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. 1993 Aug;61(8):3259–3264. doi: 10.1128/iai.61.8.3259-3264.1993

Isolation and characterization of a Streptococcus pyogenes protein that binds to basal laminae of human cardiac muscle.

B D Winters 1, N Ramasubbu 1, M W Stinson 1
PMCID: PMC280997  PMID: 8335359

Abstract

A 9-kDa glycosaminoglycan-binding protein (GAG-BP) was isolated from Streptococcus pyogenes and purified to homogeneity by affinity chromatography on heparin-agarose. The protein selectively bound to the basal laminae of human cardiac muscle and had an apparent dissociation constant of 2.5 x 10(-7) M. Chemical analyses indicated that the GAG-BP was rich in alanine, lysine, and arginine (pI 9.5) and devoid of tyrosine, methionine, histidine, and half-cystine. There were no detectable carbohydrate or phosphate substituents. The amino acid sequence of the N terminus of GAG-BP showed homology with those of histone-like DNA-binding proteins of several other bacteria. Circular dichroism spectroscopy indicated that the protein was made up of 50% beta-sheet and 50% beta-turn and random coil in aqueous solution; however, when the protein complexed with heparin, it adopted a more ordered structure containing 25% alpha-helix, 50% beta-sheet, and 25% beta-turn and random coil. The GAG-BP cross-reacted serologically with a component of similar size in extracts of other group A streptococci and was present in the culture medium during late logarithmic growth.

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Selected References

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  1. Bergey E. J., Stinson M. W. Heparin-inhibitable basement membrane-binding protein of Streptococcus pyogenes. Infect Immun. 1988 Jul;56(7):1715–1721. doi: 10.1128/iai.56.7.1715-1721.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  3. Choi S. H., Stinson M. W. Binding of a Streptococcus mutans cationic protein to kidney in vitro. Infect Immun. 1991 Feb;59(2):537–543. doi: 10.1128/iai.59.2.537-543.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Choi S. H., Stinson M. W. Purification of a Streptococcus mutans protein that binds to heart tissue and glycosaminoglycans. Infect Immun. 1989 Dec;57(12):3834–3840. doi: 10.1128/iai.57.12.3834-3840.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cronin W., Deol H., Azadegan A., Lange K. Endostreptosin: isolation of the probable immunogen of acute post-streptococcal glomerulonephritis (PSGN). Clin Exp Immunol. 1989 May;76(2):198–203. [PMC free article] [PubMed] [Google Scholar]
  6. De Scheerder I., Wulfrank D., Van Renterghem L., Sabbe L., Robbrecht D., Clement D., Derom F., Plum J., Verdonk G. Association of anti-heart antibodies and circulating immune complexes in the post-pericardiotomy syndrome. Clin Exp Immunol. 1984 Aug;57(2):423–428. [PMC free article] [PubMed] [Google Scholar]
  7. Fillit H., Damle S. P., Gregory J. D., Volin C., Poon-King T., Zabriskie J. Sera from patients with poststreptococcal glomerulonephritis contain antibodies to glomerular heparan sulfate proteoglycan. J Exp Med. 1985 Feb 1;161(2):277–289. doi: 10.1084/jem.161.2.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Glurich I., Winters B., Albini B., Stinson M. Identification of Streptococcus pyogenes proteins that bind to rabbit kidney in vitro and in vivo. Microb Pathog. 1991 Mar;10(3):209–220. doi: 10.1016/0882-4010(91)90055-f. [DOI] [PubMed] [Google Scholar]
  9. Hol W. G., van Duijnen P. T., Berendsen H. J. The alpha-helix dipole and the properties of proteins. Nature. 1978 Jun 8;273(5662):443–446. doi: 10.1038/273443a0. [DOI] [PubMed] [Google Scholar]
  10. Imber R., Kimura M., Groch N., Heinemann U. DNA-binding properties and primary structure of HB protein from Bacillus globigii. Eur J Biochem. 1987 Jun 15;165(3):547–552. doi: 10.1111/j.1432-1033.1987.tb11474.x. [DOI] [PubMed] [Google Scholar]
  11. Johnston K. H., Zabriskie J. B. Purification and partial characterization of the nephritis strain-associated protein from Streptococcus pyogenes, group A. J Exp Med. 1986 Mar 1;163(3):697–712. doi: 10.1084/jem.163.3.697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kefalides N. A., Pegg M. T., Ohno N., Poon-King T., Zabriskie J., Fillit H. Antibodies to basement membrane collagen and to laminin are present in sera from patients with poststreptococcal glomerulonephritis. J Exp Med. 1986 Mar 1;163(3):588–602. doi: 10.1084/jem.163.3.588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Khanaka H., Laine B., Sautiere P., Guillaume J. Characterization and primary structures of DNA-binding HU-type proteins from Rhizobiaceae. Eur J Biochem. 1985 Mar 1;147(2):343–349. doi: 10.1111/j.1432-1033.1985.tb08755.x. [DOI] [PubMed] [Google Scholar]
  14. Kimura M., Wilson K. S. On the DNA binding protein II from Bacillus stearothermophilus. II. The amino acid sequence and its relation to those of homologous proteins from other prokaryotes. J Biol Chem. 1983 Mar 25;258(6):4007–4011. [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Laine B., Belaiche D., Sautiere P., Biserte G. Characterization and structural study of the DNA-binding protein HRm From Rhizobium meliloti. Biochem Biophys Res Commun. 1982 May 14;106(1):101–107. doi: 10.1016/0006-291x(82)92063-0. [DOI] [PubMed] [Google Scholar]
  17. Lange K., Seligson G., Cronin W. Evidence for the in situ origin of poststreptococcal glomerulonephritis: glomerular localization of endostreptosin and the clinical significance of the subsequent antibody response. Clin Nephrol. 1983 Jan;19(1):3–10. [PubMed] [Google Scholar]
  18. Leon O., Panos C. An electron microscope study of kidney basement membrane changes in the mouse by lipoteichoic acid from Streptococcus pyogenes. Can J Microbiol. 1987 Aug;33(8):709–717. doi: 10.1139/m87-124. [DOI] [PubMed] [Google Scholar]
  19. Makino H., Gibbons J. T., Reddy M. K., Kanwar Y. S. Nephritogenicity of antibodies to proteoglycans of the glomerular basement membrane--I. J Clin Invest. 1986 Jan;77(1):142–156. doi: 10.1172/JCI112269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Morrissey J. H. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem. 1981 Nov 1;117(2):307–310. doi: 10.1016/0003-2697(81)90783-1. [DOI] [PubMed] [Google Scholar]
  21. Ozols J. Amino acid analysis. Methods Enzymol. 1990;182:587–601. doi: 10.1016/0076-6879(90)82046-5. [DOI] [PubMed] [Google Scholar]
  22. Seligson G., Lange K., Majeed H. A., Deol H., Cronin W., Bovie R. Significance of endostreptosin antibody titers in poststreptococcal glomerulonephritis. Clin Nephrol. 1985 Aug;24(2):69–75. [PubMed] [Google Scholar]
  23. Stinson M. W., Bergey E. J. Isolation of heart- and kidney-binding protein from group A streptococci. Infect Immun. 1982 Jan;35(1):335–342. doi: 10.1128/iai.35.1.335-342.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Swartzwelder F. J., Barua P. K., Albini B., Stinson M. W. Heart-reactive antibodies in rabbit anti-Streptococcus mutans sera fail to cross-react with Streptococcus mutans. J Immunol. 1988 Feb 1;140(3):954–961. [PubMed] [Google Scholar]
  25. Tanaka I., Appelt K., Dijk J., White S. W., Wilson K. S. 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature. 1984 Aug 2;310(5976):376–381. doi: 10.1038/310376a0. [DOI] [PubMed] [Google Scholar]
  26. Tomlinson K., Leon O., Panos C. Morphological changes and pathology of mouse glomeruli infected with a streptococcal L-form or exposed to lipoteichoic acid. Infect Immun. 1983 Dec;42(3):1144–1151. doi: 10.1128/iai.42.3.1144-1151.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Vogt A., Batsford S., Rodríguez-Iturbe B., García R. Cationic antigens in poststreptococcal glomerulonephritis. Clin Nephrol. 1983 Dec;20(6):271–279. [PubMed] [Google Scholar]
  28. van de Rijn I., Kessler R. E. Growth characteristics of group A streptococci in a new chemically defined medium. Infect Immun. 1980 Feb;27(2):444–448. doi: 10.1128/iai.27.2.444-448.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]

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