ScFv-mediated in vivo targeting of DAF to erythrocytes inhibits lysis by complement

Molecular Immunology

Volumn 40, Issue 13, 2004, Pages 911-919

  Spitzer, Dirk ^a   Unsinger, Jacqueline ^a   Bessler, Monica ^a   Atkinson, John P ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Decay accelerating factor; Erythrocytes; Fusion protein; In vivo; Single chain Fv; Targeting

Indexed keywords

C REACTIVE PROTEIN; COMPLEMENT; DECAY ACCELERATING FACTOR; EPITOPE; HYBRID PROTEIN; MEMBRANE ANTIGEN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL TYPE; CONTROLLED STUDY; ERYTHROCYTE; FOLLOW UP; HUMAN; IN VITRO STUDY; IN VIVO STUDY; INJECTION; LYSIS; MOLECULE; MOUSE; NONHUMAN; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; RAT; REGULATORY MECHANISM; STATISTICAL SIGNIFICANCE;

EID: 0346023953     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2003.10.017     Document Type: Article

References (58)

1. Atkinson, J.P., Bessler, M., 2000. Paroxysmal nocturnal hemoglobinuria. The Molecular Basis of Blood Disease, third ed. Saunders, Philadelphia, PA, pp. 564-577.
2. Auffray I., Marfatia S., de Jong K., Lee G., Huang C.-H., Paszty C., Tanner M.J.A., Mohandas N., Chasis J.A. Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice. Blood. 97:2001;2872-2878.
3. Bessler M., Mason P.J., Hillmen P., Miyata T., Yamada N., Takeda J., Luzzatto L., Kinoshita T. Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 13:1994;110-117.
4. Böldicke T., Tesar M., Griesel C., Rohde M., Grone H.-J., Waltenberger J., Kollet O., Lapidot T., Yayon A., Weich H. Anti-VEGFR-2 scFvs for cell isolation. Single-chain antibodies recognizing the human vascular endothelial growth factor receptor-2 (VEGFR-2/flk-1) on the surface of primary endothelial cells and preselected CD34+ cells from cord blood. Stem Cells. 19:2001;24-36.
5. Caras I.W., Weddell G.N., Davitz M.A., Nussenzweig V., Martin D.W. Signal for attachment of a phospholipid membrane anchor in decay accelerating factor. Science. 238:1987;1280-1283.
6. Christiansen D., Milland J., Thorley B.R., McKenzie I.F., Mottram P.L., Purcell L.J., Loveland B.E. Engineering of recombinant soluble CD46: an inhibitor of complement activation. Immunology. 87:1996;348-354.
7. Coyne K.E., Hall S.E., Thompson E.S., Arce M.A., Kinoshita T., Fujita T., Anstee D.J., Rosse W., Lublin D.M. Mapping of epitopes, glycosylation sites, and complement regulatory domains in human decay accelerating factor. J. Immunol. 149:1992;2906-2913.
8. Dacie, J.V., Luzzatto, L., 1996. Paroxysmal nocturnal haemoglobinuria. In: Wetherall, D.J., Warrel, A., Ledigham. L. (Eds.), Oxford Textbook of Medicine, vol. 3, third ed. Oxford University Press, Oxford, UK, pp. 3449-3452.
9. Davitz M.A., Low M.G., Nussenzweig V. Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PIPLC). J. Exp. Med. 163:1986;1150-1161.
10. Dirks W., Wirth M., Hauser H. Dicistronic transcription units for gene expression in mammalian cells. Gene. 128:1993;247-249.
11. Dübel S., Breitling F., Fuchs P., Zewe M., Gotter S., Welschof M., Moldenhauer G., Little M. Isolation of IgG antibody Fv-DNA from various mouse and rat hybridoma cell lines using the polymerase chain reaction with a simple set of primers. J. Immunol. Methods. 175:1994;89-95.
12. Fearon D.T. Anti-inflammatory and immunosuppressive effects of recombinant soluble complement receptors. Clin. Exp. Immunol. 86(Suppl. 1):1991;43-46.
13. Fodor W.L., Rollins S.A., Guilmette E.R. A novel bifunctional chimeric complement inhibitor that regulates C3 convertase and formation of the membrane attack complex. J. Immunol. 155:1995;4135-4138.
14. Galili U., Shohet S., Kobrin E., Stults C., Macher B. Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells. J. Biol. Chem. 263:1988;17755-17762.
15. Harris C.L., Fraser D.A., Morgan B.P. Tailoring anti-complement therapeutics. Biochem. Soc. Trans. 30:2002;1019-1026.
16. Harris C.L., Williams A.S., Linton S.M., Morgan B.P. Coupling complement regulators to immunoglobulin domains generates effective anti-complement reagents with extended half-life in vivo. Clin. Exp. Immunol. 129:2002;198-207.
17. Harris C.L., Hughes C.L., Williams A.S., Goodfellow I., Evans D.J., Caterson B., Morgan B.P. Generation of anti-complement "prodrugs" J. Biol. Chem. 278:2003;36068-36076.
18. Kina T., Ikuta K., Takayama E., Wada K., Majumdar A.S., Weissman I.L., Katsura Y. The monoclonal antibody TER-119 recognizes a molecular associated with glycophorin A and specifically marks the late stages of murine erythroid lineage. Br. J. Haematol. 109:2000;280-287.
19. Kirshfink M. Targeting complement in therapy. Immunol. Rev. 180:2001;177-189.
20. Klickstein, L.B., Moore Jr., F.D., Atkinson, J.P., 2000. Therapeutic inhibition of complement activation with emphasis on drugs in clinical trials. In: Austen, K.F., Burakoff, S.J., Strom, T.B., Rosen, F.S. (Eds.), Ther. Immunol. Blackwell, Malden, MA, pp. 287-301.
21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
22. Lambris, J.D., Holers, V.M. (Eds.), 2000. Therapeutic Interventions in the Complement System. Humana Press, Totawa, NJ.
23. Linton S.M., Williams A.S., Dodd I., Smith R., Williams B.D., Morgan B.P. Therapeutic efficacy of a novel membrane-targeted complement regulator in antigen-induced arthritis in the rat. Arthritis Rheum. 43:2000;2590-2597.
24. Liszewski M.K., Farries T.C., Lublin D.M., Rooney I.A., Atkinson J.P. Control of the complement system. Adv. Immunol. 61:1996;201-283.
25. Lublin D.M., Atkinson J.P. Decay accelerating factor: biochemistry, molecular biology, and function. Annu. Rev. Immunol. 7:1989;35-58.
26. Lublin D.M., Coyne K.E. Phospholipid-anchored and transmembrane versions of either decay-accelerating factor or membrane cofactor protein show equal efficiency in protection from complement-mediated cell damage. J. Exp. Med. 174:1991;35-44.
27. Lublin D.M., Krsek-Staples J., Pangburn M.K., Atkinson J.P. Biosynthesis and glycosylation of the human complement regulatory protein decay-accelerating factor. J. Immunol. 137:1986;1629-1635.
28. Magnani M., Rossi L., Stocchi V., Cucchiarini L., Piacentini G., Fornaini G. Effect of age on some properties of mice erythrocytes. Mech. Ageing Dev. 42:1988;37-47.
29. Medof M.E., Walter E.I., Roberts W.L., Haas R., Rosenberry T.L. Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid. Biochemistry. 25:1986;6740-6747.
30. Moran P., Beasley H., Gorrell A., Martin E., Gribling P., Fuchs H., Gillett N., Burton L.E., Caras I.W. Human recombinant soluble decay accelerating factor inhibits complement activation in vitro and in vivo. J. Immunol. 149:1992;1736-1743.
31. Morgan, B.P., 1990. In: Morgan, B.P. (Ed.), Complement: Clinical Aspects and Relevance to Disease. Harcourt Brace Javanovich, London.
32. Morgan, B.P., Harris, C.L., 1999. In: Morgan, B.P., Harris, C.L. (Eds.), Complement Regulatory Proteins. Harcourt Brace & Company, San Diego.
33. Morgan B.P., Meri S. Membrane proteins that protect against complement lysis. Springer Semin. Immunopathol. 15:1994;369-396.
34. Nakano Y., Sumida K., Kikuta N., Murira N.H., Tobe T., Tomita M. Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen). Biochem. Biophys. Acta. 1116:1992;235-240.
35. Nicholson-Weller A., March J.P., Rosenfeld S.I., Austen K.F. Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor. Proc. Natl. Acad. Sci. U.S.A. 80:1983;5066-5070.
36. Nielsen P.J., Lorenz B., Müller A.M., Wenger R.H., Brombacher F., Simon M., von der Weid T., Langhorne W.J., Mossmann H., Kohler G. Altered erythrocytes and a leaky block in B-cell development in CD24/HSA-deficient mice. Blood. 89:1997;1058-1067.
37. Pangburn M.K. Localization of the host recognition functions of complement factor H at the carboxyl-terminal: implications for hemolytic uremic syndrome. J. Immunol. 169:2002;4702-4706.
38. Pangburn M.K., Schreiber R.D., Müller-Eberhard H.J. Deficiency of an erythrocyte membrane protein with complement regulatory activity in paroxysmal nocturnal hemoglobinuria. Proc. Natl. Acad. Sci. U.S.A. 80:1983;5430-5434.
39. Parker C.J. Historical aspects of paroxysmal nocturnal haemoglobinuria: Defining the disease. Br. J. Haematol. 117:2002;3-22.
40. Parker, C.M., 1992. Membrane Defenses against Attack by Complement and Perforins. Springer-Verlag, Berlin.
41. Quigg R.J., Kozono Y., Berthiaume D., Lim A., Salant D.J., Weinfeld A., Griffin P., Kremmer E., Holers V.M. Blockade of antibody-induced glomerulonephritis with Crry-Ig, a soluble murine complement inhibitor. J. Immunol. 160:1998;4553-4560.
42. Rittershaus C.W., Thomas L.J., Miller D.P., Picard M.D., Geoghegan-Barek K.M., Scesney S.M., Henry L.D., Sen A.C., Bertino A.M., Hannig G., Adari H., Mealey R.A., Gosselin M.L., Couto M., Hayman E.G., Levin J.L., Reinhold V.N., Marsh H.C. Jr. Recombinant glycoproteins that inhibit complement activation and also bind the selectin adhesion molecules. J. Biol. Chem. 274:1999;11237-11244.
43. Rosse W.F. Paroxysmal nocturnal hemoglobinuria as a molecular disease. Medicine (Baltimore). 76:1997;63-93.
44. Rother R.P., Squinto S.P. The α-galactosyl epitope: a sugar coating that makes viruses and cells unpalatable. Cell. 86:1996;185-188.
45. Smith G.P., Smith R.A. Membrane-targeted complement inhibitors. Mol. Immunol. 38:2001;249-255.
46. Spitzer D., Dittmar K.E.J., Rohde M., Hauser H., Wirth D. Green fluorescent protein-tagged retroviral envelope protein for analysis of virus-cell interactions. J. Virol. 77:2003;6070-6075.
47. Spitzer D., Hauser H., Wirth D. Complement-protected amphotropic retroviruses from murine packaging cells. Hum. Gene Ther. 10:1999;1893-1902.
48. Sugita Y., Ito K., Shiozuka K., Suzuki H., Gushima H., Tomita M., Masuho Y. Recombinant soluble CD59 inhibits reactive haemolysis with complement. Immunology. 82:1994;34-41.
49. Takeda J., Miyata T., Kawagoe K., Iida Y., Endo Y., Fujita T., Takahashi M., Kitani T., Kinoshita T. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal haemoglobinuria. Cell. 73:1993;703-711.
50. Tremml G., Dominguez C., Rosti V., Zhang Z., Pandolfi P.P., Keller P., Bessler M. Increased sensitivity to complement and a decreased red blood cell life span in mice mosaic for a nonfunctional Piga gene. Blood. 94:1999;2945-2954.
51. Verma I.M., Somia N. Gene therapy - promises, problems and prospects. Nature. 389:1997;239-242.
52. Volanakis, J.E., Frank, M.M., 1998. The Human Complement System in Health and Disease. Marcel Dekker, New York.
53. Walport M.J. Complement. First of two parts. N. Engl. J. Med. 344:2001a;1058-1066.
54. Walport M.J. Complement. Second of two parts. N. Engl. J. Med. 344:2001b;1140-1144.
55. Watanabe R., Inoue N., Westfall B., Taron C.H., Orlean P., Takeda J., Kinoshita T. The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 17:1998;877-885.
56. Weisman H.F., Bartow T., Leppo M.K., Marsh H.C. Jr., Carson G.R., Concino M.F., Boyle M.P., Reux K.H., Weisfeldt M.L., Fearon D.T. Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post ischemic myocardial inflammation and necrosis. Science. 249:1990;146-151.
57. Zhang H., Lu S., Morrison S.L., Tomlinson S. Targeting of functional antibody-decay-accelerating factor fusion proteins to a cell surface. J. Biol. Chem. 276:2001;27290-27295.
58. Zhang H.F., Yu J., Bajwa E., Morrison S.L., Tomlinson S. Targeting of functional antibody-CD59 fusion proteins to a cell surface. J. Clin. Invest. 103:1999;55-61.