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. 1986 Mar 1;163(3):697–712. doi: 10.1084/jem.163.3.697

Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A

PMCID: PMC2188047  PMID: 3512759

Abstract

We report the isolation and purification of the nephritis strain- associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed that NSAP could act as a plasminogen activator; immunological investigations indicated that NSAP is antigenically different from streptokinase from group C streptococcus, and possibly represents a unique streptokinase. It is this uniqueness that may contribute to the role of NSAP in the pathogenesis of acute poststreptococcal glomerulonephritis.

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Selected References

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  1. Arroyave C. M., Müller-Eberhard H. J. Interactions between human C5, C6, and C7 and their functional significance in complement-dependent cytolysis. J Immunol. 1973 Aug;111(2):536–545. [PubMed] [Google Scholar]
  2. Brade V., Nicholson A., Bitter-Suermann D., Hadding U. Formation of the C3-cleaving properdin enzyme on zymosan. Demonstration that factor D is replaceable by proteolytic enzymes. J Immunol. 1974 Dec;113(6):1735–1743. [PubMed] [Google Scholar]
  3. Brockway W. J., Castellino F. J. A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex. Biochemistry. 1974 May 7;13(10):2063–2070. doi: 10.1021/bi00707a010. [DOI] [PubMed] [Google Scholar]
  4. DILLON H. C., Jr, WANNAMAKER L. W. PHYSICAL AND IMMUNOLOGICAL DIFFERENCES AMONG STREPTOKINASES. J Exp Med. 1965 Mar 1;121:351–371. doi: 10.1084/jem.121.3.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Elliott S. D., Dole V. P. AN INACTIVE PRECURSOR OF STREPTOCOCCAL PROTEINASE. J Exp Med. 1947 Feb 28;85(3):305–320. doi: 10.1084/jem.85.3.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gerlach D., Köhler W. Untersuchungen zur Heterogenität von Streptokinasen II. Mitteilung: Aminosäurezusammensetzung und serologische Aktivitt. Zentralbl Bakteriol Orig A. 1979 Jul;244(2-3):210–221. [PubMed] [Google Scholar]
  7. Gerlach D., Köhler W. Untersuchungen zur Heterogenität von Streptokinasen verschiedener Herkunft. Zentralbl Bakteriol Orig A. 1977 Jul;238(3):336–349. [PubMed] [Google Scholar]
  8. Hamilton J. A., Zabriskie J. B., Lachman L. B., Chen Y. S. Streptococcal cell walls and synovial cell activation. Stimulation of synovial fibroblast plasminogen activator activity by monocytes treated with group A streptococcal cell wall sonicates and muramyl dipeptide. J Exp Med. 1982 Jun 1;155(6):1702–1718. doi: 10.1084/jem.155.6.1702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hiles R. A., Henderson L. M. The partial purification and properties of hydroxylysine kinase from rat liver. J Biol Chem. 1972 Feb 10;247(3):646–651. [PubMed] [Google Scholar]
  10. Houba V., Hána I. The difference in immunological characteristics of two streptokinases. Immunology. 1966 Oct;11(4):387–397. [PMC free article] [PubMed] [Google Scholar]
  11. Jackson K. W., Esmon N., Tang J. Streptokinase and staphylokinase. Methods Enzymol. 1981;80(Pt 100):387–394. doi: 10.1016/s0076-6879(81)80033-x. [DOI] [PubMed] [Google Scholar]
  12. Jackson K. W., Tang J. Complete amino acid sequence of streptokinase and its homology with serine proteases. Biochemistry. 1982 Dec 21;21(26):6620–6625. doi: 10.1021/bi00269a001. [DOI] [PubMed] [Google Scholar]
  13. Kaplan A. P., Austen K. F. A prealbumin activator of prekallikrein. II. Derivation of activators of prekallikrein from active Hageman factor by digestion with plasmin. J Exp Med. 1971 Apr 1;133(4):696–712. doi: 10.1084/jem.133.4.696. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kluthe R. Ten years clinical nephrology. Clin Nephrol. 1983 Jan;19(1):1–2. [PubMed] [Google Scholar]
  15. LIU T. Y., ELLIOTT S. D. STREPTOCOCCAL PROTEINASE: THE ZYMOGEN TO ENZYME TRANSFROMATION. J Biol Chem. 1965 Mar;240:1138–1142. [PubMed] [Google Scholar]
  16. 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]
  17. Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
  18. Manjula B. N., Acharya A. S., Mische S. M., Fairwell T., Fischetti V. A. The complete amino acid sequence of a biologically active 197-residue fragment of M protein isolated from type 5 group A streptococci. J Biol Chem. 1984 Mar 25;259(6):3686–3693. [PubMed] [Google Scholar]
  19. McCluskey R. T., Vassalli P., Gallo G., Baldwin D. S. An immunofluorescent study of pathogenic mechanisms in glomerular diseases. N Engl J Med. 1966 Mar 31;274(13):695–701. doi: 10.1056/NEJM196603312741301. [DOI] [PubMed] [Google Scholar]
  20. Morgan F. J., Henschen A. The structure of streptokinase. I. Cyanogen bromide fragmentation, amino acid composition and partial amino acid sequences. Biochim Biophys Acta. 1969 May;181(1):93–104. doi: 10.1016/0005-2795(69)90230-x. [DOI] [PubMed] [Google Scholar]
  21. Ohkuni H., Friedman J., van de Rijn I., Fischetti V. A., Poon-King T., Zabriskie J. B. Immunological studies of post-streptococcal sequelae: serological studies with an extracellular protein associated with nephritogenic streptococci. Clin Exp Immunol. 1983 Oct;54(1):185–193. [PMC free article] [PubMed] [Google Scholar]
  22. Ratnoff O. D., Naff G. B. The conversion of C'IS to C'1 esterase by plasmin and trypsin. J Exp Med. 1967 Feb 1;125(2):337–358. doi: 10.1084/jem.125.2.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. SEEGAL B. C., ANDRES G. A., HSU K. C., ZABRISKIE J. B. STUDIES ON THE PATHOGENESIS OF ACUTE AND PROGRESSIVE GLOMERULONEPHRITIS IN MAN BY IMMUNOFLUORESCEIN AND IMMUNOFERRITIN TECHNIQUES. Fed Proc. 1965 Jan-Feb;24:100–108. [PubMed] [Google Scholar]
  24. SHEDLOVSKY T., ELLIOTT S. D. An electrophoretic study of a streptococcal proteinase and its precursor. J Exp Med. 1951 Nov;94(5):363–372. doi: 10.1084/jem.94.5.363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stollerman G. H. Rheumatogenic and nephritogenic streptococci. Circulation. 1971 Jun;43(6):915–921. doi: 10.1161/01.cir.43.6.915. [DOI] [PubMed] [Google Scholar]
  26. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Villarreal H., Jr, Fischetti V. A., van de Rijn I., Zabriskie J. B. The occurrence of a protein in the extracellular products of streptococci isolated from patients with acute glomerulonephritis. J Exp Med. 1979 Feb 1;149(2):459–472. doi: 10.1084/jem.149.2.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. 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]
  29. WEINSTEIN L. Antigenic dissimilarity of streptokinases. Proc Soc Exp Biol Med. 1953 Aug-Sep;83(4):689–691. doi: 10.3181/00379727-83-20460. [DOI] [PubMed] [Google Scholar]
  30. Zabriskie J. B. The role of streptococci in human glomerulonephritis. J Exp Med. 1971 Sep 1;134(3):180–192. [PMC free article] [PubMed] [Google Scholar]
  31. 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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