Conservation in decay accelerating factor (DAF) structure among primates

Developmental and Comparative Immunology

Volumn 24, Issue 8, 2000, Pages 815-827

  Kuttner Kondo, Lisa ^a   Bala Subramanian, V ^b   Atkinson, John P ^b   Yu, Jianliang ^a   Medof, M Edward ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

C3 convertases; Cancer; CD55; Cell surface regulatory proteins; Complement; DAF; Primates; Recognition of self; Xenotransplants

Indexed keywords

CELL SURFACE PROTEIN; CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT; DECAY ACCELERATING FACTOR; REGULATOR PROTEIN;

ALTERNATIVE RNA SPLICING; AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; BABOON; CHIMPANZEE; COMPARATIVE STUDY; CONTROLLED STUDY; EVOLUTION; GENETIC CONSERVATION; GORILLA; IMMUNOBLOTTING; MACACA; MOLECULAR WEIGHT; NONHUMAN; ORANG UTAN; PHENOTYPE; PRIMATE; PRIORITY JOURNAL;

CERCOPITHECIDAE; ERYTHROCEBUS PATAS; HAMADRYAS; MACACA MULATTA; PAN TROGLODYTES; PAPIO HAMADRYAS; PRIMATES;

EID: 0033936342     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0145-305X(00)00026-4     Document Type: Article

References (38)

1. Medof M.E., Walter E.I., Rutgers J.L., Knowles D.M., Nussenzweig V. Identification of the complement decay-accelerating factor (DAF) on epithelium and glandular cells and in body fluids. J. Exp. Med. 165:1987;848-864.
2. Fujita T., Inoue T., Ogawa K., Iida K., Tamura N. The mechanism of action of decay-accelerating factor (DAF). DAF inhibits the assembly of C3 convertases by dissociating C2a and Bb. J. Exp. Med. 166:1987;1221-1228.
3. 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.
4. Medof M.E., Lublin D.M., Holers V.M., Ayers D.J., Getty R.R., Leykam J.F., Atkinson J.P., Tykocinski M.L. Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement. Proc. Natl. Acad. Sci. USA. 84:1987;2007-2011.
5. Lublin D.M., Krsek-Staples J., Pangburn M.K., Atkinson J.P. Biosynthesis and glycosylation of the complement regulatory protein decay accelerating factor. J. Immunol. 137:1986;1629-1635.
6. 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.
7. Brodbeck W.G., Liu D., Sperry J., Mold C., Medof M.E. Localization of classical and alternative pathway regulatory activity within the decay-accelerating factor. J. Immunol. 156:1996;2528-2533.
8. Nickells M.W., Alvarez J.I., Lublin D.M., Atkinson J.P. Characterization of DAF-2, a high molecular weight form of decay-accelerating factor (DAF; CD55), as a covalently cross-linked dimer of DAF-1. J. Immunol. 152:1994;676-685.
9. Spicer A.P., Seldin M.F., Gendler S.J. Molecular cloning and chromosomal localization of the mouse decay-accelerating factor genes. Duplicated genes encode glycosylphosphatidylinositol-anchored and transmembrane forms. J. Immunol. 155:1995;3079-3091.
10. Nonaka M., Miwa T., Okada N., Nonaka M., Okada H. Multiple isoforms of guinea pig decay-accelerating factor (DAF) generated by alternative splicing. J. Immunol. 155:1995;3037-3048.
11. Hinchliffe S.J., Spiller O.B., Rushmere N.K., Morgan B.P. Molecular cloning and functional characterization of the rat analogue of human decay-accelerating factor (CD55). J. Immunol. 161:1998;5695-5703.
12. Stafford H.A., Tykocinski M.L., Lublin D.M., Holers V.M., Rosse W.F., Atkinson J.P., Medof M.E. Normal polymorphic variations and transcription of the decay-accelerating factor (DAF) gene in normal and paroxysmal nocturnal hemoglobinuria (PNH) cells. Proc. Natl. Acad. Sci. USA. 85:1988;880-884.
13. Wang G., Nonaka M., He C., Okada N., Nakashima I., Okada H. Functional differences among multiple isoforms of guinea pig decay-accelerating factor. J. Immunol. 160:1998;3014-3022.
14. Miwa T., Okada N., Okada H. Alternative exon usage in the 3′ region of a single gene generates glycosyl-phosphatidylinositol-anchored and transmembrane forms of rat decay-accelerating factor. Immunogenetics. 51:2000;129-137.
15. Caras I.W., Davitz M.A., Rhee L., Weddell G., Martin D.W. Jr. Cloning of decay accelerating factor suggests novel use of splicing to generate two proteins. Nature. 325:1987;545-549.
16. Nonaka M., Nonaka M., Takenaka O., Okada N., Okada H. A new repetitive sequence uniquely present in the decay-accelerating factor genes. Immunogenetics. 47:1998;246-255.
17. Post T.W., Arce M.A., Liszewski M.K., Thompson E.S., Atkinson J.P., Lublin D.M. Structure of the gene for human complement protein decay accelerating factor. J. Immunol. 144:1990;740-744.
18. Kuttner-Kondo L., Medof M.E., Brodbeck W., Shoham M. Molecular modeling and mechanism of action of human decay-accelerating factor. Prot. Eng. 9:1996;1143-1149.
19. Kinoshita T., Medof M.E., Silber R., Nussenszweig V. Distribution of decay-accelerating factor in the peripheral blood of normal individuals and patients with paroxysmal nocturnal hemoglobinuria. J. Exp. Med. 162:1985;75-92.
20. Higgins D.G., Bleasby A.J., Fuchs R. CLUSTAL V: improved software for multiple sequence alignment. CABIOS. 8:1992;189-191.
21. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
22. Subramaniam S. Biology workbench - a seamless database and analysis environment for the biologist. Proteins. 32:1998;1-2.
23. Unwin R., Fenton J., Whitsitt M., Jamison C., Stupar M., Jakobsson E., Subramaniam S. Biology workbench: a computing and analysis environment for the biological sciences. Letovsky S. Bioinformatics: databases and systems. 1999;233-244 Kluwer Academic Publishers, Boston.
24. Felsenstein J. PHYLIP - Phylogeny Inference Package (Version 3.2). Cladistics. 5:1989;164-166.
25. Felsenstein J. PHYLIP (Phylogeny Inference Package), Version 3.5c. Seattle: Department of Genetics, University of Washington, 1993.
26. Lublin D.M., Mallison G., Poole J., Reid M.E., Thompson E.S., Ferdman B.R., Telen M.J., Anstee D.J., Tanner M.J.A. Molecular basis of reduced or absent expression of decay-accelerating factor in Cromer blood group. Blood. 84:1994;1276-1287.
27. Ewulonu U.K., Ravi L., Medof M.E. Characterization of the decay-accelerating factor gene promoter region. Proc. Natl. Acad. Sci. USA. 88:1991;4675-4679.
28. Stewart C.-B., Disotell T.R. Primate evolution - in and out of Africa. Curr. Biol. 8:1998;R582-R588.
29. Hsu E.C., Dörig R.E., Sarangi F., Marcil A., Iorio C., Richardson C.D. Artificial mutations and natural variations in the CD46 molecules from human and monkey cells define regions important for measles virus binding. J. Virol. 71:1997;6144-6154.
30. Kotwal G.J., Moss B. Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins. Nature. 335:1988;176-178.
31. Kotwal G.J., Isaacs S.N., McKenzie R., Frank M.M., Moss B. Inhibition of the complement cascade by the major secretory protein of vaccinia virus. Science. 250:1995;827-830.
32. Isaacs S.N., Kotwal G.J., Moss B. Vaccinia virus complement-control protein prevents antibody-dependent complement-enhanced neutralization of infectivity and contributes to virulence. Proc. Natl. Acad. Sci. USA. 89:1992;628-632.
33. Brodbeck W.G., Kuttner-Kondo L., Yu J., Medof M.E. XVIIth International Complement Workshop, Rhodes, Greece :1998.
34. Krych-Goldberg M., Hauhart R.E., Subramanian V.B., Yurcisin II B.M., Crimmins D.L., Hourcade D.E., Atkinson J.P. Decay accelerating activity of complement receptor type 1 (CD35). J. Biol. Chem. 274:1999;31160-31168.
35. Field M.C., Moran P., Li W., Keller G.-A., Caras I.W. Retention and degradation of proteins containing an uncleaved glycosylphosphatidylinositol signal. J. Biol. Chem. 269:1994;10830-10837.
36. Pham T., Kaul A., Hart A., Golusko P., Moulds J., Nowicki S., Lublin D.M., Nowicki B.J. dra-related X adhesins of gestational pyelonephritis-associated Escherichia coli recognize SCR-3 and SCR-4 domains of recombinant decay -accelerating factor. Infect. Immun. 63:1995;1663-1668.
37. Nowicki B., Hart A., Coyne K.E., Lublin D.M., Nowicki S. Short consensus repeat-3 domain of recombinant decay-accelerating factor is recognized by Escherichia coli recombinant Dr adhesin in a model of a cell-cell interaction. J. Exp. Med. 178:1993;2115-2121.
38. Clarkson N.A., Kaufman R., Lublin D.M., Ward T., Pipkin P.A., Minor P.D., Evans D.J., Almond J.W. Characterization of the echovirus 7 receptor: domains of CD55 critical for virus binding. J. Virol. 69:1995;5497-5501.