A common site within factor H SCR 7 responsible for binding heparin, C-reactive protein and streptococcal M protein

European Journal of Immunology

Volumn 33, Issue 4, 2003, Pages 962-969

  Giannakis, Eleni ^a   Jokiranta, T Sakari ^a,b   Male, Dean A ^a   Ranganathan, Shoba ^c   Ormsby, Rebecca J ^a   Fischetti, Vince A ^d   Mold, Carolyn ^e   Gordon, David L ^a  

^a FLINDERS MEDICAL CENTRE   (Australia)

^b HELSINKI UNIVERSITY CENTRAL HOSPITAL   (Finland)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^d ROCKEFELLER UNIVERSITY   (United States)

^e UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE   (United States)

Author keywords

Alternative pathway; Complement; Streptococcus

Indexed keywords

ALANINE; BACTERIAL PROTEIN; C REACTIVE PROTEIN; COMPLEMENT FACTOR H; HEPARIN; LIGAND; M PROTEIN; VIRUS PROTEIN;

AMINO ACID SUBSTITUTION; COMPUTER MODEL; CONSENSUS SEQUENCE; CONTROLLED STUDY; DNA TEMPLATE; ENZYME LINKED IMMUNOSORBENT ASSAY; GENE CONSTRUCT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SEQUENCE HOMOLOGY; STREPTOCOCCUS; SURFACE CHARGE; VACCINIA VIRUS;

AMINO ACID SUBSTITUTION; ANTIGENS, BACTERIAL; BACTERIAL OUTER MEMBRANE PROTEINS; BINDING SITES; C-REACTIVE PROTEIN; CARRIER PROTEINS; COMPLEMENT FACTOR H; HEPARIN; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; REPETITIVE SEQUENCES, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 0038068044     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200323541     Document Type: Review

References (55)

1. Fearon, D. T. and Austen, K. F., Activation of the alternative complement pathway with rabbit erythrocytes by circumvention of the regulatory action of endogenous control proteins. J. Exp. Med. 1977. 146: 22-33.
2. Fearon, D. T. and Austen, K. F., Activation of the alternative complement pathway due to resistance of zymosan-bound amplification convertase to endogenous regulatory mechanisms. Proc. Natl. Acad. Sci. USA 1977. 74: 1683-1687.
3. Kazatchkine, M. D., Fearon, D. T. and Austen, K. F., Human alternative complement pathway: membrane associated sialic acid regulates the competition between B and beta 1H for cell-bound C3b. J. Immunol. 1979. 122:75-81.
4. Meri, S. and Pangburn, M. K., Discrimination between activators and non-activators of the alternative pathway of complement regulation via sialic acid/polyanion binding site on fH. Proc. Natl. Acad Sci. USA 1990. 87: 3982-3986.
5. Volanakis, J. E. and Wirtz, K. W., Interaction of C-reactive protein with artificial phosphatidylcholine bilayers. Nature 1979. 281: 155-157.
6. Li, Y. P., Mold, C. and Du Clos, T. W., Sublytic complement attack exposes C-reactive protein binding sites on cell membranes. J. Immunol. 1994. 152: 2995-3005.
7. Du Clos, T. W., The interaction of C-reactive protein and serum amyloid P component with nuclear antigens. Mol. Biol. Rep. 1996. 23: 253-260.
8. Hack, C. E., Wolbink, G. J., Schalkwijk, C., Speijer, H., Hermens, W. T. and van den Bosch, H., A role for secretory phospholipase A2 and C-reactive protein in the removal of injured cells. Immunol. Today 1997. 18: 111-115.
9. Kaplan, M. H. and Volanakis, J. E., Interactions of the C-reactive protein complexes with the complement system. I. Consumption of human complement associated with the reaction of C-reactive protein with pneumococcal C polysaccharide and with choline phophatides, lecithin and sphingomyelin. J. Immunol. 1974. 112: 2135-2147.
10. Mold, C., Kingzette, M. and Gewurz, H., C-reactive protein inhibits pneumococcal activation of the alternative pathway by increasing the interaction between factor H and C3b. J. Immunol. 1984. 133: 882-885.
11. Berman, S., Gewürz, H. and Mold, C., Binding of C-reactive protein to nucleated cells leads to complement activation without cytolysis. J. Immunol. 1986. 136: 1354-1359.
12. Mold, C. and Gewürz, H., Inhibitory effect of C-reactive protein on alternative C pathway activation by liposomes and Streptococcus pneumoniae. J. Immunol. 1981. 127: 2089-2092.
13. Aronen, M., Lehto, T. and Meri, S., Regulation of the alternative pathway complement activation by an interaction of C-reactive protein with factor H. Immunol. Infect. Dis. 1993. 3: 83-87.
14. Jarva, H., Jokiranta, T. S., Hellwage, J., Zipfel, P. F. and Meri, S., Regulation of complement activation by C-reactive protein: Targeting the complement regulatory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11. J. Immunol. 1999. 163: 3957-3962.
15. Mold, C., Gewürz, H. and Du Clos, T. W., Regulation of complement activation by C-reactive protein. Immunopharmacology 1999. 42: 23-30.
16. Bisno, A. L. and Stevens, D. L., Streptococcal infections of skin and soft tissue. N. Engl. J. Med. 1996. 334: 240-245.
17. Curtis, N., Invasive group A streptococcal infections. Curr. Opin. Infect. Dis. 1996. 9: 191-202.
18. Horstmann, R. D., Sievertsen, H. J., Knobloch, J. and Fischetti, V. A., Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc. Natl. Acad. Sci. USA 1988. 88: 1657-1661.
19. Johnsson, E., Berggård, K., Kotarsky, H., Hellwage, J., Zipfel, P. F., Sjöbring, U. and Lindahl, G., Role of the hypervariable region in streptococcal M proteins: Binding of human complement inhibitor. J. Immunol. 1998. 161: 4894-4901.
20. Kotarsky, H., Hellwage, J., Johnson, E., Skerka, C., Svensson, H. G., Lindahl, G., Söbring, U. and Zipfel, P. F., Identification of a domain in human factor H and factor H-like protein 1 required for interaction with streptococcal M protein. J. Immunol. 1998. 160: 3349-3354.
21. Campbell, D. R., Law, S. K., Reid, K. B. and Sim, R. B., Structure, organization and regulation of the complement genes. Annu. Rev. Immunol. 1988. 6: 161-195.
22. Perkins, S. J., Haris, P. I., Sim, R. B. and Chapman, D. D., A study of the structure of human complement component factor H by fourier transform infrared spectroscopy and secondary structure averaging. Biochemistry 1988. 27: 4004-4012.
23. DiScipio, R. G., Ultrastructures and interactions of complement factor H and I. J. Immunol. 1992. 149: 2592-2599.
24. Barlow, P. N., Norman, D. G., Steinkasserer, A., Horne, T. J., Pearce, J., Driscoll, P. C., Sim, R. B. and Campbell, I. P., Solution structure of the fifth repeat of factor H: a second example of the complement control protein module. Biochemistry 1992. 31: 3626-3634.
25. Ripoche, J., Day, A. J., Harris, T. J. R. and Sim, R. B., The complete amino acid sequence of human complement factor H. Biochem. J. 1988. 249: 593-602.
26. Zipfel, P. F., Jokiranta, T. S., Hellwage, J., Koistinen, V. and Meri, S., The factor H protein family. Immunopharmacology 1999. 42: 53-60.
27. Gordon, D. L., Kaufman, R. M., Blackmore, T. K., Kwong, J. and Lublin, D. M., Identification of complement regulatory domains in human factor H. J. Immunol. 1995. 155: 348-356.
28. Blackmore, T. K., Sadlon, T. A., Ward, H. M., Lublin, D. M. and Gordon, D. L., Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H. J. Immunol. 1996. 157: 5422-5427.
29. Blackmore, T. K., Hellwage, J., Sadlon, T. A., Higgs, N., Zipfel, P. F., Ward, H. M. and Gordon, D. L., Identification of the second heparin binding domain in human complement factor H. J. Immunol. 1998. 160: 3342-3348.
30. Sharma, A. K. and Pangburn, M. K., Localization by site directed mutagenesis of the site in human complement factor H that binds to Streptococcus pyogenes M protein. Infect. Immun. 1997. 65: 484-487.
31. Blackmore, T. K., Fischetti, V. A., Higgs, N. H., Sadlon, T. A., Ward, H. M and Gordon, D. L., M protein of group A streptococcus binds to the seventh short consensus repeat of the human complement factor H. Infect. Immun. 1998. 66: 1427-1431.
32. Perez-Caballero, D., Alberti, S., Vivanco, F., Sanchez-Corral, P. and Rodriguez de Cordoba, S., Assessment of the interaction of human complement regulatory proteins with group A streptococcus. Identification of a high affinity group A streptococcus binding site in FHL-1. Eur. J. Immunol. 2000. 30: 1243-1253.
33. Barlow, P. N., Steinkasserer, A., Norman, D. G., Keifer, B., Wiles, A. P., Sim, R. B. and Campbell, I. D., Solution structure of a pair of complement modules by nuclear magnetic resonance. J. Mol. Biol. 1993. 232: 268-284.
34. Wiles, A. P., Shaw, G., Bright, J., Perczel, A., Campbell, I. D. and Barlow, P. N., NMR studies of a viral protein that mimics the regulators of complement activation. J. Mol. Biol. 1997. 272: 253-265.
35. Ranganathan, S., Male, D. A., Ormsby, R. J., Giannakis, E. and Gordon, D. L., Pinpointing the putative heparin/sialic-binding residues in the 'sushi' domain 7 of factor H: a molecular modeling study. Pac. Symp. Biocomputing 2000. 5: 152-164.
36. Fromm, J. R., Hileman, R. E., Caldwell, E. E., Weiler, J. M. and Lindhardt, R. J., Pattern and spacing of basic amino acids in heparin binding sites. Arch. Biochem. Biophys. 1997. 343: 92-100.
37. Norman, D. G., Barlow, P. N., Baron, M., Day, A. J., Sim, R. B. and Campbell, I. D., Three-dimensional structure of a complement control protein module in solution. J. Mol. Biol. 1991. 219: 717-725.
38. Barlow, P. N., Baron, M., Norman, D. G., Day, A. J., Willis, A. C., Sim, R. B. and Campbell, I. D., Secondary structure of a complement control protein module by two-dimensional 1H NMR. Biochemistry 1991. 30: 997-1004.
39. Villoutreix, B. O., Hardig, Y., Wallqvist, A., Covell, D. G., Garcia de Frutos, P. and Dahlback, B., Structural investigation of C4b-binding protein by molecular modeling: localization of putative binding sites. Proteins 1998. 31: 391-405.
40. Villoutreix, B. O., Blom, A. M., Webb, J. and Dahlback, B., The complement regulator C4b-binding protein analyzed by molecular modeling, bioinformatics and computer-aided experimental design. Immunopharmacology 1999. 42: 121-134.
41. Blom, A. M., Berggård, K., Webb, J. H., Lindahl, G., Villoutreix, B. O. and Dahlbåck, B., Human C4b-binding protein has overlapping, but not identical, binding sites for C4b and streptococcal M proteins. J. Immunol. 2000. 164: 5328-5336.
42. Pangburn, M. K., Cutting edge: localisation of the host recognition functions of complement factor H at the carboxyl-terminal: implications for hemolytic uremic syndrome. J. Immunol. 2002. 169: 4702-4706.
43. Perez-Caballero, D., Gonzalez-Rubio, C., Gallardo, M. E., Vera, M., Lopez-Trascasa, M., Rodriguez de Cardoba, S. and Sanchez-Corral, P., Clustering of missense mutations in the C-terminal region of factor H in atypical hemolytic uremic syndrome. Am. J. Hum. Genet. 2001. 68: 478-484.
44. Richards, A., Buddles, M. R. H., Donne, R. L., Kaplan, B. S., Kirk, E., Venning, M. C., Tielemans, C. L., Goodship, J. A. and Goodship, T. H., Factor H mutations in hemolytic uremic syndrome cluster in exons 18-20, a domain important for host cell recognition. Am. J. Hum. Genet. 2001. 68: 485-490.
45. Giannakis, E., Jokiranta, T. S., Ormsby, R. J., Male, D. A., Christiansen, D., Fischetti, V. A., Bagley, C., Loveland, B. E. and Gordon, D. L., Identification of the streptococcal M protein binding site on membrane cofactor protein (CD46). J. Immunol. 2002, 168: 4585-4592.
46. Liszewski, M. K., Leung, M., Cui, W., Subramanian, V. B., Parkinson, J., Barlow, P. N., Manchester, M. and Atkinson, J. P., Dissecting sites important for complement regulatory activity in membrane cofactor protein (MCP; CD46). J. Biol. Chem. 2000. 275: 37692-37701.
47. Srinivasan, N., White, H. E., Emsley, J., Wood, S. P., Pepys, M. B. and Blundell, T. L., Comparative analyses of pentraxins: implications for protomer assembly and ligand binding. Structure 1994. 2: 1017-1027.
48. Shrive, A. K., Cheetham, G. M., Holden, D., Myles, D. A., Turnell, W. G., Volanakis, J. E., Pepys, M. B., Bloomer, A. C. and Greenhough, T. J., Three dimensional structure of human C-reactive protein. Nat. Struct. Biol. 1996. 3: 346-354.
49. Thompson, D., Pepys, M. B. and Wood, S. P., The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure Fold. Des. 1999. 7: 169-177.
50. Nicholls, A., Sharp, K. A. and Honig., B., Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991. 11: 281-296.
51. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N. and Bourne, P. E., The Protein Data Bank. Nucleic Acids Res. 2000. 28: 235-242.
52. Fischetti, V. A., Jones, K. F., Manjula, B. N. and Scott, J. R., Streptococcal M6 protein expressed in Escherichia coli. Localization, purification, and comparison with streptococcal-derived M protein. J. Exp. Med. 1984. 159: 1083-1095.
53. Du Clos, T. W., Zlock, L. T. and Marnell, L., Definition of a C-reactive protein binding determinant on histones. J. Biol. Chem. 1991. 266: 2167-2171.
54. Scott, J. R., Guenthner, P. C., Malone, L. M. and Fischetti, V. A., Conversion of an M-group A streptococcus to M+ by transfer of a plasmid containing an M6 gene. J. Exp. Med. 1986. 164: 1641-1651.
55. Caparon, M. G., Geist, R. T., Perez-Casal, J. and Scott, J. R., Environmental regulation of virulence in group A streptococci: transcription of the gene encoding M protein is stimulated by carbon dioxide. J. Bacteriol. 1992. 174: 5693-5701.