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. 1988 Jan;170(1):34–41. doi: 10.1128/jb.170.1.34-41.1988

Nucleotide sequence of the type A staphylococcal enterotoxin gene.

M J Betley 1, J J Mekalanos 1
PMCID: PMC210602  PMID: 3335483

Abstract

We determined the nucleotide sequence of the gene encoding staphylococcal enterotoxin A (entA). The gene, composed of 771 base pairs, encodes an enterotoxin A precursor of 257 amino acid residues. A 24-residue N-terminal hydrophobic leader sequence is apparently processed, yielding the mature form of staphylococcal enterotoxin A (Mr, 27,100). Mature enterotoxin A has 82, 72, 74, and 34 amino acid residues in common with staphylococcal enterotoxins B and C1, type A streptococcal exotoxin, and toxic shock syndrome toxin 1, respectively. This level of homology was determined to be significant based on the results of computer analysis and biological considerations. DNA sequence homology between the entA gene and genes encoding other types of staphylococcal enterotoxins was examined by DNA-DNA hybridization analysis with probes derived from the entA gene. A 624-base-pair DNA probe that represented an internal fragment of the entA gene hybridized well to DNA isolated from EntE+ strains and some EntA+ strains. In contrast, a 17-base oligonucleotide probe that encoded a peptide conserved among staphylococcal enterotoxins A, B, and C1 hybridized well to DNA isolated from EntA+, EntB+, EntC1+, and EntD+ strains. These hybridization results indicate that considerable sequence divergence has occurred within this family of exotoxins.

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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. Archer D. L., Wess J. A., Johnson H. M. Inverse relationship between immune interferon induction and mitogen effects on the maturation of the primary antibody response. Immunopharmacology. 1981 Feb;3(1):71–81. doi: 10.1016/0162-3109(81)90041-2. [DOI] [PubMed] [Google Scholar]
  3. Betley M. J., Löfdahl S., Kreiswirth B. N., Bergdoll M. S., Novick R. P. Staphylococcal enterotoxin A gene is associated with a variable genetic element. Proc Natl Acad Sci U S A. 1984 Aug;81(16):5179–5183. doi: 10.1073/pnas.81.16.5179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Betley M. J., Mekalanos J. J. Staphylococcal enterotoxin A is encoded by phage. Science. 1985 Jul 12;229(4709):185–187. doi: 10.1126/science.3160112. [DOI] [PubMed] [Google Scholar]
  5. Blomster-Hautamaa D. A., Kreiswirth B. N., Kornblum J. S., Novick R. P., Schlievert P. M. The nucleotide and partial amino acid sequence of toxic shock syndrome toxin-1. J Biol Chem. 1986 Nov 25;261(33):15783–15786. [PubMed] [Google Scholar]
  6. Chu F. S., Bergdoll M. S. Studies on the chemical modification of staphylococcal enterotoxin B. I. Alkylation and oxidation of methionine residues. Biochim Biophys Acta. 1969 Nov 11;194(1):279–286. doi: 10.1016/0005-2795(69)90204-9. [DOI] [PubMed] [Google Scholar]
  7. Clark W. G., Page J. S. Pyrogenic responses to staphylococcal enterotoxins A and B in cats. J Bacteriol. 1968 Dec;96(6):1940–1946. doi: 10.1128/jb.96.6.1940-1946.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Czop J. K., Bergdoll M. S. Staphylococcal enterotoxin synthesis during the exponential, transitional, and stationary growth phases. Infect Immun. 1974 Feb;9(2):229–235. doi: 10.1128/iai.9.2.229-235.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dornbusch K., Hallander H. O., Löfquist F. Extrachromosomal control of methicillin resistance and toxin production in Staphylococcus aureus. J Bacteriol. 1969 May;98(2):351–358. doi: 10.1128/jb.98.2.351-358.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Johnson L. P., L'Italien J. J., Schlievert P. M. Streptococcal pyrogenic exotoxin type A (scarlet fever toxin) is related to Staphylococcus aureus enterotoxin B. Mol Gen Genet. 1986 May;203(2):354–356. doi: 10.1007/BF00333979. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Jones C. L., Khan S. A. Nucleotide sequence of the enterotoxin B gene from Staphylococcus aureus. J Bacteriol. 1986 Apr;166(1):29–33. doi: 10.1128/jb.166.1.29-33.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Langford M. P., Stanton G. J., Johnson H. M. Biological effects of staphylococcal enterotoxin A on human peripheral lymphocytes. Infect Immun. 1978 Oct;22(1):62–68. doi: 10.1128/iai.22.1.62-68.1978. [DOI] [PMC free article] [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. Manoil C., Beckwith J. TnphoA: a transposon probe for protein export signals. Proc Natl Acad Sci U S A. 1985 Dec;82(23):8129–8133. doi: 10.1073/pnas.82.23.8129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mekalanos J. J. Duplication and amplification of toxin genes in Vibrio cholerae. Cell. 1983 Nov;35(1):253–263. doi: 10.1016/0092-8674(83)90228-3. [DOI] [PubMed] [Google Scholar]
  20. Mekalanos J. J., Swartz D. J., Pearson G. D., Harford N., Groyne F., de Wilde M. Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development. Nature. 1983 Dec 8;306(5943):551–557. doi: 10.1038/306551a0. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. Michaelis S., Beckwith J. Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu Rev Microbiol. 1982;36:435–465. doi: 10.1146/annurev.mi.36.100182.002251. [DOI] [PubMed] [Google Scholar]
  23. Moseley S. L., Falkow S. Nucleotide sequence homology between the heat-labile enterotoxin gene of Escherichia coli and Vibrio cholerae deoxyribonucleic acid. J Bacteriol. 1980 Oct;144(1):444–446. doi: 10.1128/jb.144.1.444-446.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Murray N. E., Batten P. L., Murray K. Restriction of bacteriophage lambda by Escherichia coli K. J Mol Biol. 1973 Dec 15;81(3):395–407. doi: 10.1016/0022-2836(73)90149-6. [DOI] [PubMed] [Google Scholar]
  25. Newland J. W., Strockbine N. A., Miller S. F., O'Brien A. D., Holmes R. K. Cloning of Shiga-like toxin structural genes from a toxin converting phage of Escherichia coli. Science. 1985 Oct 11;230(4722):179–181. doi: 10.1126/science.2994228. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. Novick R. P., Brodsky R. Studies on plasmid replication. I. Plasmid incompatibility and establishment in Staphylococcus aureus. J Mol Biol. 1972 Jul 21;68(2):285–302. doi: 10.1016/0022-2836(72)90214-8. [DOI] [PubMed] [Google Scholar]
  28. O'Brien A. D., Chen M. E., Holmes R. K., Kaper J., Levine M. M. Environmental and human isolates of Vibrio cholerae and Vibrio parahaemolyticus produce a Shigella dysenteriae 1 (Shiga)-like cytotoxin. Lancet. 1984 Jan 14;1(8368):77–78. doi: 10.1016/s0140-6736(84)90006-0. [DOI] [PubMed] [Google Scholar]
  29. Pattee P. A., Neveln D. S. Transformation analysis of three linkage groups in Staphylococcus aureus. J Bacteriol. 1975 Oct;124(1):201–211. doi: 10.1128/jb.124.1.201-211.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Peavy D. L., Adler W. H., Smith R. T. The mitogenic effects of endotoxin and staphylococcal enterotoxin B on mouse spleen cells and human peripheral lymphocytes. J Immunol. 1970 Dec;105(6):1453–1458. [PubMed] [Google Scholar]
  31. Quimby F., Nguyen H. T. Animal studies of toxic shock syndrome. Crit Rev Microbiol. 1985;12(1):1–44. doi: 10.3109/10408418509104424. [DOI] [PubMed] [Google Scholar]
  32. Ranelli D. M., Jones C. L., Johns M. B., Mussey G. J., Khan S. A. Molecular cloning of staphylococcal enterotoxin B gene in Escherichia coli and Staphylococcus aureus. Proc Natl Acad Sci U S A. 1985 Sep;82(17):5850–5854. doi: 10.1073/pnas.82.17.5850. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Reiser R. F., Robbins R. N., Noleto A. L., Khoe G. P., Bergdoll M. S. Identification, purification, and some physicochemical properties of staphylococcal enterotoxin C3. Infect Immun. 1984 Sep;45(3):625–630. doi: 10.1128/iai.45.3.625-630.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. 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]
  35. 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]
  36. Schantz E. J., Roessler W. G., Woodburn M. J., Lynch J. M., Jacoby H. M., Silverman S. J., Gorman J. C., Spero L. Purification and some chemical and physical properties of staphylococcal enterotoxin A. Biochemistry. 1972 Feb 1;11(3):360–366. doi: 10.1021/bi00753a009. [DOI] [PubMed] [Google Scholar]
  37. 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]
  38. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  40. Stelma G. N., Jr, Bergdoll M. S. Inactivation of staphylococcal enterotoxin A by chemical modification. Biochem Biophys Res Commun. 1982 Mar 15;105(1):121–126. doi: 10.1016/s0006-291x(82)80019-3. [DOI] [PubMed] [Google Scholar]
  41. Takao T., Tominaga N., Shimonishi Y., Hara S., Inoue T., Miyama A. Primary structure of heat-stable enterotoxin produced by Yersinia enterocolitica. Biochem Biophys Res Commun. 1984 Dec 28;125(3):845–851. doi: 10.1016/0006-291x(84)91360-3. [DOI] [PubMed] [Google Scholar]
  42. Thuring R. W., Sanders J. P., Borst P. A freeze-squeeze method for recovering long DNA from agarose gels. Anal Biochem. 1975 May 26;66(1):213–220. doi: 10.1016/0003-2697(75)90739-3. [DOI] [PubMed] [Google Scholar]
  43. Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
  44. Warren J. R., Leatherman D. L., Metzger J. F. Evidence for cell-receptor activity in lymphocyte stimulation by staphylococcal enterotoxin. J Immunol. 1975 Jul;115(1):49–53. [PubMed] [Google Scholar]
  45. Weeks C. R., Ferretti J. J. Nucleotide sequence of the type A streptococcal exotoxin (erythrogenic toxin) gene from Streptococcus pyogenes bacteriophage T12. Infect Immun. 1986 Apr;52(1):144–150. doi: 10.1128/iai.52.1.144-150.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. 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]
  47. Zehavi-Willner T., Shenberg E., Barnea A. In vivo effect of staphylococcal enterotoxin A on peripheral blood lymphocytes. Infect Immun. 1984 May;44(2):401–405. doi: 10.1128/iai.44.2.401-405.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]

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