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CD59: A long-known complement inhibitor has advanced to a blood group system


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Zalman LS, Wood LM, Muller-Eberhard HJ. Isolation of a human erythrocyte membrane protein capable of inhibiting expression of homologous complement transmembrane channels. Proc Natl Acad Sci U S A 1986;83:6975–9.10.1073/pnas.83.18.6975Search in Google Scholar

Schönermark S, Filsinger S, Berger B, et al. The C8-binding protein of human erythrocytes: interaction with the components of the complement-attack phase. Immunology 1988;63:585–90.Search in Google Scholar

Zalman LS, Wood LM, Frank MM, Muller-Eberhard HJ. Deficiency of the homologous restriction factor in paroxysmal nocturnal hemoglobinuria. J Exp Med 1987;165:572–7.10.1084/jem.165.2.572Search in Google Scholar

Hänsch GM, Schönermark S, Roelcke D. Paroxysmal nocturnal hemoglobinuria type III: lack of an erythrocyte membrane protein restricting the lysis by C5b-9. J Clin Invest 1987;80: 7–12.10.1172/JCI113065Search in Google Scholar

Watts MJ, Dankert JR, Morgan EP. Isolation and characterization of a membrane-attack-complex-inhibiting protein present in human serum and other biological fluids. Biochem J 1990;265:471–7.10.1042/bj2650471Search in Google Scholar

Sugita Y, Nakano Y, Tomita M. Isolation from human erythrocytes of a new membrane protein which inhibits the formation of complement transmembrane channels. J Biochem 1988;104:633–7.10.1093/oxfordjournals.jbchem.a122524Search in Google Scholar

Holguin MH, Fredrick LR, Bernshaw NJ, Wilcox LA, Parker CJ. Isolation and characterization of a membrane protein from normal human erythrocytes that inhibits reactive lysis of the erythrocytes of paroxysmal nocturnal hemoglobinuria. J Clin Invest 1989;84:7–17.10.1172/JCI114172Search in Google Scholar

Okada N, Harada R, Fujita T, Okada H. A novel membrane glycoprotein capable of inhibiting membrane attack by homologous complement. Int Immunol 1989;1:205–8.10.1093/intimm/1.2.205Search in Google Scholar

Whitlow MB, Iida K, Stefanova I, Bernard A, Nussenzweig V. H19, a surface membrane molecule involved in T-cell activation, inhibits channel formation by human complement. Cell Immunol 1990;126:176–84.10.1016/0008-8749(90)90310-NSearch in Google Scholar

Stefanova I, Hilgert I, Kristofova H, Brown R, Low MG, Horejsi V. Characterization of a broadly expressed human leucocyte surface antigen MEM-43 anchored in membrane through phosphatidylinositol. Mol Immunol 1989;26:153–61.10.1016/0161-5890(89)90097-7Search in Google Scholar

Meri S, Morgan BP, Wing M, et al. Human protectin (CD59), an 18-20-kD homologous complement restriction factor, does not restrict perforin-mediated lysis. J Exp Med 1990;172:367–70.10.1084/jem.172.1.36721881361694224Search in Google Scholar

Yamashina M, Ueda E, Kinoshita T, et al. Inherited complete deficiency of 20-kilodalton homologous restriction factor (CD59) as a cause of paroxysmal nocturnal hemoglobinuria. N Engl J Med 1990;323:1184–9.10.1056/NEJM199010253231707Search in Google Scholar

Motoyama N, Okada N, Yamashina M, Okada H. Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion in the HRF20 (CD59) gene. Eur J Immunol 1992;22:2669–73.10.1002/eji.1830221029Search in Google Scholar

Nevo Y, Ben-Zeev B, Tabib A, et al. CD59 deficiency is associated with chronic hemolysis and childhood relapsing immune-mediated polyneuropathy. Blood 2013;121:129–35.10.1182/blood-2012-07-441857Search in Google Scholar

Höchsmann B, Dohna-Schwake C, Kyrieleis HA, Pannicke U, Schrezenmeier H. Targeted therapy with eculizumab for inherited CD59 deficiency. N Engl J Med 2014;370:90–2.10.1056/NEJMc1308104Search in Google Scholar

Anliker M, von Zabern I, Höchsmann B, et al. A new blood group antigen is defined by anti-CD59, detected in a CD59-deficient patient. Transfusion 2014;54:1817–22.10.1111/trf.12531Search in Google Scholar

Haliloglu G, Maluenda J, Sayinbatur B, et al. Early-onset chronic axonal neuropathy, strokes, and hemolysis: inherited CD59 deficiency. Neurology 2015;84:1220–4.10.1212/WNL.0000000000001391Search in Google Scholar

International Society of Blood Transfusion. Table of blood group antigens v4.0 141224 ISBT Working Party Red Cell Immunogenetics and Blood Group Terminology. http://www. isbtweb.org/working-parties/red-cell-immunogenetics-and-blood-group-terminology/.Search in Google Scholar

Tone M, Walsh LA, Waldmann H. Gene structure of human CD59 and demonstration that discrete mRNAs are generated by alternative polyadenylation. J Mol Biol 1992;227:971–6.10.1016/0022-2836(92)90239-GSearch in Google Scholar

Holguin MH, Martin CB, Eggett T, Parker CJ. Analysis of the gene that encodes the complement regulatory protein, membrane inhibitor of reactive lysis (CD59): identification of an alternatively spliced exon and characterization of the transcriptional regulatory regions of the promoter. J Immunol 1996;157:1659–68.Search in Google Scholar

Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D. Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure 1994;2: 185–99.10.1016/S0969-2126(00)00020-4Search in Google Scholar

Kieffer B, Driscoll PC, Campbell ID, Willis AC, van der Merwe PA, Davis SJ. Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins. Biochemistry 1994;33:4471–82.10.1021/bi00181a006Search in Google Scholar

Huang Y, Fedarovich A, Tomlinson S, Davies C. Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex. Acta Crystallogr D Biol Crystallogr 2007;63:714–21.10.1107/S090744490701555717505110Search in Google Scholar

Rudd PM, Morgan BP, Wormald MR, et al. The glycosylation of the complement regulatory protein, human erythrocyte CD59. J Biol Chem 1997;272:7229–44.10.1074/jbc.272.11.7229Search in Google Scholar

Zhao J, Rollins SA, Maher SE, Bothwell AL, Sims PJ. Amplified gene expression in CD59-transfected Chinese hamster ovary cells confers protection against the membrane attack complex of human complement. J Biol Chem 1991;266:13418–22.10.1016/S0021-9258(18)98856-3Search in Google Scholar

Ninomiya H, Stewart BH, Rollins SA, Zhao J, Bothwell AL, Sims PJ. Contribution of the N-linked carbohydrate of erythrocyte antigen CD59 to its complement-inhibitory activity. J Biol Chem 1992;267:8404–10.10.1016/S0021-9258(18)42459-3Search in Google Scholar

Carroll MV, Sim RB. Complement in health and disease. Adv Drug Deliv Rev 2011;63:965–75.10.1016/j.addr.2011.06.005Search in Google Scholar

Aleshin AE, Schraufstatter IU, Stec B, Bankston LA, Liddington RC, DiScipio RG. Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). J Biol Chem 2012;287:10210–22.10.1074/jbc.M111.327809Search in Google Scholar

Meri S, Lehto T, Sutton CW, Tyynela J, Baumann M. Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis. Biochem J 1996;316:923–35.10.1042/bj3160923Search in Google Scholar

Hakulinen J, Meri S. Shedding and enrichment of the glycolipid-anchored complement lysis inhibitor protectin (CD59) into milk fat globules. Immunology 1995;85:495–501.Search in Google Scholar

Huang Y, Smith CA, Song H, Morgan BP, Abagyan R, Tomlinson S. Insights into the human CD59 complement binding interface toward engineering new therapeutics. J Biol Chem 2005;280:34073–9.10.1074/jbc.M504922200Search in Google Scholar

Leath KJ, Johnson S, Roversi P, et al. High-resolution structures of bacterially expressed soluble human CD59. Acta Crystallogr Sect F Struct Biol Cryst Commun 2007;63:648–52.10.1107/S1744309107033477Search in Google Scholar

Fraser DA, Harris CL, Williams AS, et al. Generation of a recombinant, membrane-targeted form of the complement regulator CD59: activity in vitro and in vivo. J Biol Chem 2003; 278:48921–7.10.1074/jbc.M302598200Search in Google Scholar

Fishelson Z, Donin N, Zell S, Schultz S, Kirschfink M. Obstacles to cancer immunotherapy: expression of membrane complement regulatory proteins (mCRPs) in tumors. Mol Immunol 2003;40:109–23.10.1016/S0161-5890(03)00112-3Search in Google Scholar

Hu W, Yu Q, Hu N, et al. A high-affinity inhibitor of human CD59 enhances complement-mediated virolysis of HIV-1: implications for treatment of HIV-1/AIDS. J Immunol 2010; 184:359–68.10.4049/jimmunol.0902278427287119955519Search in Google Scholar

Wickham SE, Hotze EM, Farrand AJ, et al. Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9. J Biol Chem 2011;286:20952–62.10.1074/jbc.M111.237446312147121507937Search in Google Scholar

Cai B, Xie S, Liu F, et al. Rapid degradation of the complement regulator, CD59, by a novel inhibitor. J Biol Chem 2014;289: 12109–25.10.1074/jbc.M113.547083400211624616098Search in Google Scholar

van der Merwe PA, Barclay AN, Mason DW, et al. Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59. Biochemistry 1994;33:10149–60.10.1021/bi00199a0437520278Search in Google Scholar

Baalasubramanian S, Harris CL, Donev RM, et al. CD59a is the primary regulator of membrane attack complex assembly in the mouse. J Immunol 2004;173:3684–92.10.4049/jimmunol.173.6.368415356114Search in Google Scholar

Kimberley FC, Sivasankar B, Paul MB. Alternative roles for CD59. Mol Immunol 2007;44:73–81.10.1016/j.molimm.2006.06.01916884774Search in Google Scholar

Yazer MH, Judd WJ, Davenport RD, et al. Case report and literature review: transient Inab phenotype and an agglutinating anti-IFC in a patient with a gastrointestinal problem. Transfusion 2006;46:1537–42.10.1111/j.1537-2995.2006.00933.x16965581Search in Google Scholar

Höchsmann B. Personal communication. 2015.Search in Google Scholar

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Medicine, Clinical Medicine, Laboratory Medicine