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. 1995 Apr;63(4):1229–1234. doi: 10.1128/iai.63.4.1229-1234.1995

Biological activity of toxic shock syndrome toxin 1 and a site-directed mutant, H135A, in a lipopolysaccharide-potentiated mouse lethality model.

B G Stiles 1, T Krakauer 1, P F Bonventre 1
PMCID: PMC173139  PMID: 7890377

Abstract

A recombinant of toxic shock syndrome toxin 1 (TSST-1) which contains a single histidine-to-alanine mutation at residue 135 (H135A) was analyzed for toxicity and vaccine potential in a lipopolysaccharide (LPS)-potentiated mouse lethality model. The 50% lethal dose (LD50) of TSST-1 in BALB/c mice was 47.2 micrograms/kg, but H135A was not lethal when tested at a dose equivalent to 10 LD50s of TSST-1. Levels of tumor necrosis factor (TNF) and gamma interferon (IFN-gamma) in serum were, respectively, 10- and 50-fold higher in LPS-potentiated mice injected with 15 LD50s of TSST-1 than in mice given H135A. Mice injected with only TSST-1 did not have elevated levels of TNF or IFN-gamma in serum, while H135A plus LPS or LPS alone elicited identical, yet very low, levels of TNF and IFN-gamma. An enzyme-linked immunosorbent assay of H135A and TSST-1 with anti-TSST-1 serum yielded very similar dose-response curves, which strongly suggests that H135A serologically and conformationally resembles the native toxin. Mice immunized with H135A developed antibodies that recognized TSST-1 in an enzyme-linked immunosorbent assay and afforded protection against a 15-LD50 challenge of TSST-1 plus LPS. The pooled sera of mice immunized with either TSST-1 or H135A also prevented lymphocyte proliferation due to TSST-1.

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Selected References

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  1. Acharya K. R., Passalacqua E. F., Jones E. Y., Harlos K., Stuart D. I., Brehm R. D., Tranter H. S. Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. Nature. 1994 Jan 6;367(6458):94–97. doi: 10.1038/367094a0. [DOI] [PubMed] [Google Scholar]
  2. Akatsuka H., Imanishi K., Inada K., Yamashita H., Yoshida M., Uchiyama T. Production of tumour necrosis factors by human T cells stimulated by a superantigen, toxic shock syndrome toxin-1. Clin Exp Immunol. 1994 Jun;96(3):422–426. doi: 10.1111/j.1365-2249.1994.tb06045.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Alakhov VYu, Klinsky EYu, Kolosov M. I., Maurer-Fogy I., Moskaleva EYu, Sveshnikov P. G., Pozdnyakova L. P., Shemchukova O. B., Severin E. S. Identification of functionally active fragments of staphylococcal enterotoxin B. Eur J Biochem. 1992 Nov 1;209(3):823–828. doi: 10.1111/j.1432-1033.1992.tb17353.x. [DOI] [PubMed] [Google Scholar]
  4. Beezhold D. H., Best G. K., Bonventre P. F., Thompson M. Endotoxin enhancement of toxic shock syndrome toxin 1-induced secretion of interleukin 1 by murine macrophages. Rev Infect Dis. 1989 Jan-Feb;11 (Suppl 1):S289–S293. doi: 10.1093/clinids/11.supplement_1.s289. [DOI] [PubMed] [Google Scholar]
  5. Beezhold D. H., Best G. K., Bonventre P. F., Thompson M. Synergistic induction of interleukin-1 by endotoxin and toxic shock syndrome toxin-1 using rat macrophages. Infect Immun. 1987 Dec;55(12):2865–2869. doi: 10.1128/iai.55.12.2865-2869.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Benjamin D. C., Berzofsky J. A., East I. J., Gurd F. R., Hannum C., Leach S. J., Margoliash E., Michael J. G., Miller A., Prager E. M. The antigenic structure of proteins: a reappraisal. Annu Rev Immunol. 1984;2:67–101. doi: 10.1146/annurev.iy.02.040184.000435. [DOI] [PubMed] [Google Scholar]
  7. Blanco L., Choi E. M., Connolly K., Thompson M. R., Bonventre P. F. Mutants of staphylococcal toxic shock syndrome toxin 1: mitogenicity and recognition by a neutralizing monoclonal antibody. Infect Immun. 1990 Sep;58(9):3020–3028. doi: 10.1128/iai.58.9.3020-3028.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Bohach G. A., Fast D. J., Nelson R. D., Schlievert P. M. Staphylococcal and streptococcal pyrogenic toxins involved in toxic shock syndrome and related illnesses. Crit Rev Microbiol. 1990;17(4):251–272. doi: 10.3109/10408419009105728. [DOI] [PubMed] [Google Scholar]
  9. Bohach G. A., Hovde C. J., Handley J. P., Schlievert P. M. Cross-neutralization of staphylococcal and streptococcal pyrogenic toxins by monoclonal and polyclonal antibodies. Infect Immun. 1988 Feb;56(2):400–404. doi: 10.1128/iai.56.2.400-404.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Bonventre P. F., Heeg H., Cullen C., Lian C. J. Toxicity of recombinant toxic shock syndrome toxin 1 and mutant toxins produced by Staphylococcus aureus in a rabbit infection model of toxic shock syndrome. Infect Immun. 1993 Mar;61(3):793–799. doi: 10.1128/iai.61.3.793-799.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Bonventre P. F., Heeg H., Edwards C. K., 3rd, Cullen C. M. A mutation at histidine residue 135 of toxic shock syndrome toxin yields an immunogenic protein with minimal toxicity. Infect Immun. 1995 Feb;63(2):509–515. doi: 10.1128/iai.63.2.509-515.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Bonventre P. F., Thompson M. R., Adinolfi L. E., Gillis Z. A., Parsonnet J. Neutralization of toxic shock syndrome toxin-1 by monoclonal antibodies in vitro and in vivo. Infect Immun. 1988 Jan;56(1):135–141. doi: 10.1128/iai.56.1.135-141.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Bulanda M., Zaleska M., Mandel L., Talafantova M., Travnicek J., Kunstmann G., Mauff G., Pulverer G., Heczko P. B. Toxicity of staphylococcal toxic shock syndrome toxin 1 for germ-free and conventional piglets. Rev Infect Dis. 1989 Jan-Feb;11 (Suppl 1):S248–S253. doi: 10.1093/clinids/11.supplement_1.s248. [DOI] [PubMed] [Google Scholar]
  14. Cannon J. G., Tompkins R. G., Gelfand J. A., Michie H. R., Stanford G. G., van der Meer J. W., Endres S., Lonnemann G., Corsetti J., Chernow B. Circulating interleukin-1 and tumor necrosis factor in septic shock and experimental endotoxin fever. J Infect Dis. 1990 Jan;161(1):79–84. doi: 10.1093/infdis/161.1.79. [DOI] [PubMed] [Google Scholar]
  15. Chen J. Y., Qiao Y., Komisar J. L., Baze W. B., Hsu I. C., Tseng J. Increased susceptibility to staphylococcal enterotoxin B intoxication in mice primed with actinomycin D. Infect Immun. 1994 Oct;62(10):4626–4631. doi: 10.1128/iai.62.10.4626-4631.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Choi Y., Lafferty J. A., Clements J. R., Todd J. K., Gelfand E. W., Kappler J., Marrack P., Kotzin B. L. Selective expansion of T cells expressing V beta 2 in toxic shock syndrome. J Exp Med. 1990 Sep 1;172(3):981–984. doi: 10.1084/jem.172.3.981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Crass B. A., Bergdoll M. S. Toxin involvement in toxic shock syndrome. J Infect Dis. 1986 May;153(5):918–926. doi: 10.1093/infdis/153.5.918. [DOI] [PubMed] [Google Scholar]
  18. Edwin C., Parsonnet J., Kass E. H. Structure-activity relationship of toxic-shock-syndrome toxin-1: derivation and characterization of immunologically and biologically active fragments. J Infect Dis. 1988 Dec;158(6):1287–1295. doi: 10.1093/infdis/158.6.1287. [DOI] [PubMed] [Google Scholar]
  19. Edwin C., Swack J. A., Williams K., Bonventre P. F., Kass E. H. Activation of in vitro proliferation of human T cells by a synthetic peptide of toxic shock syndrome toxin 1. J Infect Dis. 1991 Mar;163(3):524–529. doi: 10.1093/infdis/163.3.524. [DOI] [PubMed] [Google Scholar]
  20. Fleischer B., Gerardy-Schahn R., Metzroth B., Carrel S., Gerlach D., Köhler W. An evolutionary conserved mechanism of T cell activation by microbial toxins. Evidence for different affinities of T cell receptor-toxin interaction. J Immunol. 1991 Jan 1;146(1):11–17. [PubMed] [Google Scholar]
  21. Fujikawa H., Takayama H., Uchiyama T., Igarashi H. Bindings of toxic shock syndrome toxin-1 and staphylococcal enterotoxins A, B, and C to rabbit spleen cells. Microbiol Immunol. 1989;33(5):381–390. doi: 10.1111/j.1348-0421.1989.tb01986.x. [DOI] [PubMed] [Google Scholar]
  22. Fujiwaka H., Igarashi H., Usami H., Tanaka S., Tamura H. Clearance of endotoxin from blood of rabbits injected with staphylococcal toxic shock syndrome toxin-1. Infect Immun. 1986 Apr;52(1):134–137. doi: 10.1128/iai.52.1.134-137.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Hackett S. P., Stevens D. L. Superantigens associated with staphylococcal and streptococcal toxic shock syndrome are potent inducers of tumor necrosis factor-beta synthesis. J Infect Dis. 1993 Jul;168(1):232–235. doi: 10.1093/infdis/168.1.232. [DOI] [PubMed] [Google Scholar]
  24. Harris T. O., Grossman D., Kappler J. W., Marrack P., Rich R. R., Betley M. J. Lack of complete correlation between emetic and T-cell-stimulatory activities of staphylococcal enterotoxins. Infect Immun. 1993 Aug;61(8):3175–3183. doi: 10.1128/iai.61.8.3175-3183.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Harris T. O., Hufnagle W. O., Betley M. J. Staphylococcal enterotoxin type A internal deletion mutants: serological activity and induction of T-cell proliferation. Infect Immun. 1993 May;61(5):2059–2068. doi: 10.1128/iai.61.5.2059-2068.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Henne E., Campbell W. H., Carlson E. Toxic shock syndrome toxin 1 enhances synthesis of endotoxin-induced tumor necrosis factor in mice. Infect Immun. 1991 Sep;59(9):2929–2933. doi: 10.1128/iai.59.9.2929-2933.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Hynes W. L., Weeks C. R., Iandolo J. J., Ferretti J. J. Immunologic cross-reactivity of type A streptococcal exotoxin (erythrogenic toxin) and staphylococcal enterotoxins B and C1. Infect Immun. 1987 Mar;55(3):837–838. doi: 10.1128/iai.55.3.837-838.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Jett M., Neill R., Welch C., Boyle T., Bernton E., Hoover D., Lowell G., Hunt R. E., Chatterjee S., Gemski P. Identification of staphylococcal enterotoxin B sequences important for induction of lymphocyte proliferation by using synthetic peptide fragments of the toxin. Infect Immun. 1994 Aug;62(8):3408–3415. doi: 10.1128/iai.62.8.3408-3415.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Jupin C., Anderson S., Damais C., Alouf J. E., Parant M. Toxic shock syndrome toxin 1 as an inducer of human tumor necrosis factors and gamma interferon. J Exp Med. 1988 Mar 1;167(3):752–761. doi: 10.1084/jem.167.3.752. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Kappler J. W., Herman A., Clements J., Marrack P. Mutations defining functional regions of the superantigen staphylococcal enterotoxin B. J Exp Med. 1992 Feb 1;175(2):387–396. doi: 10.1084/jem.175.2.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Karp D. R., Teletski C. L., Scholl P., Geha R., Long E. O. The alpha 1 domain of the HLA-DR molecule is essential for high-affinity binding of the toxic shock syndrome toxin-1. Nature. 1990 Aug 2;346(6283):474–476. doi: 10.1038/346474a0. [DOI] [PubMed] [Google Scholar]
  32. Keane W. F., Gekker G., Schlievert P. M., Peterson P. K. Enhancement of endotoxin-induced isolated renal tubular cell injury by toxic shock syndrome toxin 1. Am J Pathol. 1986 Jan;122(1):169–176. [PMC free article] [PubMed] [Google Scholar]
  33. Kokan-Moore N. P., Bergdoll M. S. Determination of biologically active region in toxic shock syndrome toxin 1. Rev Infect Dis. 1989 Jan-Feb;11 (Suppl 1):S125–S129. [PubMed] [Google Scholar]
  34. Lee A. C., Robbins R. N., Bergdoll M. S. Isolation of specific and common antibodies to staphylococcal enterotoxins A and E by affinity chromatography. Infect Immun. 1978 Aug;21(2):387–391. doi: 10.1128/iai.21.2.387-391.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Lee A. C., Robbins R. N., Reiser R. F., Bergdoll M. S. Isolation of specific and common antibodies to staphylococcal enterotoxins B, C1, and C2. Infect Immun. 1980 Feb;27(2):431–434. doi: 10.1128/iai.27.2.431-434.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Marrack P., Blackman M., Kushnir E., Kappler J. The toxicity of staphylococcal enterotoxin B in mice is mediated by T cells. J Exp Med. 1990 Feb 1;171(2):455–464. doi: 10.1084/jem.171.2.455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Marrack P., Kappler J. The staphylococcal enterotoxins and their relatives. Science. 1990 May 11;248(4956):705–711. doi: 10.1126/science.2185544. [DOI] [PubMed] [Google Scholar]
  38. Metzroth B., Marx T., Linnig M., Fleischer B. Concomitant loss of conformation and superantigenic activity of staphylococcal enterotoxin B deletion mutant proteins. Infect Immun. 1993 Jun;61(6):2445–2452. doi: 10.1128/iai.61.6.2445-2452.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Meyer R. F., Miller L., Bennett R. W., MacMillan J. D. Development of a monoclonal antibody capable of interacting with five serotypes of Staphylococcus aureus enterotoxin. Appl Environ Microbiol. 1984 Feb;47(2):283–287. doi: 10.1128/aem.47.2.283-287.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Micusan V. V., Desrosiers M., Gosselin J., Mercier G., Oth D., Bhatti A. R., Heremans H., Billiau A. Stimulation of T cells and induction of interferon by toxic shock syndrome toxin 1. Rev Infect Dis. 1989 Jan-Feb;11 (Suppl 1):S305–S312. doi: 10.1093/clinids/11.supplement_1.s305. [DOI] [PubMed] [Google Scholar]
  41. Micusan V. V., Mercier G., Bhatti A. R., Reiser R. F., Bergdoll M. S., Oth D. Production of human and murine interleukin-2 by toxic shock syndrome toxin-1. Immunology. 1986 Jun;58(2):203–208. [PMC free article] [PubMed] [Google Scholar]
  42. Miethke T., Duschek K., Wahl C., Heeg K., Wagner H. Pathogenesis of the toxic shock syndrome: T cell mediated lethal shock caused by the superantigen TSST-1. Eur J Immunol. 1993 Jul;23(7):1494–1500. doi: 10.1002/eji.1830230715. [DOI] [PubMed] [Google Scholar]
  43. Miethke T., Wahl C., Heeg K., Echtenacher B., Krammer P. H., Wagner H. T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: critical role of tumor necrosis factor. J Exp Med. 1992 Jan 1;175(1):91–98. doi: 10.1084/jem.175.1.91. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Miethke T., Wahl C., Regele D., Gaus H., Heeg K., Wagner H. Superantigen mediated shock: a cytokine release syndrome. Immunobiology. 1993 Nov;189(3-4):270–284. doi: 10.1016/S0171-2985(11)80362-1. [DOI] [PubMed] [Google Scholar]
  45. Murray D. L., Prasad G. S., Earhart C. A., Leonard B. A., Kreiswirth B. N., Novick R. P., Ohlendorf D. H., Schlievert P. M. Immunobiologic and biochemical properties of mutants of toxic shock syndrome toxin-1. J Immunol. 1994 Jan 1;152(1):87–95. [PubMed] [Google Scholar]
  46. Parsonnet J., Gillis Z. A. Production of tumor necrosis factor by human monocytes in response to toxic-shock-syndrome toxin-1. J Infect Dis. 1988 Nov;158(5):1026–1033. doi: 10.1093/infdis/158.5.1026. [DOI] [PubMed] [Google Scholar]
  47. Parsonnet J., Hickman R. K., Eardley D. D., Pier G. B. Induction of human interleukin-1 by toxic-shock-syndrome toxin-1. J Infect Dis. 1985 Mar;151(3):514–522. doi: 10.1093/infdis/151.3.514. [DOI] [PubMed] [Google Scholar]
  48. Pettit G. W., Elwell M. R., Jahrling P. B. Possible endotoxemia in rabbits after intravenous injection of Staphylococcus aureus enterotoxin B. J Infect Dis. 1977 Apr;135(4):646–648. doi: 10.1093/infdis/135.4.646. [DOI] [PubMed] [Google Scholar]
  49. Prasad G. S., Earhart C. A., Murray D. L., Novick R. P., Schlievert P. M., Ohlendorf D. H. Structure of toxic shock syndrome toxin 1. Biochemistry. 1993 Dec 21;32(50):13761–13766. doi: 10.1021/bi00213a001. [DOI] [PubMed] [Google Scholar]
  50. Reiser R. F., Robbins R. N., Khoe G. P., Bergdoll M. S. Purification and some physicochemical properties of toxic-shock toxin. Biochemistry. 1983 Aug 2;22(16):3907–3912. doi: 10.1021/bi00285a028. [DOI] [PubMed] [Google Scholar]
  51. SUGIYAMA H., MCKISSIC E. M., Jr, BERGDOLL M. S., HELLER B. ENHANCEMENT OF BACTERIAL ENDOTOXIN LETHALITY BY STAPHYLOCOCCAL ENTEROTOXIN. J Infect Dis. 1964 Apr;114:111–118. doi: 10.1093/infdis/114.2.111. [DOI] [PubMed] [Google Scholar]
  52. Schlievert P. M. Enhancement of host susceptibility to lethal endotoxin shock by staphylococcal pyrogenic exotoxin type C. Infect Immun. 1982 Apr;36(1):123–128. doi: 10.1128/iai.36.1.123-128.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Schlievert P. M. Role of superantigens in human disease. J Infect Dis. 1993 May;167(5):997–1002. doi: 10.1093/infdis/167.5.997. [DOI] [PubMed] [Google Scholar]
  54. Schlievert P. M., Shands K. N., Dan B. B., Schmid G. P., Nishimura R. D. Identification and characterization of an exotoxin from Staphylococcus aureus associated with toxic-shock syndrome. J Infect Dis. 1981 Apr;143(4):509–516. doi: 10.1093/infdis/143.4.509. [DOI] [PubMed] [Google Scholar]
  55. Scholl P. R., Diez A., Geha R. S. Staphylococcal enterotoxin B and toxic shock syndrome toxin-1 bind to distinct sites on HLA-DR and HLA-DQ molecules. J Immunol. 1989 Oct 15;143(8):2583–2588. [PubMed] [Google Scholar]
  56. Scholl P. R., Sekaly R. P., Diez A., Glimcher L. H., Geha R. S. Binding of toxic shock syndrome toxin-1 to murine major histocompatibility complex class II molecules. Eur J Immunol. 1990 Sep;20(9):1911–1916. doi: 10.1002/eji.1830200907. [DOI] [PubMed] [Google Scholar]
  57. See R. H., Krystal G., Chow A. W. Receptors for toxic shock syndrome toxin-1 and staphylococcal enterotoxin A on human blood monocytes. Can J Microbiol. 1992 Sep;38(9):937–944. doi: 10.1139/m92-151. [DOI] [PubMed] [Google Scholar]
  58. Soos J. M., Russell J. K., Jarpe M. A., Pontzer C. H., Johnson H. M. Identification of binding domains on the superantigen, toxic shock syndrome-1, for class II MHC molecules. Biochem Biophys Res Commun. 1993 Mar 31;191(3):1211–1217. doi: 10.1006/bbrc.1993.1346. [DOI] [PubMed] [Google Scholar]
  59. Stiles B. G., Bavari S., Krakauer T., Ulrich R. G. Toxicity of staphylococcal enterotoxins potentiated by lipopolysaccharide: major histocompatibility complex class II molecule dependency and cytokine release. Infect Immun. 1993 Dec;61(12):5333–5338. doi: 10.1128/iai.61.12.5333-5338.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Stone R. L., Schlievert P. M. Evidence for the involvement of endotoxin in toxic shock syndrome. J Infect Dis. 1987 Apr;155(4):682–689. doi: 10.1093/infdis/155.4.682. [DOI] [PubMed] [Google Scholar]
  61. Swaminathan S., Furey W., Pletcher J., Sax M. Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature. 1992 Oct 29;359(6398):801–806. doi: 10.1038/359801a0. [DOI] [PubMed] [Google Scholar]
  62. Talmadge J. E., Bowersox O., Tribble H., Lee S. H., Shepard H. M., Liggitt D. Toxicity of tumor necrosis factor is synergistic with gamma-interferon and can be reduced with cyclooxygenase inhibitors. Am J Pathol. 1987 Sep;128(3):410–425. [PMC free article] [PubMed] [Google Scholar]
  63. Todd J., Fishaut M., Kapral F., Welch T. Toxic-shock syndrome associated with phage-group-I Staphylococci. Lancet. 1978 Nov 25;2(8100):1116–1118. doi: 10.1016/s0140-6736(78)92274-2. [DOI] [PubMed] [Google Scholar]
  64. Uchiyama T., Saito S., Inoko H., Yan X. J., Imanishi K., Araake M., Igarashi H. Relative activities of distinct isotypes of murine and human major histocompatibility complex class II molecules in binding toxic shock syndrome toxin 1 and determination of CD antigens expressed on T cells generated upon stimulation by the toxin. Infect Immun. 1990 Dec;58(12):3877–3882. doi: 10.1128/iai.58.12.3877-3882.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Uchiyama T., Tadakuma T., Imanishi K., Araake M., Saito S., Yan X. J., Fujikawa H., Igarashi H., Yamaura N. Activation of murine T cells by toxic shock syndrome toxin-1. The toxin-binding structures expressed on murine accessory cells are MHC class II molecules. J Immunol. 1989 Nov 15;143(10):3175–3182. [PubMed] [Google Scholar]
  66. de Azavedo J. C., Arbuthnott J. P. Toxicity of staphylococcal toxic shock syndrome toxin 1 in rabbits. Infect Immun. 1984 Nov;46(2):314–317. doi: 10.1128/iai.46.2.314-317.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]

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