Abstract
As evidenced by precipitin analysis with pooled human gamma globulin, at least 12 distinct antigens were produced in cultures by one strain of Group A streptococcus (C203S). It was suggested on this basis, that these antigens were produced in vivo during human infections. By the combined use of continuous flow electrophoresis on paper curtains, and column chromatography with calcium phosphate gels, five of these have been isolated in a probable high state of purity. One of the components was obtained from culture filtrates of a Group C streptococcal strain. Three of the purified antigens have been tentatively identified as streptolysin "O", diphosphopyridinenucleotidase, and proteinase precursor. The latter could be very readily crystallized, and appears "identical" with that described by Elliott. The DPNase was of extremely high potency, 1 mg. being capable of destroying 12.6 gm. of DPN in 7½ minutes at 37°C. The identity of the other two components is uncertain as yet. They are distinct from each other and the above products immunologically, and are not related to the "C" carbohydrate. The applicability of these methods for the analysis of infectious diseases generally was discussed.
Full Text
The Full Text of this article is available as a PDF (2.1 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BERNHEIMER A. W., CARLSON A. S., KELLNER A. Selective inhibition by preparations of streptococcal filtrates of the oxidative metabolism of mitochondria procured from rabbit myocardium. J Exp Med. 1956 Oct 1;104(4):577–587. doi: 10.1084/jem.104.4.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BERNHEIMER A. W., LAZARIDES P. D., WILSON A. T. Diphosphopyridine nucleotidase as an extracellular product of streptococcal growth and its possible relationship to leukotoxicity. J Exp Med. 1957 Jul 1;106(1):27–37. doi: 10.1084/jem.106.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CARLSON A. S., KELLNER A., BERNHEIMER A. W., FREEMAN E. B. A streptococcal enzyme that acts specifically upon diphosphopyridine nucleotide: characterization of the enzyme and its separation from streptolysin O. J Exp Med. 1957 Jul 1;106(1):15–26. doi: 10.1084/jem.106.1.15. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ELLIOTT S. D. The crystallization and serological differentiation of a streptococcal proteinase and its precursor. J Exp Med. 1950 Sep;92(3):201–218. doi: 10.1084/jem.92.3.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elliott S. D. A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN. J Exp Med. 1945 Jun 1;81(6):573–592. doi: 10.1084/jem.81.6.573. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GISPEN R. Analysis of pox-virus antigens by means of double diffusion: a method for direct serological differentiation of cowpox. J Immunol. 1955 Feb;74(2):134–141. [PubMed] [Google Scholar]
- GRABAR P. Agar-gel diffusion and immunoelectrophoretic analysis. Ann N Y Acad Sci. 1957 Dec 16;69(4):591–607. doi: 10.1111/j.1749-6632.1957.tb49699.x. [DOI] [PubMed] [Google Scholar]
- HALBERT S. P., SWICK L., SONN C. The use of precipitin analysis in agar for the study of human streptococcal infections. I. Oudin technic. J Exp Med. 1955 May 1;101(5):539–556. doi: 10.1084/jem.101.5.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HALBERT S. P., SWICK L., SONN C. The use of precipitin analysis in agar for the study of human streptococcal infections. II. Ouchterlony and Oakley technics. J Exp Med. 1955 May 1;101(5):557–576. doi: 10.1084/jem.101.5.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HARRIS T. N., HARRIS S., OGBURN C. A. Gel-precipitation of streptococcal culture supernates with sera of patients with rheumatic fever and streptococcal infection. Proc Soc Exp Biol Med. 1955 Oct;90(1):39–45. doi: 10.3181/00379727-90-21933. [DOI] [PubMed] [Google Scholar]
- HJERTEN S., LEVIN O., TISELIUS A. Protein chromatography on calcium phosphate columns. Arch Biochem Biophys. 1956 Nov;65(1):132–155. doi: 10.1016/0003-9861(56)90183-7. [DOI] [PubMed] [Google Scholar]
- KAPLAN N. O., COLOWICK S. P., NASON A. Neurospora diphosphopyridine nucleotidase. J Biol Chem. 1951 Aug;191(2):473–483. [PubMed] [Google Scholar]
- LAZARIDES P. D., BERNHEIMER A. W. Association of production of diphosphopyridine nucleotidase with serological type of group A Streptococcus. J Bacteriol. 1957 Sep;74(3):412–413. doi: 10.1128/jb.74.3.412-413.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LIEF F. S., FABIYI A., HENLE W. Antigenic analyses of influenza viruses by complement fixation. I. The production of antibodies to the soluble antigen in guinea pigs. J Immunol. 1958 Jan;80(1):53–65. [PubMed] [Google Scholar]
- McCARTY M. The inhibition of streptococcal desoxyribonuclease by rabbit and human antisera. J Exp Med. 1949 Dec;90(6):543–553. doi: 10.1084/jem.90.6.543. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'CONNOR G. R. Precipitating antibody to toxoplasma; a follow-up study on findings in the blood and aqueous humor. Am J Ophthalmol. 1957 Oct;44(4 Pt 2):75–85. [PubMed] [Google Scholar]
- OUCHTERLONY O. Antigen-antibody reactions in gels. Acta Pathol Microbiol Scand. 1949;26(4):507–515. doi: 10.1111/j.1699-0463.1949.tb00751.x. [DOI] [PubMed] [Google Scholar]
- STOCK A. H., VERNEY E. Properties of scarlet fever toxin of the NY5 strain. J Immunol. 1952 Oct;69(4):373–378. [PubMed] [Google Scholar]
- TANAKA C. The agar-diffusion technique in studies on immunity to adenoviruses. AMA Arch Ophthalmol. 1957 Dec;58(6):850–856. doi: 10.1001/archopht.1957.00940010872006. [DOI] [PubMed] [Google Scholar]
- WANNAMAKER L. W. The differentiation of three distinct desoxyrlbonucleases of group A Streptococci. J Exp Med. 1958 Jun 1;107(6):797–812. doi: 10.1084/jem.107.6.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WILSON M. W., PRINGLE B. H. Experimental studies of the agar-plate precipitin test of Ouchterlony. J Immunol. 1954 Oct;73(4):232–243. [PubMed] [Google Scholar]