIBOSE HYDROLASE 1; CD38 PROTEIN, HUMAN; IMMUNOLOGICAL ANTINEOPLASTIC AGENT; MEMBRANE PROTEIN; NANOBODY; PROTEIN BINDING;

AMINO ACID SEQUENCE; ANTIBODY SPECIFICITY; BETA SHEET; CELL LINE; CHEMISTRY; DRUG SCREENING; HUMAN; IMMUNOLOGY; METABOLISM; MOLECULAR MODEL; MULTIPLE MYELOMA; PROTEIN DOMAIN; TUMOR CELL LINE; X RAY CRYSTALLOGRAPHY;

ADP-RIBOSYL CYCLASE 1; AMINO ACID SEQUENCE; ANTIBODY SPECIFICITY; ANTINEOPLASTIC AGENTS, IMMUNOLOGICAL; CELL LINE; CELL LINE, TUMOR; CRYSTALLOGRAPHY, X-RAY; DRUG SCREENING ASSAYS, ANTITUMOR; HUMANS; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MULTIPLE MYELOMA; PROTEIN BINDING; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; SINGLE-DOMAIN ANTIBODIES;

EID: 84973338633     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep27055     Document Type: Article

References (56)

1. Lee, H. C. Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization. J Biol Chem 287, 31633-31640, doi: R112.349464/jbc.R112.349464 (2012).
2. Lee, H. C. Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling. Sci China Life Sci 54, 699-711, doi: 10.1007/s11427-011-4197-3 (2011).
3. Zhao, Y. J., Lam, C. M. & Lee, H. C. The membrane-bound enzyme CD38 exists in two opposing orientations. Sci Signal 5, ra67, doi: 5/241/ra67/scisignal.2002700 (2012).
4. Dianzani, U. et al. Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120. Eur J Immunol 25, 1306-1311, doi: 10.1002/eji.1830250526 (1995).
5. Savarino, A. et al. Human CD38 interferes with HIV-1 fusion through a sequence homologous to the V3 loop of the viral envelope glycoprotein gp120. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 17, 461-463, doi: 10.1096/fj.02-0512fje (2003).
6. Deaglio, S. et al. Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member. J Immunol 160, 395-402 (1998).
7. Deaglio, S. et al. CD38/CD31 interactions activate genetic pathways leading to proliferation and migration in chronic lymphocytic leukemia cells. Molecular medicine 16, 87-91, doi: 10.2119/molmed.2009.00146 (2010).
8. Malavasi, F. et al. Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology. Physiological reviews 88, 841-886, doi: 10.1152/physrev.00035.2007 (2008).
9. Hoy, S. M. Carfilzomib Triple Combination Therapy: A Review in Relapsed Multiple Myeloma. Targeted oncology, doi: 10.1007/s11523-016-0428-7 (2016).
10. Stevenson, G. T. CD38 as a therapeutic target. Molecular medicine 12, 345-346, doi: 10.2119/2006-00082.Stevenson (2006).
11. Deaglio, S., Aydin, S., Vaisitti, T., Bergui, L. & Malavasi, F. CD38 at the junction between prognostic marker and therapeutic target. Trends in molecular medicine 14, 210-218, doi: 10.1016/j.molmed.2008.02.005 (2008).
12. Vaisitti, T. et al. Multiple metamorphoses of CD38 from prognostic marker to disease modifier to therapeutic target in chronic lymphocytic leukemia. Current topics in medicinal chemistry 13, 2955-2964 (2013).
13. Magarotto, V., Salvini, M., Bonello, F., Bringhen, S. & Palumbo, A. Strategy for the treatment of multiple myeloma utilizing monoclonal antibodies: A new era begins. Leukemia & lymphoma 57, 537-556, doi: 10.3109/10428194.2015.1102245 (2016).
14. Unciti-Broceta, J. D., Del Castillo, T., Soriano, M., Magez, S. & Garcia-Salcedo, J. A. Novel therapy based on camelid nanobodies. Therapeutic delivery 4, 1321-1336, doi: 10.4155/tde.13.87 (2013).
15. Muyldermans, S., Atarhouch, T., Saldanha, J., Barbosa, J. A. & Hamers, R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein engineering 7, 1129-1135 (1994).
16. Munshi, C. et al. Identification of the Enzymatic Active Site of CD38 by Site-directed Mutagenesis. Journal of Biological Chemistry 275, 21566-21571, doi: 10.1074/jbc.M909365199 (2000).
17. Zhao, Y. J., Zhang, H. M., Lam, C. M., Hao, Q. & Lee, H. C. Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose. J Biol Chem 286, 22170-22177, doi: M111.228379/jbc.M111.228379 (2011).
18. Liu, Q. et al. Crystal Structure of Human CD38 Extracellular Domain. Structure 13, 1331-1339, doi: http://dx.doi.org/10.1016/j.str.2005.05.012 (2005).
19. Schornack, S. et al. Protein mislocalization in plant cells using a GFP-binding chromobody. The Plant journal : for cell and molecular biology 60, 744-754, doi: 10.1111/j.1365-313X.2009.03982.x (2009).
20. Mehta, K. et al. Involvement of retinoic acid receptor-alpha-mediated signaling pathway in induction of CD38 cell-surface antigen. Blood 89, 3607-3614 (1997).
21. Prus, E. & Fibach, E. Retinoic acid induction of CD38 antigen expression on normal and leukemic human myeloid cells: relationship with cell differentiation. Leukemia & lymphoma 44, 691-698, doi: 10.1080/1042819031000060564 (2003).
22. Coetzee, L. M., Tay, S. S., Lawrie, D., Janossy, G. & Glencross, D. K. From research tool to routine test: CD38 monitoring in HIV patients. Cytometry. Part B, Clinical cytometry 76, 375-384, doi: 10.1002/cyto.b.20478 (2009).
23. Kreitman, R. J. Immunotoxins for targeted cancer therapy. The AAPS Journal 8, E532-E551, doi: 10.1208/aapsj080363 (2006).
24. Jiang, H. et al. Purification of clinical-grade disulfide stabilized antibody fragment variable - Pseudomonas exotoxin conjugate (dsFv-PE38) expressed in Escherichia coli. Appl Microbiol Biotechnol 97, 621-632, doi: 10.1007/s00253-012-4319-2 (2013).
25. Kreitman, R. J. et al. Complete remissions of adult T-cell leukemia with anti-CD25 recombinant immunotoxin LMB-2 and chemotherapy to block immunogenicity. Clinical Cancer Research, doi: 10.1158/1078-0432.ccr-15-1412 (2015).
26. Huarte, E. et al. Depletion of dendritic cells delays ovarian cancer progression by boosting antitumor immunity. Cancer research 68, 7684-7691, doi: 10.1158/0008-5472.CAN-08-1167 (2008).
27. Kubala, M. H., Kovtun, O., Alexandrov, K. & Collins, B. M. Structural and thermodynamic analysis of the GFP:GFP-nanobody complex. Protein science : a publication of the Protein Society 19, 2389-2401, doi: 10.1002/pro.519 (2010).
28. Liu, Z. et al. Elevated CD38 antigen expression on CD8+ T cells is a stronger marker for the risk of chronic HIV disease progression to AIDS and death in the Multicenter AIDS Cohort Study than CD4+ cell count, soluble immune activation markers, or combinations of HLA-DR and CD38 expression. Journal of acquired immune deficiency syndromes and human retrovirology : official publication of the International Retrovirology Association 16, 83-92 (1997).
29. Leo, R. et al. Multiparameter analyses of normal and malignant human plasma cells: CD38+ +, CD56+, CD54+, cIg+ is the common phenotype of myeloma cells. Annals of hematology 64, 132-139 (1992).
30. Lee, H. C. & Aarhus, R. Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADPribose. J Cell Sci 113 Pt 24, 4413-4420 (2000).
31. Calcraft, P. J. et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature 459, 596-600, doi: 10.1038/nature08030 (2009).
32. Kato, I. et al. CD38 disruption impairs glucose-induced increases in cyclic ADP-ribose, [Ca2+]i, and insulin secretion. J Biol Chem 274, 1869-1872 (1999).
33. Partida-Sanchez, S. et al. Regulation of dendritic cell trafficking by the ADP-ribosyl cyclase CD38: impact on the development of humoral immunity. Immunity 20, 279-291 (2004).
34. Jin, D. et al. CD38 is critical for social behaviour by regulating oxytocin secretion. Nature 446, 41-45, doi: 10.1038/nature05526 (2007).
35. Van Audenhove, I. et al. Mapping cytoskeletal protein function in cells by means of nanobodies. Cytoskeleton 70, 604-622, doi: 10.1002/cm.21122 (2013).
36. Rocchetti, A., Hawes, C. & Kriechbaumer, V. Fluorescent labelling of the actin cytoskeleton in plants using a cameloid antibody. Plant methods 10, 12, doi: 10.1186/1746-4811-10-12 (2014).
37. Platonova, E. et al. Single-molecule microscopy of molecules tagged with GFP or RFP derivatives in mammalian cells using nanobody binders. Methods 88, 89-97, doi: 10.1016/j.ymeth.2015.06.018 (2015).
38. de Weers, M. et al. Daratumumab, a novel therapeutic human CD38 monoclonal antibody, induces killing of multiple myeloma and other hematological tumors. J Immunol 186, 1840-1848, doi: jimmunol.1003032/jimmunol.1003032 (2011).
39. Deckert, J. et al. SAR650984, a novel humanized CD38-targeting antibody, demonstrates potent antitumor activity in models of multiple myeloma and other CD38+ hematologic malignancies. Clinical cancer research : an official journal of the American Association for Cancer Research 20, 4574-4583, doi: 10.1158/1078-0432.CCR-14-0695 (2014).
40. Goldmacher, V. S. et al. Anti-CD38-blocked ricin: an immunotoxin for the treatment of multiple myeloma. Blood 84, 3017-3025 (1994).
41. Bolognesi, A. et al. CD38 as a target of IB4 mAb carrying saporin-S6: design of an immunotoxin for ex vivo depletion of hematological CD38+ neoplasia. Journal of biological regulators and homeostatic agents 19, 145-152 (2005).
42. Gerdts, J., Brace, E. J., Sasaki, Y., DiAntonio, A. & Milbrandt, J. SARM1 activation triggers axon degeneration locally via NAD(+) destruction. Science 348, 453-457, doi: 10.1126/science.1258366 (2015).
43. Tran, M. et al. Production of unique immunotoxin cancer therapeutics in algal chloroplasts. Proceedings of the National Academy of Sciences of the United States of America 110, E15-22, doi: 10.1073/pnas.1214638110 (2013).
44. Spiess, C., Zhai, Q. T. & Carter, P. J. Alternative molecular formats and therapeutic applications for bispecific antibodies. Molecular Immunology 67, 95-106, doi: 10.1016/j.molimm.2015.01.003 (2015).
45. Cong, L. & Zhang, F. Genome engineering using CRISPR-Cas9 system. Methods in molecular biology 1239, 197-217, doi: 10.1007/978-1-4939-1862-1-10 (2015).
46. Zhang, H. et al. Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal. Journal of molecular biology 405, 1070-1078, doi: 10.1016/j.jmb.2010.11.044 (2011).
47. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276, 307-326, doi: 10.1016/S0076-6879(97)76066-X (1997).
48. Mccoy, A. J. et al. Phaser crystallographic software. J Appl Crystallogr 40, 658-674, doi: 10.1107/S0021889807021206 (2007).
49. Bailey, S. The Ccp4 Suite - Programs for Protein Crystallography. Acta Crystallogr D 50, 760-763 (1994).
50. Zhang, W. Z., Zhang, H. M., Zhang, T., Fan, H. F. & Hao, Q. Protein-complex structure completion using IPCAS (Iterative Protein Crystal structure Automatic Solution). Acta Crystallogr D 71, 1487-1492, doi: 10.1107/S1399004715008597 (2015).
51. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53, 240-255, doi: Doi 10.1107/S0907444996012255 (1997).
52. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr D 66, 486-501, doi: 10.1107/S0907444910007493 (2010).
53. Painter, J. & Merritt, E. A. TLSMD web server for the generation of multi-group TLS models. J Appl Crystallogr 39, 109-111, doi: 10.1107/S0021889805038987 (2006).
54. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D 66, 12-21, doi: 10.1107/S0907444909042073 (2010).
55. Graeff, R. M., Walseth, T. F., Fryxell, K., Branton, W. D. & Lee, H. C. Enzymatic synthesis and characterizations of cyclic GDP-ribose. A procedure for distinguishing enzymes with ADP-ribosyl cyclase activity. J Biol Chem 269, 30260-30267 (1994).
56. Graeff, R. M., Mehta, K. & Lee, H. C. GDP-ribosyl cyclase activity as a measure of CD38 induction by retinoic acid in HL-60 cells. Biochemical and biophysical research communications 205, 722-727, doi: 10.1006/bbrc.1994.2725 (1994).