Metal-dependent amyloid β-degrading catalytic antibody construct

Journal of Biotechnology

Volumn 180, Issue , 2014, Pages 17-22

  Nishiyama, Yasuhiro ^a   Taguchi, Hiroaki ^a   Hara, Mariko ^a   Planque, Stephanie A ^a   Mitsuda, Yukie ^a   Paul, Sudhir ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

Alzheimer disease; Amyloid clearance; Catalytic antibody light chain; Metal activation

Indexed keywords

AMINO ACIDS; CHAINS; EMISSION SPECTROSCOPY; GLYCOPROTEINS; METALS; ZINC;

1 ,10-PHENANTHROLINE; ALZHEIMER DISEASE; CATALYTIC ANTIBODIES; CONFORMATIONAL TRANSITIONS; FLUORESCENCE EMISSION SPECTROSCOPY; HYDROLYTIC ACTIVITIES; IMMUNOGLOBULIN LIGHT CHAINS; NUCLEOPHILIC ATTACK;

ANTIBODIES;

AMYLOID BETA PROTEIN; CATALYTIC ANTIBODY; CHELATING AGENT; COPPER; EDETIC ACID; ZINC;

ALZHEIMER DISEASE; CHEMISTRY; DRUG EFFECTS; HUMAN; HYDROLYSIS; METABOLISM;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANTIBODIES, CATALYTIC; CHELATING AGENTS; COPPER; EDETIC ACID; HUMANS; HYDROLYSIS; ZINC;

EID: 84898678066     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.03.026     Document Type: Article

References (49)

1. Auld D.S. Removal and replacement of metal ions in metallopeptidases. Methods Enzymol. 1995, 248:228-242.
2. Baranova S.V., Buneva V.N., Kharitonova M.A., Sizyakina L.P., Calmels C., Andreola M.L., Parissi V., Zakharova O.D., Nevinsky G.A. HIV-1 integrase-hydrolyzing IgM antibodies from sera of HIV-infected patients. Int. Immunol. 2010, 22:671-680.
3. Bard F., Cannon C., Barbour R., Burke R.L., Games D., Grajeda H., Guido T., Hu K., Huang J., Johnson-Wood K., Khan K., Kholodenko D., Lee M., Lieberburg I., Motter R., Nguyen M., Soriano F., Vasquez N., Weiss K., Welch B., Seubert P., Schenk D., Yednock T. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 2000, 6:916-919.
4. Bernardo M.M., Day D.E., Halvorson H.R., Olson S.T., Shore J.D. Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies. J. Biol. Chem. 1993, 268:12477-12483.
5. Betzel C., Pal G.P., Saenger W. Three-dimensional structure of proteinase K at 0.15-nm resolution. Eur. J. Biochem. 1988, 178:155-171.
6. Beynon R.J., Salvesen G.S. Appendix III. Commercially available protease inhibitors. Proteolytic Enzymes: A Practical Approach 2001, 317-330. Oxford University Press, Oxford. Second ed. R.J. Beynon, J.S. Bond (Eds.).
7. Chia S.E., Ong C.N., Chua L.H., Ho L.M., Tay S.K. Comparison of zinc concentrations in blood and seminal plasma and the various sperm parameters between fertile and infertile men. J. Androl. 2000, 21:53-57.
8. Duckworth W.C., Bennett R.G., Hamel F.G. Insulin degradation: progress and potential. Endocr. Rev. 1998, 19:608-624.
9. Fernandez-Gamba A., Leal M.C., Morelli L., Castano E.M. Insulin-degrading enzyme: structure-function relationship and its possible roles in health and disease. Curr. Pharm. Des. 2009, 15:3644-3655.
10. Gao Q.S., Sun M., Rees A.R., Paul S. Site-directed mutagenesis of proteolytic antibody light chain. J. Mol. Biol. 1995, 253:658-664.
11. Hashida Y., Inouye K. Kinetic analysis of the activation-and-inhibition dual effects of cobalt ion on thermolysin activity. J. Biochem. 2007, 141:843-853.
12. Hifumi E., Ohara K., Niimi Y., Uda T. Removal of catalytic activity by EDTA from antibody light chain. Biometals 2000, 13:289-294.
13. Hifumi E., Honjo E., Fujimoto N., Arakawa M., Nishizono A., Uda T. Highly efficient method of preparing human catalytic antibody light chains and their biological characteristics. FASEB J. 2012, 26:1607-1615.
14. Hu Z., Periyannan G.R., Crowder M.W. Folding strategy to prepare Co(II)-substituted metallo-beta-lactamase L1. Anal. Biochem. 2008, 378:177-183.
15. Jellinger K.A. Alzheimer disease and cerebrovascular pathology: an update. J. Neural Transm. 2002, 109:813-836.
16. Kang C.Y., Kohler H. Immunoglobulin with complementary paratope and idiotope. J. Exp. Med. 1986, 163:787-796.
17. Kasturirangan S., Boddapati S., Sierks M.R. Engineered proteolytic nanobodies reduce Abeta burden and ameliorate Abeta-induced cytotoxicity. Biochemistry 2010, 49:4501-4508.
18. Kohler H., Paul S. Superantibody activities: new players in innate and adaptive immune responses. Immunol. Today 1998, 19:221-227.
19. Liu Y.H., Giunta B., Zhou H.D., Tan J., Wang Y.J. Immunotherapy for Alzheimer disease: the challenge of adverse effects. Nat. Rev. Neurol. 2012, 8:465-469.
20. Llobet J.M., Domingo J.L., Corbella J. Comparison of the effectiveness of several chelators after single administration on the toxicity, excretion and distribution of cobalt. Arch. Toxicol. 1986, 58:278-281.
21. McCall K.A., Huang C., Fierke C.A. Function and mechanism of zinc metalloenzymes. J. Nutr. 2000, 130:1437S-1446S.
22. Mukherjee A., Song E., Kihiko-Ehmann M., Goodman J.P., Pyrek J.S., Estus S., Hersh L.B. Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques. J. Neurosci. 2000, 20:8745-8749.
23. Neshat M.N., Goodglick L., Lim K., Braun J. Mapping the B cell superantigen binding site for HIV-1 gp120 on a V(H)3 Ig. Int. Immunol. 2000, 12:305-312.
24. Nishiyama Y., Taguchi H., Luo J.Q., Zhou Y.X., Burr G., Karle S., Paul S. Covalent reactivity of phosphonate monophenyl esters with serine proteinases: an overlooked feature of presumed transition state analogs. Arch. Biochem. Biophys. 2002, 402:281-288.
25. Nishiyama Y., Mitsuda Y., Taguchi H., Planque S., Hara M., Karle S., Hanson C.V., Uda T., Paul S. Broadly distributed nucleophilic reactivity of proteins coordinated with specific ligand binding activity. J. Mol. Recognit. 2005, 18:295-306.
26. Park M.H., Lee J.K., Choi S., Ahn J., Jin H.K., Park J.S., Bae J.S. Recombinant soluble neprilysin reduces amyloid-beta accumulation and improves memory impairment in Alzheimer's disease mice. Brain Res. 2013, 1529:113-124.
27. Paul S., Planque S., Nishiyama Y. Immunological origin and functional properties of catalytic autoantibodies to amyloid beta peptide. J. Clin. Immunol. 2010, 30(Suppl. 1):S43-S49.
28. Paul S., Planque S.A., Nishiyama Y., Hanson C.V., Massey R.J. Nature and nurture of catalytic antibodies. Adv. Exp. Med. Biol. 2012, 750:56-75.
29. Piazza F., Greenberg S.M., Savoiardo M., Gardinetti M., Chiapparini L., Raicher I., Nitrini R., Sakaguchi H., Brioschi M., Billo G., Colombo A., Lanzani F., Piscosquito G., Carriero M.R., Giaccone G., Tagliavini F., Ferrarese C., Difrancesco J.C. Anti-amyloid beta autoantibodies in cerebral amyloid angiopathy-related inflammation: implications for Amyloid-Modifying Therapies. Ann. Neurol. 2013, 73:449-458.
30. Planque S., Bangale Y., Song X.T., Karle S., Taguchi H., Poindexter B., Bick R., Edmundson A., Nishiyama Y., Paul S. Ontogeny of proteolytic immunity: IgM serine proteases. J. Biol. Chem. 2004, 279:14024-14032.
31. Planque S.A., Taniguchi R., Watanabe K., Sigurdsson E.M., Fukuchi K., Massey R.J., Nishiyama Y., Paul S. Preclinical catalytic immunotherapy of Alzheimer's disease. Keystone Symposia 2012.
32. Polosukhina D.I., Kanyshkova T.G., Doronin B.M., Tyshkevich O.B., Buneva V.N., Boiko A.N., Gusev E.I., Nevinsky G.A., Favorova O.O. Metal-dependent hydrolysis of myelin basic protein by IgGs from the sera of patients with multiple sclerosis. Immunol. Lett. 2006, 103:75-81.
33. Radisky E.S., Lee J.M., Lu C.J., Koshland D.E. Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:6835-6840.
34. Ramsland P.A., Terzyan S.S., Cloud G., Bourne C.R., Farrugia W., Tribbick G., Geysen H.M., Moomaw C.R., Slaughter C.A., Edmundson A.B. Crystal structure of a glycosylated Fab from an IgM cryoglobulin with properties of a natural proteolytic antibody. Biochem. J. 2006, 395:473-481.
35. Rawlings N.D., Barrett A.J. Chapter 77 - Introduction: metallopeptidases and their clans. Handbook of Proteolytic Enzymes 2013, Vol. 1:325-370. Academic Press/Elsevier, London. third ed.
36. Reshetnyak A.V., Armentano M.F., Ponomarenko N.A., Vizzuso D., Durova O.M., Ziganshin R., Serebryakova M., Govorun V., Gololobov G., Morse H.C., Friboulet A., Makker S.P., Gabibov A.G., Tramontano A. Routes to covalent catalysis by reactive selection for nascent protein nucleophiles. J. Am. Chem. Soc. 2007, 129:16175-16182.
37. Sabel C.E., Carbone R., Dabous J.R., Lo S.Y., Siemann S. Preparation and characterization of cobalt-substituted anthrax lethal factor. Biochem. Biophys. Res. Commun. 2011, 416:106-110.
38. Sapparapu G., Planque S., Mitsuda Y., McLean G., Nishiyama Y., Paul S. Constant domain-regulated antibody catalysis. J. Biol. Chem. 2012, 287:36096-36104.
39. Shuster A.M., Gololobov G.V., Kvashuk O.A., Bogomolova A.E., Smirnov I.V., Gabibov A.G. DNA hydrolyzing autoantibodies. Science 1992, 256:665-667.
40. Sodhi J.S., Bryson K., McGuffin L.J., Ward J.J., Wernisch L., Jones D.T. Predicting metal-binding site residues in low-resolution structural models. J. Mol. Biol. 2004, 342:307-320.
41. Stec B., Holtz K.M., Kantrowitz E.R. A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J. Mol. Biol. 2000, 299:1303-1311.
42. Sumitomo M., Shen R., Nanus D.M. Involvement of neutral endopeptidase in neoplastic progression. Biochim. Biophys. Acta 2005, 1751:52-59.
43. Taguchi H., Planque S., Sapparapu G., Boivin S., Hara M., Nishiyama Y., Paul S. Exceptional amyloid beta peptide hydrolyzing activity of nonphysiological immunoglobulin variable domain scaffolds. J. Biol. Chem. 2008, 283:36724-36733.
44. Taguchi H., Planque S., Nishiyama Y., Symersky J., Boivin S., Szabo P., Friedland R.P., Ramsland P.A., Edmundson A.B., Weksler M.E., Paul S. Autoantibody-catalyzed hydrolysis of amyloid beta peptide. J. Biol. Chem. 2008, 283:4714-4722.
45. Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 2003, 60:523-533.
46. Vadivel K., Bajaj S.P. Structural biology of factor VIIa/tissue factor initiated coagulation. Front. Biosci. (Landmark Ed.) 2012, 17:2476-2494.
47. Warmlander S., Tiiman A., Abelein A., Luo J., Jarvet J., Soderberg K.L., Danielsson J., Graslund A. Biophysical studies of the amyloid beta-peptide: interactions with metal ions and small molecules. Chembiochem 2013, 14:1692-1704.
48. Zago W., Schroeter S., Guido T., Khan K., Seubert P., Yednock T., Schenk D., Gregg K.M., Games D., Bard F., Kinney G.G. Vascular alterations in PDAPP mice after anti-Abeta immunotherapy: implications for amyloid-related imaging abnormalities. Alzheimers Dement. 2013, 9:S105-S115.
49. Zhou Y.X., Karle S., Taguchi H., Planque S., Nishiyama Y., Paul S. Prospects for immunotherapeutic proteolytic antibodies. J. Immunol. Methods 2002, 269:257-268.