DAF regulates the complement system on the cell surface. It recognizes C4b and C3b fragments that are created during activation of C4 (classical or lectin pathway) or C3 (alternative pathway). Interaction of DAF with cell-associated C4b of the classical and lectin pathways interferes with the conversion of C2 to C2b, thereby preventing formation of the C4b2a C3-convertase, and interaction of DAF with C3b of the alternative pathway interferes with the conversion of factor B to Bb by factor D, thereby preventing formation of the C3bBb C3 convertase of the alternative pathway. Thus, by limiting the amplification convertases of the complement cascade, DAF indirectly blocks the formation of the membrane attack complex.[6]
This glycoprotein is broadly distributed among hematopoietic and non-hematopoietic cells. It is a determinant for the Cromer blood group system.
DAF contains four complement control protein (CCP) repeats with a single N-linked glycan positioned between CCP1 and CCP2. CCP2, CCP3, CCP4 and three consecutive lysine residues in a positively charged pocket between CCP2 and CCP3 are involved in its inhibition of the alternate complement pathway. CCP2 and CCP3 alone are involved in its inhibition of the classical pathway.[7]
Pathologyedit
Paroxysmal nocturnal hemoglobinuriaedit
Because DAF is a GPI-anchored protein, its expression is reduced in persons with mutations that reduce GPI levels such as those with paroxysmal nocturnal hemoglobinuria (PNH). In PNH disorder, red blood cells with very low levels of DAF and CD59 undergo complement-mediated hemolysis. Symptoms include low red blood cell count (anemia), fatigue, and episodes of dark colored urine and other complications.[8]
Infectious diseasesedit
DAF is used as a receptor by some coxsackieviruses and other enteroviruses.[9] Recombinant soluble DAF-Fc has been tested in mice as an anti-enterovirus therapy for heart damage;[10] however, the human enterovirus that was tested binds much more strongly to human DAF than to mouse or rat DAF. Echoviruses and coxsackie B viruses that use human decay-accelerating factor (DAF) as a receptor do not bind the rodent analogues of DAF.[11] and DAF-Fc has yet to be tested in humans.
Binding of DAF to human HIV-1 when the virons are budding from the surface of infected cells protects HIV-1 from complement mediated lysis.[12][13]
^Brodbeck WG, Kuttner-Kondo L, Mold C, Medof ME (Sep 2000). "Structure/function studies of human decay-accelerating factor". Immunology. 101 (1): 104–11. doi:10.1046/j.1365-2567.2000.00086.x. PMC2327052. PMID 11012760.
^Parker C, Omine M, Richards S, et al. (2005). "Diagnosis and management of paroxysmal nocturnal hemoglobinuria". Blood. 106 (12): 3699–709. doi:10.1182/blood-2005-04-1717. PMC1895106. PMID 16051736.
^Karnauchow TM, Tolson DL, Harrison BA, Altman E, Lublin DM, Dimock K (August 1996). "The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55)". J. Virol. 70 (8): 5143–52. doi:10.1128/JVI.70.8.5143-5152.1996. PMC190469. PMID 8764022.
^Yanagawa B, Spiller OB, Choy J, Luo H, Cheung P, Zhang HM, Goodfellow IG, Evans DJ, Suarez A, Yang D, McManus BM (January 2003). "Coxsackievirus B3-associated myocardial pathology and viral load reduced by recombinant soluble human decay-accelerating factor in mice". Lab. Invest. 83 (1): 75–85. doi:10.1097/01.lab.0000049349.56211.09. PMID 12533688.
^Spiller OB, Goodfellow IG, Evans DJ, Almond JW, Morgan BP (January 2000). "Echoviruses and coxsackie B viruses that use human decay-accelerating factor (DAF) as a receptor do not bind the rodent analogues of DAF". J. Infect. Dis. 181 (1): 340–3. doi:10.1086/315210. PMID 10608785. S2CID 31672193.
^Marschang P, Sodroski J, Würzner R, Dierich MP (January 1995). "Decay-accelerating factor (CD55) protects human immunodeficiency virus type 1 from inactivation by human complement". Eur J Immunol. 25 (1): 285–90. doi:10.1002/eji.1830250147. PMID 7531147. S2CID 31079892.
^Guibinga GH, Friedmann T (April 2005). "Baculovirus GP64-pseudotyped HIV-based lentivirus vectors are stabilized against complement inactivation by codisplay of decay accelerating factor (DAF) or of a GP64-DAF fusion protein". Mol Ther. 11 (4): 645–51. doi:10.1016/j.ymthe.2004.12.002. PMID 15771967.
Further readingedit
Selinka HC, Wolde A, Sauter M, et al. (2004). "Virus-receptor interactions of coxsackie B viruses and their putative influence on cardiotropism". Med. Microbiol. Immunol. 193 (2–3): 127–31. doi:10.1007/s00430-003-0193-y. PMID 12920584. S2CID 21083098.
Mikesch JH, Schier K, Roetger A, et al. (2007). "The expression and action of decay-accelerating factor (CD55) in human malignancies and cancer therapy". Cell. Oncol. 28 (5–6): 223–32. doi:10.1155/2006/814816. PMC4618202. PMID 17167176.
External linksedit
Decay-Accelerating+Factor at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Cromer blood group system at BGMUT Blood Group Antigen Gene Mutation Database at NCBI, NIH
Overview of all the structural information available in the PDB for UniProt: P08174 (Complement decay-accelerating factor) at the PDBe-KB.
December 07, 2023
decay, accelerating, factor, complement, decay, accelerating, factor, also, known, cd55, protein, that, humans, encoded, cd55, gene, cd55available, structurespdbortholog, search, pdbe, rcsblist, codes1h03, 1h04, 1h2p, 1h2q, 1m11, 1nwv, 1ojv, 1ojw, 1ojy, 1ok1, . Complement decay accelerating factor also known as CD55 or DAF is a protein that in humans is encoded by the CD55 gene 5 CD55Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1H03 1H04 1H2P 1H2Q 1M11 1NWV 1OJV 1OJW 1OJY 1OK1 1OK2 1OK3 1OK9 1UOT 1UPN 2C8I 2QZD 2QZF 2QZH 3IYP 3J24 5FOAIdentifiersAliasesCD55 CR CROM DAF TC CD55 molecule Cromer blood group CHAPLEExternal IDsOMIM 125240 MGI 104849 HomoloGene 479 GeneCards CD55Gene location Human Chr Chromosome 1 human 1 Band1q32 2Start207 321 519 bp 1 End207 386 804 bp 1 Gene location Mouse Chr Chromosome 1 mouse 2 Band1 E4 1 56 89 cMStart130 316 274 bp 2 End130 350 746 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inparotid glandpalpebral conjunctivalower lobe of lungright lungupper lobe of lungupper lobe of left lungbloodsynovial jointleft adrenal glandmucosa of urinary bladderTop expressed inspermatidspermatocyteseminiferous tubulerectumsecondary oocyteHindgutblastocystduodenumperipheral nervous systemislet of LangerhansMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionvirus receptor activity protein binding lipid bindingCellular componentmembrane Golgi membrane plasma membrane integral component of plasma membrane transport vesicle extracellular region cell surface membrane raft anchored component of membrane extracellular exosome endoplasmic reticulum Golgi intermediate compartment membrane secretory granule membrane ficolin 1 rich granule membraneBiological processregulation of lipopolysaccharide mediated signaling pathway immune system process positive regulation of cytosolic calcium ion concentration positive regulation of CD4 positive alpha beta T cell proliferation respiratory burst endoplasmic reticulum to Golgi vesicle mediated transport positive regulation of CD4 positive alpha beta T cell activation CD4 positive alpha beta T cell cytokine production complement activation classical pathway viral process regulation of complement activation innate immune response viral entry into host cell neutrophil degranulation negative regulation of complement activation regulation of complement dependent cytotoxicitySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez160413137EnsemblENSG00000196352ENSMUSG00000026401UniProtP08174Q61476RefSeq mRNA NM 000574NM 001114543NM 001114544NM 001114752NM 001300902NM 001300903NM 001300904NM 007827NM 001317361RefSeq protein NP 000565NP 001108224NP 001287831NP 001287832NP 001287833NP 001304290NP 031853NP 001391877Location UCSC Chr 1 207 32 207 39 MbChr 1 130 32 130 35 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseDAF regulates the complement system on the cell surface It recognizes C4b and C3b fragments that are created during activation of C4 classical or lectin pathway or C3 alternative pathway Interaction of DAF with cell associated C4b of the classical and lectin pathways interferes with the conversion of C2 to C2b thereby preventing formation of the C4b2a C3 convertase and interaction of DAF with C3b of the alternative pathway interferes with the conversion of factor B to Bb by factor D thereby preventing formation of the C3bBb C3 convertase of the alternative pathway Thus by limiting the amplification convertases of the complement cascade DAF indirectly blocks the formation of the membrane attack complex 6 This glycoprotein is broadly distributed among hematopoietic and non hematopoietic cells It is a determinant for the Cromer blood group system Contents 1 Structure 2 Pathology 2 1 Paroxysmal nocturnal hemoglobinuria 2 2 Infectious diseases 3 See also 4 References 5 Further reading 6 External linksStructure editDAF is a 70 kDa membrane protein that attaches to the cell membrane via a glycophosphatidylinositol GPI anchor DAF contains four complement control protein CCP repeats with a single N linked glycan positioned between CCP1 and CCP2 CCP2 CCP3 CCP4 and three consecutive lysine residues in a positively charged pocket between CCP2 and CCP3 are involved in its inhibition of the alternate complement pathway CCP2 and CCP3 alone are involved in its inhibition of the classical pathway 7 Pathology editParoxysmal nocturnal hemoglobinuria edit Because DAF is a GPI anchored protein its expression is reduced in persons with mutations that reduce GPI levels such as those with paroxysmal nocturnal hemoglobinuria PNH In PNH disorder red blood cells with very low levels of DAF and CD59 undergo complement mediated hemolysis Symptoms include low red blood cell count anemia fatigue and episodes of dark colored urine and other complications 8 Infectious diseases edit DAF is used as a receptor by some coxsackieviruses and other enteroviruses 9 Recombinant soluble DAF Fc has been tested in mice as an anti enterovirus therapy for heart damage 10 however the human enterovirus that was tested binds much more strongly to human DAF than to mouse or rat DAF Echoviruses and coxsackie B viruses that use human decay accelerating factor DAF as a receptor do not bind the rodent analogues of DAF 11 and DAF Fc has yet to be tested in humans Binding of DAF to human HIV 1 when the virons are budding from the surface of infected cells protects HIV 1 from complement mediated lysis 12 13 See also editList of human clusters of differentiation CD59References edit a b c GRCh38 Ensembl release 89 ENSG00000196352 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000026401 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Medof ME Lublin DM Holers VM Ayers DJ Getty RR Leykam JF Atkinson JP Tykocinski ML April 1987 Cloning and characterization of cDNAs encoding the complete sequence of decay accelerating factor of human complement Proc Natl Acad Sci U S A 84 7 2007 11 Bibcode 1987PNAS 84 2007M doi 10 1073 pnas 84 7 2007 PMC 304572 PMID 2436222 Molecular function for CD55 Gene Brodbeck WG Kuttner Kondo L Mold C Medof ME Sep 2000 Structure function studies of human decay accelerating factor Immunology 101 1 104 11 doi 10 1046 j 1365 2567 2000 00086 x PMC 2327052 PMID 11012760 Parker C Omine M Richards S et al 2005 Diagnosis and management of paroxysmal nocturnal hemoglobinuria Blood 106 12 3699 709 doi 10 1182 blood 2005 04 1717 PMC 1895106 PMID 16051736 Karnauchow TM Tolson DL Harrison BA Altman E Lublin DM Dimock K August 1996 The HeLa cell receptor for enterovirus 70 is decay accelerating factor CD55 J Virol 70 8 5143 52 doi 10 1128 JVI 70 8 5143 5152 1996 PMC 190469 PMID 8764022 Yanagawa B Spiller OB Choy J Luo H Cheung P Zhang HM Goodfellow IG Evans DJ Suarez A Yang D McManus BM January 2003 Coxsackievirus B3 associated myocardial pathology and viral load reduced by recombinant soluble human decay accelerating factor in mice Lab Invest 83 1 75 85 doi 10 1097 01 lab 0000049349 56211 09 PMID 12533688 Spiller OB Goodfellow IG Evans DJ Almond JW Morgan BP January 2000 Echoviruses and coxsackie B viruses that use human decay accelerating factor DAF as a receptor do not bind the rodent analogues of DAF J Infect Dis 181 1 340 3 doi 10 1086 315210 PMID 10608785 S2CID 31672193 Marschang P Sodroski J Wurzner R Dierich MP January 1995 Decay accelerating factor CD55 protects human immunodeficiency virus type 1 from inactivation by human complement Eur J Immunol 25 1 285 90 doi 10 1002 eji 1830250147 PMID 7531147 S2CID 31079892 Guibinga GH Friedmann T April 2005 Baculovirus GP64 pseudotyped HIV based lentivirus vectors are stabilized against complement inactivation by codisplay of decay accelerating factor DAF or of a GP64 DAF fusion protein Mol Ther 11 4 645 51 doi 10 1016 j ymthe 2004 12 002 PMID 15771967 Further reading editSelinka HC Wolde A Sauter M et al 2004 Virus receptor interactions of coxsackie B viruses and their putative influence on cardiotropism Med Microbiol Immunol 193 2 3 127 31 doi 10 1007 s00430 003 0193 y PMID 12920584 S2CID 21083098 Mikesch JH Schier K Roetger A et al 2007 The expression and action of decay accelerating factor CD55 in human malignancies and cancer therapy Cell Oncol 28 5 6 223 32 doi 10 1155 2006 814816 PMC 4618202 PMID 17167176 External links editDecay Accelerating Factor at the U S National Library of Medicine Medical Subject Headings MeSH Cromer blood group system at BGMUT Blood Group Antigen Gene Mutation Database at NCBI NIH Overview of all the structural information available in the PDB for UniProt P08174 Complement decay accelerating factor at the PDBe KB Retrieved from https en wikipedia org w index php title Decay accelerating factor amp oldid 1136260066, wikipedia, wiki, book, books, library,
