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. 1986 Apr;52(1):144–150. doi: 10.1128/iai.52.1.144-150.1986

Nucleotide sequence of the type A streptococcal exotoxin (erythrogenic toxin) gene from Streptococcus pyogenes bacteriophage T12.

C R Weeks, J J Ferretti
PMCID: PMC262210  PMID: 3514452

Abstract

The gene specifying type A streptococcal exotoxin (speA), also known as erythrogenic toxin, was cloned from the Streptococcus pyogenes bacteriophage T12 genome and analyzed by nucleotide sequencing. The speA gene consists of 753 base pairs and codes for a 29,244-molecular-weight protein. The speA gene product contains a putative 30-amino acid signal peptide, resulting in a molecular weight of 25,787 for the secreted protein. A possible promoter and ribosome-binding site are present in the region upstream from the speA gene, and a transcriptional terminator is located 69 bases downstream from the translational termination codon. The amino acid sequence of the carboxy-terminal portion of the type A streptococcal exotoxin exhibits extensive homology with the carboxy terminus of Staphylococcus aureus enterotoxins B and C1.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alouf J. E. Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol Ther. 1980;11(3):661–717. doi: 10.1016/0163-7258(80)90045-5. [DOI] [PubMed] [Google Scholar]
  2. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Gold L., Pribnow D., Schneider T., Shinedling S., Singer B. S., Stormo G. Translational initiation in prokaryotes. Annu Rev Microbiol. 1981;35:365–403. doi: 10.1146/annurev.mi.35.100181.002053. [DOI] [PubMed] [Google Scholar]
  5. Gryczan T. J., Grandi G., Hahn J., Grandi R., Dubnau D. Conformational alteration of mRNA structure and the posttranscriptional regulation of erythromycin-induced drug resistance. Nucleic Acids Res. 1980 Dec 20;8(24):6081–6097. doi: 10.1093/nar/8.24.6081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gryczan T., Israeli-Reches M., Del Bue M., Dubnau D. DNA sequence and regulation of ermD, a macrolide-lincosamide-streptogramin B resistance element from Bacillus licheniformis. Mol Gen Genet. 1984;194(3):349–356. doi: 10.1007/BF00425543. [DOI] [PubMed] [Google Scholar]
  7. Harwood C. R., Williams D. M., Lovett P. S. Nucleotide sequence of a Bacillus pumilus gene specifying chloramphenicol acetyltransferase. Gene. 1983 Oct;24(2-3):163–169. doi: 10.1016/0378-1119(83)90076-8. [DOI] [PubMed] [Google Scholar]
  8. Hawley D. K., McClure W. R. Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res. 1983 Apr 25;11(8):2237–2255. doi: 10.1093/nar/11.8.2237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Houston C. W., Ferretti J. J. Enzyme-linked immunosorbent assay for detection of type A streptococcal exotoxin: kinetics and regulation during growth of Streptococcus pyogenes. Infect Immun. 1981 Sep;33(3):862–869. doi: 10.1128/iai.33.3.862-869.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Huang I. Y., Bergdoll M. S. The primary structure of staphylococcal enterotoxin B. 3. The cyanogen bromide peptides of reduced and aminoethylated enterotoxin B, and the complete amino acid sequence. J Biol Chem. 1970 Jul 25;245(14):3518–3525. [PubMed] [Google Scholar]
  11. Johnson L. P., Schlievert P. M. Group A streptococcal phage T12 carries the structural gene for pyrogenic exotoxin type A. Mol Gen Genet. 1984;194(1-2):52–56. doi: 10.1007/BF00383496. [DOI] [PubMed] [Google Scholar]
  12. Kaczorek M., Delpeyroux F., Chenciner N., Streeck R. E., Murphy J. R., Boquet P., Tiollais P. Nucleotide sequence and expression of the diphtheria tox228 gene in Escherichia coli. Science. 1983 Aug 26;221(4613):855–858. doi: 10.1126/science.6348945. [DOI] [PubMed] [Google Scholar]
  13. Kapral F. A. Staphylococcus aureus delta toxin as an enterotoxin. Ciba Found Symp. 1985;112:215–229. doi: 10.1002/9780470720936.ch12. [DOI] [PubMed] [Google Scholar]
  14. Khan S. A., Novick R. P. Structural analysis of plasmid pSN2 in Staphylococcus aureus: no involvement in enterotoxin B production. J Bacteriol. 1982 Feb;149(2):642–649. doi: 10.1128/jb.149.2.642-649.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kim Y. B., Watson D. W. A purified group A streptococcal pyrogenic exotoxin. Physiochemical and biological properties including the enhancement of susceptibility to endotoxin lethal shock. J Exp Med. 1970 Mar 1;131(3):611–622. doi: 10.1084/jem.131.3.611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kroyer J., Chang S. The promoter-proximal region of the Bacillus licheniformis penicillinase gene: Nucleotide sequence and predicted leader peptide sequence. Gene. 1981 Dec;15(4):343–347. doi: 10.1016/0378-1119(81)90177-3. [DOI] [PubMed] [Google Scholar]
  17. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  18. Kühn S., Fritz H. J., Starlinger P. Close vicinity of IS1 integration sites in the leader sequence of the gal operon of E. coli. Mol Gen Genet. 1979 Jan 2;167(3):235–241. doi: 10.1007/BF00267414. [DOI] [PubMed] [Google Scholar]
  19. Lacks S. A., Dunn J. J., Greenberg B. Identification of base mismatches recognized by the heteroduplex-DNA-repair system of Streptococcus pneumoniae. Cell. 1982 Dec;31(2 Pt 1):327–336. doi: 10.1016/0092-8674(82)90126-x. [DOI] [PubMed] [Google Scholar]
  20. Lee G., Pero J. Conserved nucleotide sequences in temporally controlled bacteriophage promoters. J Mol Biol. 1981 Oct 25;152(2):247–265. doi: 10.1016/0022-2836(81)90242-4. [DOI] [PubMed] [Google Scholar]
  21. Lee G., Talkington C., Pero J. Nucleotide sequence of a promoter recognized by Bacillus subtilis RNA polymerase. Mol Gen Genet. 1980;180(1):57–65. doi: 10.1007/BF00267352. [DOI] [PubMed] [Google Scholar]
  22. Löfdahl S., Guss B., Uhlén M., Philipson L., Lindberg M. Gene for staphylococcal protein A. Proc Natl Acad Sci U S A. 1983 Feb;80(3):697–701. doi: 10.1073/pnas.80.3.697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Malke H., Roe B., Ferretti J. J. Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A. Gene. 1985;34(2-3):357–362. doi: 10.1016/0378-1119(85)90145-3. [DOI] [PubMed] [Google Scholar]
  24. Mandel M., Higa A. Calcium-dependent bacteriophage DNA infection. J Mol Biol. 1970 Oct 14;53(1):159–162. doi: 10.1016/0022-2836(70)90051-3. [DOI] [PubMed] [Google Scholar]
  25. Maniatis T., Hardison R. C., Lacy E., Lauer J., O'Connell C., Quon D., Sim G. K., Efstratiadis A. The isolation of structural genes from libraries of eucaryotic DNA. Cell. 1978 Oct;15(2):687–701. doi: 10.1016/0092-8674(78)90036-3. [DOI] [PubMed] [Google Scholar]
  26. McLaughlin J. R., Murray C. L., Rabinowitz J. C. Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus beta-lactamase gene. J Biol Chem. 1981 Nov 10;256(21):11283–11291. [PubMed] [Google Scholar]
  27. Messing J., Vieira J. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene. 1982 Oct;19(3):269–276. doi: 10.1016/0378-1119(82)90016-6. [DOI] [PubMed] [Google Scholar]
  28. Moran C. P., Jr, Lang N., Banner C. D., Haldenwang W. G., Losick R. Promoter for a developmentally regulated gene in Bacillus subtilis. Cell. 1981 Sep;25(3):783–791. doi: 10.1016/0092-8674(81)90186-0. [DOI] [PubMed] [Google Scholar]
  29. Moran C. P., Jr, Lang N., LeGrice S. F., Lee G., Stephens M., Sonenshein A. L., Pero J., Losick R. Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis. Mol Gen Genet. 1982;186(3):339–346. doi: 10.1007/BF00729452. [DOI] [PubMed] [Google Scholar]
  30. Murray C. L., Rabinowitz J. C. Nucleotide sequences of transcription and translation initiation regions in Bacillus phage phi 29 early genes. J Biol Chem. 1982 Jan 25;257(2):1053–1062. [PubMed] [Google Scholar]
  31. Müller-Hill B., Crapo L., Gilbert W. Mutants that make more lac repressor. Proc Natl Acad Sci U S A. 1968 Apr;59(4):1259–1264. doi: 10.1073/pnas.59.4.1259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Nauciel C., Raynaud M., Bizzini B. Purification et propriétés de la toxine érythrogèbe du streptocoque. Ann Inst Pasteur (Paris) 1968 Jun;114(6):796–811. [PubMed] [Google Scholar]
  33. Neugebauer K., Sprengel R., Schaller H. Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium. Nucleic Acids Res. 1981 Jun 11;9(11):2577–2588. doi: 10.1093/nar/9.11.2577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Norrander J., Kempe T., Messing J. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene. 1983 Dec;26(1):101–106. doi: 10.1016/0378-1119(83)90040-9. [DOI] [PubMed] [Google Scholar]
  35. Ohmura K., Yamazaki H., Takeichi Y., Nakayama A., Otozai K., Yamane K., Yamasaki M., Tamura G. Nucleotide sequence of the promoter and NH2-terminal signal peptide region of Bacillus subtilis alpha-amylase gene cloned in pUB110. Biochem Biophys Res Commun. 1983 Apr 29;112(2):678–683. doi: 10.1016/0006-291x(83)91516-4. [DOI] [PubMed] [Google Scholar]
  36. Oliver D. Protein secretion in Escherichia coli. Annu Rev Microbiol. 1985;39:615–648. doi: 10.1146/annurev.mi.39.100185.003151. [DOI] [PubMed] [Google Scholar]
  37. Palva I., Pettersson R. F., Kalkkinen N., Lehtovaara P., Sarvas M., Söderlund H., Takkinen K., Käriäinen L. Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the alpha-amylase gene from Bacillus amyloliquefaciens. Gene. 1981 Oct;15(1):43–51. doi: 10.1016/0378-1119(81)90103-7. [DOI] [PubMed] [Google Scholar]
  38. Pósfai G., Baldauf F., Erdei S., Pósfai J., Venetianer P., Kiss A. Structure of the gene coding for the sequence-specific DNA-methyltransferase of the B. subtilis phage SPR. Nucleic Acids Res. 1984 Dec 11;12(23):9039–9049. doi: 10.1093/nar/12.23.9039. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Rosenberg M., Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet. 1979;13:319–353. doi: 10.1146/annurev.ge.13.120179.001535. [DOI] [PubMed] [Google Scholar]
  40. Sako T., Tsuchida N. Nucleotide sequence of the staphylokinase gene from Staphylococcus aureus. Nucleic Acids Res. 1983 Nov 25;11(22):7679–7693. doi: 10.1093/nar/11.22.7679. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Sanger F., Coulson A. R., Barrell B. G., Smith A. J., Roe B. A. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161–178. doi: 10.1016/0022-2836(80)90196-5. [DOI] [PubMed] [Google Scholar]
  42. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Schmidt J. J., Spero L. The complete amino acid sequence of staphylococcal enterotoxin C1. J Biol Chem. 1983 May 25;258(10):6300–6306. [PubMed] [Google Scholar]
  44. Spero L., Morlock B. A. Biological activities of the peptides of staphylococcal enterotoxin C formed by limited tryptic hydrolysis. J Biol Chem. 1978 Dec 25;253(24):8787–8791. [PubMed] [Google Scholar]
  45. Weeks C. R., Ferretti J. J. The gene for type A streptococcal exotoxin (erythrogenic toxin) is located in bacteriophage T12. Infect Immun. 1984 Nov;46(2):531–536. doi: 10.1128/iai.46.2.531-536.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Wells J. A., Ferrari E., Henner D. J., Estell D. A., Chen E. Y. Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis. Nucleic Acids Res. 1983 Nov 25;11(22):7911–7925. doi: 10.1093/nar/11.22.7911. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]

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