Abstract
An extracellular product of group A streptococci which induces lymphocyte blastogenesis has been purified to homogeneity by DEAE- cellulose and CM-cellulose chromatography. The protein, termed streptococcal blastogen A, has a mol wt of approximately or equal to 17,500 and is inactivated by protease treatment and by heating at 100 degrees C. The purified blastogen gave rise to multiple protein bands on nondenaturing polyacrylamide gel electrophoresis, only two of which possessed blastogenic activity. Treatment of the protein with dithiothreitol before electrophoresis resulted in the apparent conversion of the multiple forms to a single active species. Blastogen A differs in electrophoretic mobility from the streptococcal pyrogenic exotoxins and its lymphocyte stimulating activity is not inhibited by rabbit antisera to the exotoxins. An enzyme immunoassay has been developed to measure human antibodies against blastogen A. A selection of sera with varying levels of anti-DNase B contained antiblastogen A- IgG.
Full Text
The Full Text of this article is available as a PDF (751.9 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Barsumian E. L., Cunningham C. M., Schlievert P. M., Watson D. W. Heterogeneity of group A streptococcal pyrogenic exotoxin type B. Infect Immun. 1978 May;20(2):512–518. doi: 10.1128/iai.20.2.512-518.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cunningham C. M., Barsumian E. L., Watson D. W. Further purification of group A streptococcal pyrogenic exotoxin and characterization of the purified toxin. Infect Immun. 1976 Sep;14(3):767–775. doi: 10.1128/iai.14.3.767-775.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- Engvall E., Perlmann P. Enzyme-linked immunosorbent assay, Elisa. 3. Quantitation of specific antibodies by enzyme-labeled anti-immunoglobulin in antigen-coated tubes. J Immunol. 1972 Jul;109(1):129–135. [PubMed] [Google Scholar]
- GELL P. G., BENACERRAF B. Studies on hypersensitivity. II. Delayed hypersensitivity to denatured proteins in guinea pigs. Immunology. 1959 Jan;2(1):64–70. [PMC free article] [PubMed] [Google Scholar]
- Greenberg L. J., Gray E. D., Yunis E. J. Association of HL-A 5 and immune responsiveness in vitro to streptococcal antigens. J Exp Med. 1975 May 1;141(5):935–943. doi: 10.1084/jem.141.5.935. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Holbrook I. B., Leaver A. G. A procedure to increase the sensitivity of staining by Coomassie brilliant blue G250-perchloric acid solution. Anal Biochem. 1976 Oct;75(2):634–636. doi: 10.1016/0003-2697(76)90118-4. [DOI] [PubMed] [Google Scholar]
- Marker S. C., Gray E. D. Simple method for the preparation of streptococcal nucleases. Appl Microbiol. 1972 Feb;23(2):368–371. doi: 10.1128/am.23.2.368-371.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mathiesen L. R., Feinstone S. M., Wong D. C., Skinhoej P., Purcell R. H. Enzyme-linked immunosorbent assay for detection of hepatitis A antigen in stool and antibody to hepatitis A antigen in sera: comparison with solid-phase radioimmunoassay, immune electron microscopy, and immune adherence hemagglutination assay. J Clin Microbiol. 1978 Feb;7(2):184–193. doi: 10.1128/jcm.7.2.184-193.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nauciel C., Blass J., Mangalo R., Raynaud M. Evidence for two molecular forms of streptococcal erythrogenic toxin. Conversion to a single form by 2-mercaptoethanol. Eur J Biochem. 1969 Nov;11(1):160–164. doi: 10.1111/j.1432-1033.1969.tb00754.x. [DOI] [PubMed] [Google Scholar]
- Nelson J., Ayoub E. M., Wannamaker L. W. Streptococcal anti-desoxyribonuclease B: microtechnique determination. J Lab Clin Med. 1968 May;71(5):867–873. [PubMed] [Google Scholar]
- Petermann F., Knöll H., Köhler W. Untersuchungen zur Mitogenität erythrogener Toxine. I. Typenspezifische Hemmung der mitogenen Aktivität erythrogener Toxine durch antitoxische Seren von Kaninchen. Zentralbl Bakteriol Orig A. 1978 Apr;240(3):366–379. [PubMed] [Google Scholar]
- Plate J. M., Amos B. Lymphocyte stimulation by a glycopeptide isolated from Streptococcus pyogenes C203S. I. Isolation and partial purification. Cell Immunol. 1970 Nov;1(5):476–487. doi: 10.1016/0008-8749(70)90036-5. [DOI] [PubMed] [Google Scholar]
- Plate J. M., Amos B. Lymphocyte stimulation by a glycopeptide isolated from Streptococcus pyogenes C203S. II. Kinetics of the response. Cell Immunol. 1970 Nov;1(5):488–499. doi: 10.1016/0008-8749(70)90037-7. [DOI] [PubMed] [Google Scholar]
- Schlievert P. M., Bettin K. M., Watson D. W. Purification and characterization of group A streptococcal pyrogenic exotoxin type C. Infect Immun. 1977 May;16(2):673–679. doi: 10.1128/iai.16.2.673-679.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Seravalli E., Taranta A. Lymphocyte transformation and macrophage migration inhibition by electrofocused and gel-filtered fractions of group A streptococcal filtrate. Cell Immunol. 1974 Dec;14(3):366–375. doi: 10.1016/0008-8749(74)90186-5. [DOI] [PubMed] [Google Scholar]
- Taylor A. G. Lymphocyte-transforming activity of streptococci belonging to various Lancefield groups. J Med Microbiol. 1972 Feb;5(1):61–65. doi: 10.1099/00222615-5-1-61. [DOI] [PubMed] [Google Scholar]
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]