1887

Chapter 38 : Exotoxins

Author: Gregory A. Bohach
Content Type: Reference
Publication Year: 2006

Category: Bacterial Pathogenesis

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Preview this chapter:
Preview Magnify
Zoom in
Zoomout

Exotoxins, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555816513/9781555813437_Chap38-1.gif /docserver/preview/fulltext/10.1128/9781555816513/9781555813437_Chap38-2.gif

Abstract:

This chapter talks about exotoxins fall into three general groups: (i) membrane-active agents, (ii) pyrogenic toxin superantigens (PTSAgs), and (iii) exfoliative toxins (ETs). Researchers proposed the existence of delta-toxin as the fourth cytolytic toxin in 1947. Panton-Valentine leukocidin (PVL) and gamma-toxin are two prototypic bicomponent toxins. Unfortunately, the rapid rate of new toxin discovery has resulted in more than one SE being given the same designation in the literature. Therefore, it is now recommended that nomenclature for new PTSAgs be assigned by the International Nomenclature Committee for Staphylococcal Superantigens prior to publication. The major cytokines induced initially include IL-1, tumor necrosis factors alpha and beta, interferon-γ, and IL-2. The ETs have been conclusively implicated in staphylococcal scalded-skin syndrome (SSSS). Two antigenically distinct forms, designated ETA and ETB, are the best characterized ETs and are produced most frequently by phage group II by isolates; strains expressing ETs constitute group IV staphylococcal isolates. Lesions in SSSS and mice are characterized by separation of stratum granulosa cells causing intraepidermal skin peeling.

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Staphylococcus aureus Exotoxins
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555816513.chap38-1,webId=/content/author/10.1128/9781555816513.chap38-1,properties={foaf_givenname=Gregory A., foaf_name=Gregory A. Bohach, foaf_surname=Bohach}]]
Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
/content/10.1128/9781555816513.chap38.fig38-1
FIGURE 1

Membrane pore formation by alpha-toxin. (A) Rabbit erythrocyte membrane fragment negatively stained following lysis with alpha-toxin. Arrows designate representative ring-shaped structures (10 nm) on the membrane. (B) Ringshaped alpha-toxin multimers isolated in detergent solution. (Inset) The rings are magnified so that the internal channel (2.5 nm) and ring perimeter (10 nm) are clearly visible.

10.1128/9781555816513/fig38-1_thmb.gif
10.1128/9781555816513/fig38-1.gif
Image of FIGURE 1
FIGURE 1

Membrane pore formation by alpha-toxin. (A) Rabbit erythrocyte membrane fragment negatively stained following lysis with alpha-toxin. Arrows designate representative ring-shaped structures (10 nm) on the membrane. (B) Ringshaped alpha-toxin multimers isolated in detergent solution. (Inset) The rings are magnified so that the internal channel (2.5 nm) and ring perimeter (10 nm) are clearly visible.

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555816513.chap38.fig38-2
FIGURE 2

Model for alpha-toxin assembly based on crystallographic data and structure-function experiments. The model depicts the formation of a heptameric ring (α7 and α7*). A cross-section of the ring revealing only four monomers is shown so that the proposed structural alterations are visible. In this model, alpha-toxin is expressed and secreted as a monomer (α1). α1, bound to the target membrane (designated α1*), promotes assembly of the heptamer (α7). In the final stage of assembly, β-sheets in each monomer (depicted as small circles) insert into the membrane, forming a channel, and the N-terminal latches contact adjacent monomers, rendering them resistant to proteolysis.

10.1128/9781555816513/fig38-2_thmb.gif
10.1128/9781555816513/fig38-2.gif
Image of FIGURE 2
FIGURE 2

Model for alpha-toxin assembly based on crystallographic data and structure-function experiments. The model depicts the formation of a heptameric ring (α7 and α7*). A cross-section of the ring revealing only four monomers is shown so that the proposed structural alterations are visible. In this model, alpha-toxin is expressed and secreted as a monomer (α1). α1, bound to the target membrane (designated α1*), promotes assembly of the heptamer (α7). In the final stage of assembly, β-sheets in each monomer (depicted as small circles) insert into the membrane, forming a channel, and the N-terminal latches contact adjacent monomers, rendering them resistant to proteolysis.

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555816513.chap38.fig38-3
FIGURE 3

Properties of staphylococcal beta-toxin. (A) Sphingomyelin chemical formula showing beta-toxin cleavage site resulting in generation of phosphorylcholine and ceramide. (B) Scanning electron micrograph showing lesions in human erythrocyte membranes caused by beta-toxin after shifting the temperature to 4°C.

10.1128/9781555816513/fig38-3_thmb.gif
10.1128/9781555816513/fig38-3.gif
Image of FIGURE 3
FIGURE 3

Properties of staphylococcal beta-toxin. (A) Sphingomyelin chemical formula showing beta-toxin cleavage site resulting in generation of phosphorylcholine and ceramide. (B) Scanning electron micrograph showing lesions in human erythrocyte membranes caused by beta-toxin after shifting the temperature to 4°C.

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555816513.chap38.fig38-4
FIGURE 4

Molecular aspects of staphylococcal bicomponent toxins. Organization of bicomponent toxin genes in a strain harboring both the and loci. Any S and F component may combine to generate a unique bicomponent toxin. The two prototype bicomponent toxins, PVL and deltatoxin, are composed of LukS-PV+LukF-PV and HlgA+HlgB, respectively.

10.1128/9781555816513/fig38-4_thmb.gif
10.1128/9781555816513/fig38-4.gif
Image of FIGURE 4
FIGURE 4

Molecular aspects of staphylococcal bicomponent toxins. Organization of bicomponent toxin genes in a strain harboring both the and loci. Any S and F component may combine to generate a unique bicomponent toxin. The two prototype bicomponent toxins, PVL and deltatoxin, are composed of LukS-PV+LukF-PV and HlgA+HlgB, respectively.

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555816513.chap38.fig38-5
FIGURE 5

Structural properties and receptor interactions of PTSAgs. (A) A structural comparison of SEC3 and TSST-1. Ribbon diagrams shown are based on crystal structures published for the two toxins ( ). The two structures are oriented so that the TCR-binding cavity in each is located at the top and the cysteine loop, unique to the SEs, is on the upper right-hand corner of SEC3. Both toxins possess a similar domain organization and an overall topology despite having several important differences as discussed in the text. (B) A model of the trimolecular complex with SEB or SEC bound to TCR and MHC-II (adapted from results of references and ). In this model, SAgs orient the two receptors away from each other, inducing an aberrant mechanism of T-cell activation. Note that antigenic peptide associated with MHC-II is positioned away from the TCR-binding site.

10.1128/9781555816513/fig38-5_thmb.gif
10.1128/9781555816513/fig38-5.gif
Image of FIGURE 5
FIGURE 5

Structural properties and receptor interactions of PTSAgs. (A) A structural comparison of SEC3 and TSST-1. Ribbon diagrams shown are based on crystal structures published for the two toxins ( ). The two structures are oriented so that the TCR-binding cavity in each is located at the top and the cysteine loop, unique to the SEs, is on the upper right-hand corner of SEC3. Both toxins possess a similar domain organization and an overall topology despite having several important differences as discussed in the text. (B) A model of the trimolecular complex with SEB or SEC bound to TCR and MHC-II (adapted from results of references and ). In this model, SAgs orient the two receptors away from each other, inducing an aberrant mechanism of T-cell activation. Note that antigenic peptide associated with MHC-II is positioned away from the TCR-binding site.

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555816513.chap38.fig38-6
FIGURE 6

Ribbon diagram of the ETA crystal structure showing important functional features. Similar to other chymotrypsinlike proteases, ETA has two β-barrel domains and a C-terminal α-helix. The N-terminal domain, which includes a highly charged α-helix, is unique and is suspected to be involved in receptor binding. The positions of residues H72, D102, and S195, comprising the putative catalytic triad, are superimposable with the analogous residues of α-thrombin. D164 in loop D controls access of substrate to the protease active site by hydrogen bonding to G193. This causes the P192-G193 peptide bond to flip 180 degrees compared to that seen in other serine proteases and may explain the lack of demonstrable proteolytic activity in vitro. Binding of the N-terminal α-helix to its receptor has been proposed to cause a shift in the position of loop D and thereby the P192-G193 peptide bond, allowing access to the active site in vivo ( ).

10.1128/9781555816513/fig38-6_thmb.gif
10.1128/9781555816513/fig38-6.gif
Image of FIGURE 6
FIGURE 6

Ribbon diagram of the ETA crystal structure showing important functional features. Similar to other chymotrypsinlike proteases, ETA has two β-barrel domains and a C-terminal α-helix. The N-terminal domain, which includes a highly charged α-helix, is unique and is suspected to be involved in receptor binding. The positions of residues H72, D102, and S195, comprising the putative catalytic triad, are superimposable with the analogous residues of α-thrombin. D164 in loop D controls access of substrate to the protease active site by hydrogen bonding to G193. This causes the P192-G193 peptide bond to flip 180 degrees compared to that seen in other serine proteases and may explain the lack of demonstrable proteolytic activity in vitro. Binding of the N-terminal α-helix to its receptor has been proposed to cause a shift in the position of loop D and thereby the P192-G193 peptide bond, allowing access to the active site in vivo ( ).

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555816513.chap38
1. Aarestrup, F. M.,, H. D. Larsen,, N. H. Eriksen,, C. S. Elsberg,, and N. E. Jensen. 1999. Frequency of alpha- and beta-haemolysin in Staphylococcus aureus of bovine and human origin. A comparison between pheno- and geno-type and variation in phenotypic expression. APMIS 107: 425– 430.
2. Ahrens, P.,, and L. O. Andresen. 2004. Cloning and sequence analysis of genes encoding Staphylococcus hyicus exfoliative toxin types A, B, C, and D. J. Bacteriol. 186: 1833– 1837.
3. Alber, G.,, D. K. Hammer,, and B. Fleischer. 1990. Relationship between enterotoxic- and T lymphocyte-stimulating activity of staphylococcal enterotoxin B. J. Immunol. 144: 4501– 4506.
4. Alber, G.,, P. H. Scheuber,, B. Reck,, B. Sailer-Kramer,, A. Hartmann,, and D. K. Hammer. 1989. Role of substance P in immediate-type skin reactions induced by staphylococcal enterotoxin B in unsensitized monkeys. J. Allergy Clin. Immunol. 84: 880– 885.
5. Al-Daccak, R.,, K. Mehindate,, F. Damdoumi,, P. Etongue-Mayer,, H. Nilsson,, P. Antonsson,, M. Sundstrom,, M. Dohlsten,, R. P. Sekaly,, and W. Mourad. 1998. Staphylococcal enterotoxin D is a promiscuous superantigen offering multiple modes of interactions with the MHC class II receptors. J. Immunol. 160: 225– 232.
6. Alouf, J. E., 1977. Cell membranes and cytolytic bacterial toxins, p. 220– 270. In P. Cuatrecasas (ed.), Receptors and Recognition, series B, vol. 1. The Specificity and Action of Animal, Bacterial and Plant Toxins. Chapman and Hall Ltd., London, United Kingdom
7. Amagai, M.,, N. Matsuyoshi,, Z. H. Wang,, C. Andl,, and J. R. Stanley. 2000. Toxin in bullous impetigo and staphylococcal scalded-skin syndrome targets desmoglein 1. Nat. Med. 6: 1275– 1277.
8. Amagai, M.,, T. Yamaguchi,, Y. Hanakawa,, K. Nishifuji,, M. Sugai,, and J. R. Stanley. 2002. Staphylococcal exfoliative toxin B specifically cleaves desmoglein 1. J. Invest. Dermatol. 118: 845– 850.
9. Arbuthnott, J. P., 1982. Bacterial cytolysins (membranedamaging toxins), p. 107– 129. In P. Cohen, and S. van Heyningen (ed.), Molecular Action of Toxins and Viruses. Elsevier Biomedical Press, Amsterdam, The Netherlands.
10. Bailey, C. J.,, B. P. Lockhart,, M. B. Redpath,, and T. P. Smith. 1995. The epidermolytic (exfoliative) toxins of Staphylococcus aureus. Med. Microbiol. Immunol. 184: 53– 61.
11. Bailey, C. J.,, and M. B. Redpath. 1992. The esterolytic activity of epidermolytic toxins. Biochem. J. 284: 177– 180.
12. Bayles, K. W.,, and J. J. Iandolo. 1989. Genetic and molecular analyses of the gene encoding staphylococcal enterotoxin D. J. Bacteriol. 171: 4799– 4806.
13. Bhakdi, S.,, and J. Tranum-Jensen. 1991. Alpha-toxin of Staphylococcus aureus. Microbiol. Rev. 55: 733– 751.
14. Bohach, G. A.,, D. J. Fast,, R. D. Nelson,, and P. M. Schlievert. 1990. Staphylococcal and streptococcal pyrogenic toxins involved in toxic shock syndrome and related illnesses. Crit. Rev. Microbiol. 17: 251– 272.
15. Bohach, G. A.,, L. M. Jablonski,, C. F. Deobald,, Y. I. Chi,, and C. V. Stauffacher,. 1995. Functional domains of staphylococcal enterotoxins, p. 339– 356. In M. Ecklund,, J. L. Richard,, and K. Mise (ed.), Molecular Approaches to Food Safety: Issues Involving Toxic Microorganisms. Alaken, Inc., Fort Collins, Colo.
16. Boyle, T.,, V. Lancaster,, R. Hunt,, P. Gemski,, and M. Jett. 1994. Method for simultaneous isolation and quantitation of platelet activating factor and multiple arachidonate metabolites from small samples: analysis of effects of Staphylococcus aureus enterotoxin B in mice. Anal. Biochem. 216: 373– 382.
17. Buerke, M.,, U. Sibelius,, U. Grandel,, U. Buerke,, F. Grimminger,, W. Seeger,, J. Meyer,, and H. Darius. 2002. Staphylococcus aureus alpha toxin mediates polymorphonuclear leukocyte-induced vasocontraction and endothelial dysfunction. Shock 17: 30– 35.
18. Caiazza, N. C.,, and G. A. O’Toole. 2003. Alpha-toxin is required for biofilm formation by Staphylococcus aureus. J. Bacteriol. 185: 3214– 3217.
19. Cavarelli, J.,, G. Prevost,, W. Bourguet,, L. Moulinier,, B. Chevrier,, B. Delagoutte,, A. Bilwes,, L. Mourey,, S. Rifai,, Y. Piemont,, and D. Moras. 1997. The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 Å resolution. Structure 5: 813– 824.
20. Chintagumpala, M. M.,, J. A. Mollick,, and R. R. Rich. 1991. Staphylococcal toxins bind to different sites on HLA-DR. J. Immunol. 147: 3876– 3881.
21. Choi, Y.,, B. Kotzin,, L. Herron,, J. Callahan,, P. Marrack,, and J. Kappler. 1989. Interaction of Staphylococcus aureus toxin superantigens with human T cells. Proc. Natl. Acad. Sci. USA 86: 8941– 8945.
22. Coleman, D. C.,, J. P. Arbuthnott,, H. M. Pomeroy,, and T. H. Birkbeck. 1986. Cloning and expression in Escherichia coli and Staphylococcus aureus of the beta-lysin determinant from Staphylococcus aureus: evidence that bacteriophage conversion of beta-lysin activity is caused by insertional inactivation of the beta-lysin determinant. Microb. Pathog. 1: 549– 564.
23. Colin, D. A.,, I. Mazurier,, S. Sire,, and V. Finck-Barbancon. 1994. Interaction of the two components of leukocidin from Staphylococcus aureus with human polymorphonuclear leukocyte membranes: sequential binding and subsequent activation. Infect. Immun. 62: 3184– 3188.
24. Colin, D. A.,, O. Meunier,, L. Staali,, H. Monteil,, and G. Prevost. 1996. Action mode of two components poreforming leucotoxins from Staphylococcus aureus. Med. Microbiol. Immunol. 185: 107– 114.
25. Cooney, J.,, Z. Kienle,, T. J. Foster,, and P. W. O’Toole. 1993. The gamma-hemolysin locus of Staphylococcus aureus comprises three linked genes, two of which are identical to the genes for the F and S components of leukocidin. Infect. Immun. 61: 678– 771.
26. Deringer, J. R.,, R. J. Ely,, S. R. Monday,, C. V. Stauffacher,, and G. A. Bohach. 1997 Vβ-dependent stimulation of bovine and human T cells by host-specific staphylococcal enterotoxins. Infect. Immun. 65: 4048– 4054.
27. Deringer, J. R.,, R. J. Ely,, C. V. Stauffacher,, and G. A. Bohach. 1996. Subtype-specific interactions of type C staphylococcal enterotoxins with the T-cell receptor. Mol. Microbiol. 22: 523– 534.
28. Dhople, V. M.,, and R. Nagaraj. 2005. Conformation and activity of delta-lysin and its analogs. Peptides 26: 217– 225.
29. Dufourc, E. J.,, J. Dufourcq,, T. H. Birkbeck,, and J. H. Freer. 1990. δ-Haemolysin from Staphylococcus aureus and model membranes. A solid-state 2H-NMR and 31P-NMR study. Eur. J. Biochem. 187: 581– 587.
30. Dziewanowska, K.,, V. E. Edwards,, J. R. Deringer,, G. A. Bohach,, and D. J. Guerra. 1996. Comparison of the β-toxins from Staphylococcus aureus and Staphylococcus intermedius. Arch. Biochem. Biophys. 335: 102– 108.
31. Earhart, C. A.,, D. T. Mitchell,, D. L. Murray,, D. M. Pinheiro,, M. Matsumura,, P. M. Schlievert,, and D. H. Ohlendorf. Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity. Biochemistry 37: 7194– 7202.
32. Edwards, V. M.,, J. R. Deringer,, S. D. Callantine,, C. F. Deobald,, P. H. Berger,, V. Kapur,, C. V. Stauffacher,, and G. A. Bohach. 1997. Characterization of the canine type C enterotoxin produced by Staphylococcus intermedius pyoderma isolates. Infect. Immun. 65: 2346– 2352.
33. Elwell, M. R.,, C. T. Liu,, R. O. Spertzel,, and W. R. Beisel. 1975. Mechanisms of oral staphylococcal enterotoxin B-induced emesis in the monkey. Proc. Soc. Exp. Biol. Med. 148: 424– 427.
34. Essmann, F.,, H. Bantel,, G. Totzke,, I. H. Engels,, B. Sinha,, K. Schulze-Osthoff,, and R. U. Janicke. 2003. Staphylococcus aureus alpha-toxin-induced cell death: predominant necrosis despite apoptotic caspase activation. Cell Death Differ. 10: 1260– 1272.
35. Fields, B. A.,, E. L. Malchiodi,, H. Li,, X. Ysern,, C. V. Stauffacher,, P. M. Schlievert,, K. Karjalainen,, and R. A. Mariuzza. 1996. Crystal structure of a T-cell receptor betachain complexed with a superantigen. Nature 384: 188– 192.
36. Finck-Barbancon, V.,, G. Duportail,, O. Meunier,, and D. A. Colin. 1993. Pore formation by two-component leukocidin from Staphylococcus aureus within the membrane of human polymorphonuclear leukocytes. Biochim. Biophys. Acta 1182: 275– 282.
37. Fitzgerald, J. R.,, S. D. Reid,, E. Ruotsalainen,, T. J. Tripp,, M. Liu,, R. Cole,, P. Kuusela,, P. M. Schlievert,, A. Jarvinen,, and J. M. Musser. 2003. Genome diversification in Staphylococcus aureus: molecular evolution of a highly variable chromosomal region encoding the Staphylococcal exotoxin-like family of proteins. Infect. Immun. 71: 2827– 2838.
38. Fleischer, B.,, and C. J. Bailey. 1992. Recombinant epidermolytic (exfoliative) toxin A of Staphylococcus aureus is not a superantigen. Med. Microbiol. Immunol. 180: 273– 279.
39. Florquin, S.,, and L. Aaldering. 1997. Superantigens: a tool to gain new insight into cellular immunity. Res. Immunol. 148: 373– 386.
40. Foster, T. J.,, M. O’Reilly,, P. Phonimdaeng,, J. Cooney,, A. H. Patel,, and A. J. Bramley,. 1990. Genetic studies of virulence factors of Staphylococcus aureus. Properties of coagulase and gamma-toxin and the role of alpha-toxin, beta-toxin and protein A in the pathogenesis of S. aureus infections, p. 403– 417. In R. P. Novick (ed.), Molecular Biology of the Staphylococci. VCH, Cambridge, New York, N.Y.
41. Fraser, J. D. 1989. High-affinity binding of staphylococcal enterotoxins A and B to HLA-DR. Nature 339: 221– 223.
42. Furoda, M.,, T. Ohta,, I. Uchiyama,, T. Baba,, H. Yuzawa,, I. Kobayashi,, L. Cui,, A. Oguchi,, K. Aoki,, Y. Nagai,, J. Lian,, T. Ito,, M. Kanamori,, H. Matsumaru,, A. Maruyama,, H. Murakami,, A. Hosoyama,, Y. Mizutani-Ui,, N. K. Takahashi,, T. Sawano,, R. Inoue,, C. Kaito,, K. Sekimizu,, H. Hirakawa,, S. Kuhara,, S. Goto,, J. Yabuzaki,, M. Kanehisa,, A. Yamashita,, K. Oshima,, K. Furuya,, C. Yoshino,, T. Shiba,, M. Hattori,, N. Ogasawara,, H. Hayashi,, and K. Hiramatsu. 2001. Whole genome sequencing of methicillin-resistant Staphylococcus aureus. Lancet 357: 1225– 1240.
43. Gase, K.,, J. J. Ferretti,, C. Primeaux,, and W. M. Mc-Shan. 1999. Identification, cloning, and expression of the CAMP factor gene (cfa) of group A streptococci. Infect. Immun. 67: 4725– 4731.
44. Gillet, Y.,, B. Issartel,, P. Vanhems,, J. C. Fournet,, G. Lina,, M. Bes,, F. Vandenesch,, Y. Piemont,, N. Brousse,, D. Floret,, and J. Etienne. 2002. Association between Staphylococcus aureus strains carrying gene for Panton-Valentine leukocidin and highly lethal necrotising pneumonia in young immunocompetent patients. Lancet 359: 753– 759.
45. Grundstrom, S.,, L. Cederbom,, A. Sundstedt,, P. Scheipers,, and F. Ivars. 2003. Superantigen-induced regulatory T cells display different suppressive functions in the presence or absence of natural CD4+CD25+ regulatory T cells in vivo. J. Immunol. 170: 5008– 5017.
46. Goerke, C.,, S. Matias y Papenberg,, S. Dasbach,, K. Dietz,, R. Ziebach,, B. C. Kahl,, and C. Wolz. 2004. Increased frequency of genomic alterations in Staphylococcus aureus during chronic infection is in part due to phage mobilization. J. Infect. Dis. 189: 724– 734.
47. Gravet, A.,, D. Colin,, R. Keller,, H. Giradot,, H. Monteil,, and G. Prevost. 1998. Characterization of a novel structural member, LukE-LukD, of the bi-component staphylococcal leucotoxins family. FEBS Lett. 436: 202– 208.
48. Guillet, V.,, P. Roblin,, S. Werner,, M. Coraiola,, G. Menestrina,, H. Monteil,, G. Prevost,, and L. Mourey. 2004. Crystal structure of leucotoxin S component: new insight into the staphylococcal beta-barrel pore-forming toxins. J. Biol. Chem. 279: 41028– 41037.
49. Hanakawa, Y.,, N. M. Schechter,, C. Lin,, L. Garza,, H. Li,, T. Yamaguchi,, Y. Fudaba,, K. Nishifuji,, M. Sugai,, M. Amagai,, and J. R. Stanley. 2002. Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome. J. Clin. Invest. 110: 53– 60.
50. Hanakawa, Y.,, T. Selwood,, D. Woo,, C. Lin,, N. M. Schechtern,, and J. R. Stanley. 2003. Calcium-dependent conformation of desmoglein 1 is required for its cleavage by exfoliative toxin. J. Invest. Dermatol. 121: 383– 389.
51. Harris, T. O.,, and M. J. Betley. 1995. Biological activities of staphylococcal enterotoxin type A mutants with N-terminal substitutions. Infect. Immun. 63: 2133– 2140.
52. Haslinger, B.,, K. Strangfeld,, G. Peters,, K. Schulze-Osthoff,, and B. Sinha. 2003. Staphylococcus aureus alphatoxin induces apoptosis in peripheral blood mononuclear cells: role of endogenous tumour necrosis factor-alpha and the mitochondrial death pathway. Cell Microbiol. 5: 729– 741.
53. Hildebrand, A.,, M. Roth,, and S. Bhakdi. 1991. Staphylococcus aureus alpha-toxin: dual mechanisms of binding to target cells. J. Biol. Chem. 266: 17195– 17200.
54. Holmberg, S. D.,, and P. A. Blake. 1984. Staphylococcal food poisoning in the United States. New facts and old misconceptions. JAMA 251: 487– 489.
55. Hovde, C. J.,, J. C. Marr,, M. L. Hoffmann,, S. P. Hackett,, Y. I. Chi,, K. K. Crum,, D. L. Stevens,, C. V. Stauffacher,, and G. A. Bohach. 1994. Investigation of the role of the disulphide bond in the activity and structure of staphylococcal enterotoxin C1. Mol. Microbiol. 13: 897– 909.
56. Hudson, K. R.,, R. E. Tiedemann,, R. G. Urban,, S. C. Lowe,, J. L. Strominger,, and J. D. Fraser. 1995. Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II. J. Exp. Med. 182: 711– 720.
57. Jarraud, S.,, G. J. Lyon,, A. M. Figueiredo,, L. Gerard,, F. Vandenesch,, J. Etienne,, T. W. Muir,, and R. P. Novick. 2000. Exfoliatin-producing strains define a fourth agr specificity group in Staphylococcus aureus. J. Bacteriol. 182: 6517– 6522.
58. Jardetsky, T. S.,, J. H. Brown,, J. C. Gorga,, L. J. Stern,, R. G. Urban,, Y. I. Chi,, C. V. Stauffacher,, J. L. Strominger,, and D. C. Wiley. 1994. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature 368: 711– 718.
59. Jarraud, S.,, M. A. Peyrat,, A. Lim,, A. Tristan,, M. Bes,, C. Mougel,, J. Etienne,, F. Vandenesch,, M. Bonneville,, and G. Lina. 2001. egc, a highly prevalent operon of enterotoxin gene, forms a putative nursery of superantigens in Staphylococcus aureus. J. Immunol. 166: 669– 677.
60. Jarvis, W. D.,, R. N. Kolesnick,, F. A. Fornari,, R. S. Traylor,, D. A. Gewirtz,, and S. Grant. 1994. Induction of apoptotic DNA damage and cell death by activation of the sphingomyelin pathway. Proc. Natl. Acad. Sci. USA 91: 73– 77.
61. Jonas, D.,, I. Walev,, T. Berger,, M. Liebetrau,, M. Palmer,, and S. Bhakdi. 1994. Novel path to apoptosis: small transmembrane pores created by staphylococcal alpha-toxin in T lymphocytes evoke internucleosomal DNA degradation. Infect. Immun. 62: 1304– 1312.
62. Kaneko, J.,, O. Toshiko,, T. Tomita,, and Y. Kamio. 1997. Sequential binding of staphylococcal γ-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface. Biosci. Biotechnol. Biochem. 61: 846– 851.
63. Kappler, J.,, B. Kotzin,, L. Herron,, E. W. Gelfand,, R. D. Bigler,, A. Boylston,, S. Carrel,, D. N. Posnett,, Y. Choi,, and P. Marrack. 1989. V beta-specific stimulation of human T cells by staphylococcal toxins. Science 244: 811– 813.
64. Kim, C. S.,, S. Y. Jeon,, Y. G. Min,, C. Rhyoo,, J. W. Kim,, J. B. Yun,, S. W. Park,, and T. Y. Kwon. 2000. Effects of beta-toxin of Staphylococcus aureus on ciliary activity of nasal epithelial cells. Laryngoscope 110: 2085– 2088.
65. Kim, J.,, R. G. Urban,, J. L. Strominger,, and D. C. Wiley. 1994. Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1. Science 266: 1870– 1874.
66. Leder, L.,, A. Llera,, P. M. Lavoie,, M. I. Lebedeva,, H. Li,, R. P. Sekaly,, G. A. Bohach,, P. J. Gahr,, P. M. Schlievert,, K. Karjalainen,, and R. A. Mariuzza. 1998. A mutational analysis of the binding of staphylococcal enterotoxins B and C3 to the T cell receptor beta chain and major histocompatibility complex class II. J. Exp. Med. 187: 823– 833.
67. Letertre, C.,, S. Perelle,, F. Dilasser,, and P. Fach. 2003. Identification of a new putative enterotoxin SEU encoded by the egc cluster of Staphylococcus aureus. J. Appl. Microbiol. 95: 38– 43.
68. Lina, G.,, G. A. Bohach,, S. P. Nair,, K. Hiramatsu,, E. Jouvin-Marche,, and R. Mariuzza, International Nomenclature Committee for Staphylococcal Superantigens. 2004. Standard nomenclature for the superantigens expressed by Staphylococcus. J. Infect. Dis. 189: 2334– 2336.
69. Lina, G.,, Y. Piemont,, F. Godail-Gamot,, M. Bes,, M. O. Peter,, V. Gauduchon,, F. Vandenesch,, and J. Etienne. 1999. Involvement of Panton-Valentine leukocidin-producing Staphylococcus aureus in primary skin infections and pneumonia. Clin. Infect. Dis. 29: 1128– 1132.
70. Low, D. K. R.,, and J. H. Freer. 1977. Biological effects of highly purified β-lysin (sphingomyelinase C) from Staphylococcus aureus. FEMS Microbiol. Lett. 2: 133– 138.
71. Mahlknecht, U.,, M. Herter,, M. K. Hoffmann,, D. Niethammer,, and G. E. Dannecker. 1996. The toxic shock syndrome toxin-1 induces anergy in human T cells in vivo. Hum. Immunol. 45: 42– 45.
72. Marshall, M. J.,, G. A. Bohach,, and D. F. Boehm. 2000. Characterization of Staphylococcus aureus beta-toxin induced leukotoxicity. J. Nat. Toxins 9: 125– 138.
73. Melish, M. E.,, and L. A. Glasgow. 1970. The staphylococcal scalded skin syndrome: development of an experimental model. N. Engl. J. Med. 282: 1114– 1119.
74. Mellor, I. R.,, D. H. Thomas,, and M. S. P. Sansom. 1988. Properties of ion channels formed by Staphylococcus aureus δ-toxin. Biochim. Biophys. Acta 942: 280– 294.
75. Mempel, M.,, C. Schnopp,, M. Hojka,, H. Fesq,, S. Weidinger,, M. Schaller,, H. C. Korting,, J. Ring,, and D. Abeck. 2002. Invasion of human keratinocytes by Staphylococcus aureus and intracellular bacterial persistence represent haemolysin-independent virulence mechanisms that are followed by features of necrotic and apoptotic keratinocyte cell death. Br. J. Dermatol. 146: 943– 951.
76. Menestrina, G.,, M. D. Serra,, and G. Prevost. 2001. Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family. Toxicon 39: 1661– 1672.
77. Miles, G.,, L. Movileanu,, and H. Bayley. 2002. Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore. Protein Sci. 11: 894– 902.
78. Monday, S. R.,, and G. A. Bohach,. 1999. Genetic, structural, biological, pathophysiological and clinical aspects of Staphylococcus aureus enterotoxins and toxic shock syndrome toxin-1, p. 589– 610. In J. E. Alouf, and J. H. Freer (ed.), Sourcebook of Bacterial Protein Toxins. Academic Press, London, United Kingdom.
79. Monday, S. R.,, and G. A. Bohach. 2000. Genes encoding staphylococcal enterotoxins are linked and separated by DNA related to other staphylococcal enterotoxins. J. Nat. Toxins 10: 1– 8.
80. Monday, S. R.,, G. M. Vath,, W. A. Ferens,, C. Deobald,, J. V. Rago,, P. J. Gahr,, D. Monie,, J. J. Iandolo,, S. K. Chapes,, W. C. Davis,, D. H. Ohlendorf,, P. M. Schlievert,, and G. A. Bohach. 1999. Unique superantigen activity of staphylococcal exfoliative toxins. J. Immunol. 181: 4550– 4559.
81. Munson, S. H.,, M. T. Tremaine,, M. J. Betley,, and R. A. Welch. 1998. Identification and characterization of staphylococcal enterotoxin types G and I from Staphylococcus aureus. Infect. Immun. 66: 3337– 3348.
82. Narita, S.,, J. Kaneko,, J. Chiba,, Y. Piemont,, S. Jarraud,, J. Etienne,, and Y. Kamio. 2001. Phage conversion of Panton-Valentine leukocidin in Staphylococcus aureus: molecular analysis of a PVL-converting phage, ϕSLT. Gene 268: 195– 206.
83. Noda, M.,, and I. Kato,. 1991. Leukocidal toxins, p. 243– 251. In J. E. Alouf, and J. H. Freer (ed.), Sourcebook of Bacterial Protein Toxins. Academic Press, London, United Kingdom.
84. O’Callaghan, R. J.,, M. C. Callegan,, J. M. Moreau,, L. C. Green,, T. J. Foster,, O. M. Hartford,, L. S. Engel,, and J. M. Hill. 1997. Specific roles of alpha-toxin and beta-toxins during Staphylococcus corneal infection. Infect. Immun. 65: 1571– 1578.
85. Omoe, K.,, K. Imanishi,, D. L. Hu,, H. Kato,, H. Takahashi-Omoe,, A. Nakane,, T. Uchiyama,, and K. Shinagawa. 2004. Biological properties of staphylococcal enterotoxin-like toxin type R. Infect. Immun. 72: 3664– 3667.
86. Omoe, K.,, D. L. Hu,, H. Takahashi-Omoe,, A. Nakane,, and K. Shinagawa. 2003. Identification and characterization of a new staphylococcal enterotoxin-related putative toxin encoded by two kinds of plasmids. Infect. Immun. 71: 6088– 6094.
87. Onogawa, T. 2002. Staphylococcal alpha-toxin synergistically enhances inflammation caused by bacterial components. FEMS Immunol. Med. Microbiol. 33: 15– 21.
88. Orwin, P. M.,, J. Fitzgerald,, D. Y. Leung,, J. A. Gutierrez,, G. A. Bohach,, and P. M. Schlievert. 2003. Characterization of Staphylococcus aureus enterotoxin L. Infect. Immun. 71: 2916– 2919.
89. Orwin, P. M.,, D. Y. Leung,, D. H. Donahue,, R. P. Novick,, and P. M. Schlievert. 2001. Biochemical and biological properties of Staphylococcal enterotoxin K. Infect. Immun. 69: 360– 366.
90. Orwin, P. M.,, D. Y. Leung,, T. J. Tripp,, G. A. Bohach,, C. A. Earhart,, D. H. Ohlendorf,, and P. M. Schlievert. 2002. Characterization of a novel staphylococcal enterotoxin- like superantigen, a member of the group V subfamily of pyrogenic toxins. Biochemistry 41: 14033– 14040.
91. Ozawa, T.,, J. Kaneko,, and Y. Kamio. 1995. Essential binding of LukF of staphylococcal γ-hemolysin followed by the binding of HγII for the hemolysis of human erythrocytes. Biosci. Biotech. Biochem. 559: 1181– 1183.
92. Ozawa, T.,, J. Kaneko,, H. Narija,, K. Izaki,, and Y. Kamio. 1994. Inactivation of the γ-hemolysin HγII component by addition of monoganglioside G MI to human erythrocyte. Biosci. Biotech. Biochem. 58: 602– 605.
93. Park, P. W.,, T. J. Foster,, E. Nishi,, S. J. Duncan,, M. Klagsbrun,, and Y. Chen. 2004. Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus alpha-toxin and beta-toxin. J. Biol. Chem. 279: 251– 258.
94. Parsonnet, J., 1998. Case definition of staphylococcal TSS: a proposed revision incorporating laboratory findings, p. 15. In F. Arbuthnott, and B. Furman (ed.), Proceedings of the European Conference on Toxic Shock Syndrome. T he Royal Society of Medicine Limited, London, United Kingdom.
95. Petersson, K.,, H. Pettersson,, N. J. Skartved,, B. Walse,, and G. Forsberg. 2003. Staphylococcal enterotoxin H induces V alpha-specific expansion of T cells. J. Immunol. 170: 4148– 4154.
96. Petersson, K.,, M. Hakansson,, H. Nilsson,, G. Forsberg,, L. A. Svensson,, A. Liljas,, and B. Walse. 2001. Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence. EMBO J. 20: 3306– 3312.
97. Plano, L. R.,, B. Adkins,, M. Woischnik,, R. Ewing,, and C. M. Collins. 2001. Toxin levels in serum correlate with the development of staphylococcal scalded skin syndrome in a murine model. Infect. Immun. 69: 5193– 5197.
98. Plano, L. R.,, D. M. Gutman,, M. Woischnik,, and C. M. Collins. 2000. Recombinant Staphylococcus aureus exfoliative toxins are not bacterial superantigens. Infect. Immun. 68: 3048– 3052.
99. Pokorny, A.,, T. H. Birkbeck,, and P. F. Almeida. 2002. Mechanism and kinetics of delta-lysin interaction with phospholipid vesicles. Biochemistry 41: 11044– 11056.
100. Prevost, G.,, P. Coupie,, P. Prevost,, S. Gayet,, P. Petiau,, B. Cribier,, H. Monteil,, and Y. Piemont. 1995. Epidemiological data on Staphylococcus aureus strains producing synergohymenotropic toxins. J. Med. Microbiol. 42: 237– 245.
101. Prevost, G.,, B. Cribier,, P. Couppie,, P. Petiau,, G. Supersac,, V. Finck-Barbancon,, H. Monteil,, and Y. Piemont. 1995. Panton-Valentine leucocidin and gammahemolysin from Staphylococcus aureus ATCC 49775 are encoded by distinct genetic loci and have different biological activities. Infect. Immun. 63: 4121– 4129.
102. Prevost, G.,, S. Rifai,, M. L. Chaix,, S. Meyer,, and Y. Piemont,. 1992. Is the His72, Asp120, Ser195 constitutive of the catalytic site of staphylococcal exfoliative toxin A? p. 488– 489. In B. Witholt (ed.), Bacterial Protein Toxins. Fischer, Stuttgart, Germany.
103. Projan, S. J.,, J. Kornblum,, B. Kreiswirth,, S. L. Moghazeh,, W. Eisner,, and R. P. Novick. 1989. Nucleotide sequence: the β-hemolysin gene of Staphylococcus aureus. Nucleic Acids Res. 17: 3305.
104. Rago, J. V.,, G. M. Vath,, T. J. Tripp,, G. A. Bohach,, D. H. Ohlendorf,, and P. M. Schlievert. 2000. Staphylococcal exfoliative toxins cleave alpha- and beta-melanocyte-stimulating hormones. Infect. Immun. 68: 2366– 2368.
105. Redpath, M. B.,, T. J. Foster,, and C. J. Bailey. 1991. The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus. FEMS Microbiol. Lett. 81: 151– 156.
106. Reingold, A. L.,, N. T. Hargrett,, K. N. Shands,, B. B. Dan,, G. P. Schmid,, B. Y. Strickland,, and C. V. Broome. 1982. Toxic shock syndrome surveillance in the United States, 1980 to 1981. Ann. Intern. Med. 96: 875– 880.
107. Ren, K.,, J. D. Bannan,, V. Pancholi,, A. L. Cheung,, J. C. Robbins,, V. A. Fischetti,, and J. B. Zabriskie. 1994. Characterization and biological properties of a new staphylococcal exotoxin. J. Exp. Med. 180: 1675– 1683.
108. Rich, R. R.,, J. A. Mollick,, and R. G. Cook. 1989. Superantigens: interaction of staphylococcal enterotoxins with MHC class II molecules. Trans. Am. Clin. Climatol. Assoc. 101: 195– 204.
109. Rogalsky, M. 1979. Nonenteric toxins of Staphyloccus aureus. Microbiol. Rev. 43: 320– 360.
110. Sato, H.,, K. Hirose,, R. Terauchi,, S. Abe,, I. Moromizato,, S. Kurokawa,, and N. Maehara. 2004. Purification and characterization of a novel Staphylococcus chromogenes exfoliative toxin. J. Vet. Med. B Infect. Dis. Vet. Public Health 51: 116– 122.
111. Scheuber, P. H.,, C. Denzlinger,, D. Wilker,, G. Beck,, D. Keppler,, and D. K. Hammer. 1987. Staphylococcal enterotoxin B as a nonimmunological mast cell stimulus in primates: the role of endogenous cysteinyl leukotrienes. Int. Arch. Allergy. Appl. Immunol. 82: 289– 291.
112. Smith, T. P.,, D. A. John,, and C. J. Bailey. 1987. The binding of epidermolytic toxin from Staphylococcus aureus to mouse epidermal tissue. Histochem. J. 19: 137– 149.
113. Smyth, D. S.,, P. J. Hartigan,, W. J. Meaney,, J. R. Fitzgerald,, C. F. Deobald,, G. A. Bohach,, and C. J. Smyth. 2005. Superantigen genes encoded by the egc cluster and SaPIbov are predominant among Staphylococcus aureus isolates from cows, goats, sheep, rabbits and poultry. J. Med. Microbiol. 54: 401– 411.
114. Somerville, G. A.,, A. Cockayne,, M. Durr,, A. Peschel,, M. Otto,, and J. M. Musser. 2003. Synthesis and deformylation of Staphylococcus aureus delta-toxin are linked to tricarboxylic acid cycle activity. J. Bacteriol. 185: 6686– 6694.
115. Song, L.,, M. R. Hobaugh,, C. Shustak,, S. Cheley,, H. Bayley,, and J. E. Gouaux. 1996. Structure of the staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274: 1859– 1865.
116. Stohl, W.,, J. E. Elliott,, D. H. Lynch,, and P. A. Kiener. 1998. CD95 (Fas)-based, superantigen-dependent, CD4+ T cell-mediated down-regulation of human in vitro immunoglobulin responses. J. Immunol. 160: 5231– 5238.
117. Sugawara, N.,, T. Tomita,, and Y. Kamio. 1997. Assembly of γ-hemolysin into a pore-forming ring-shaped complex on the surface of human erythrocytes. FEBS Lett. 410: 333– 337.
118. Sugawara-Tomita, N.,, T. Tomita,, and Y. Kamio. 2002. Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3. J. Bacteriol. 184: 4747– 4756.
119. Sundstrom, M.,, L. Abrahmsen,, P. Antonsson,, K. Mehindate,, W. Mourad,, and M. Dohlsten. 1996. The crystal structure of staphylococcal enterotoxin type D reveals Zn 2+-mediated homodimerization. EMBO J. 15: 6832– 6840.
120. Tappin, M. J.,, A. Pastore,, R. S. Norton,, J. H. Freer,, and I. D. Campbell. 1988. High-resolution 1H NMR study of the solution structure of δ-hemolysin. Biochemistry 27: 1643– 1647.
121. Terauchi, R.,, H. Sato,, Y. Endo,, C. Aizawa,, and N. Maehara. 2003. Cloning of the gene coding for Staphylococcus intermedius exfoliative toxin and its expression in Escherichia coli. Vet. Microbiol. 94: 31– 38.
122. Tiedemann, R. E.,, and J. D. Fraser. 1996. Cross-linking of MHC class II molecules by staphylococcal enterotoxin A is essential for antigen-presenting cell and T cell activation. J. Immunol. 157: 3958– 3966.
123. Tomita, T.,, Y. Ueda,, H. Tamura,, R. Taguchi,, and H. Ikezawa. 1993. The role of acidic amino-acid residues in catalytic and adsorptive sites of Bacillus cereus sphingomyelinase. Biochim. Biophys. Acta 1203: 85– 92.
124. Valeva, A.,, A. Weisser,, B. Walker,, M. Kehoe,, H. Bayley,, S. Bhakdi,, and M. Palmer. 1996. Molecular architecture of a toxin pore: a 15 residue sequence lines the transmembrane channel of staphylococcal alpha-toxin. EMBO J. 15: 1857– 1864.
125. Vandenesch, F.,, T. Naimi,, M. C. Enright,, G. Lina,, G. R. Nimmo,, H. Heffernan,, N. Liassine,, M. Bes,, T. Greenland,, M. E. Reverdy,, and J. Etienne. 2003. Community-acquired methicillin-resistant Staphylococcus aureus carrying Panton-Valentine leukocidin genes: worldwide emergence. Emerg. Infect. Dis. 9: 978– 984.
126. Vath, G. M.,, C. A. Earhart,, D. D. Monie,, J. J. Iandolo,, P. M. Schlievert,, and D. H. Ohlendorf. 1999. The crystal structure of exfoliative toxin B: a superantigen with enzymatic activity. Biochemistry 38: 10239– 10246.
127. Vath, G. M.,, C. A. Earhart,, J. V. Rago,, M. H. Kim,, G. A. Bohach,, P. M. Schlievert,, and D. H. Ohlendorf. 1997. The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease. Biochemistry 36: 1559– 1566.
128. von Eiff, C.,, R. A. Proctor,, and G. Peters. 2000. Small colony variants of staphylococci: a link to persistent infections. Berl. Munch. Tierarztl. Wochenschr. 113: 321– 325.
129. Walev, I.,, U. Weller,, S. Strauch,, T. Foster,, and S. Bhakdi. 1996. Selective killing of human monocytes and cytokine release provoked by sphingomyelinase (beta toxin) of Staphylococcus aureus. Infect. Immun. 64: 2974– 2979.
130. White, J.,, A. Herman,, A. M. Pullen,, R. Kubo,, J. W. Kappler,, and P. Marrack. 1989. The V beta-specific superantigen staphylococcal enterotoxin B: stimulation of mature T cells and clonal deletion in neonatal mice. Cell 56: 27– 35.
131. Williams, R. E. O.,, and G. H. Harper. 1947. Staphylococcal haemolysins on sheep blood agar with evidence for a fourth haemolysin. J. Pathol. Bacteriol. 59: 69– 78.
132. Williams, R. J.,, J. M. Ward,, B. Henderson,, S. Poole,, B. P. O’Hara,, M. Wilson,, S. P. Nair. 2000. Identification of a novel gene cluster encoding staphylococcal exotoxin-like proteins: characterization of the prototypic gene and its protein product, SET1. Infect. Immun. 68: 4407– 4415.
133. Wiseman, G. M. 1975. The hemolysins of Staphylococcus aureus. Bacteriol. Rev. 39: 317– 344.
134. Woodin, A. M., 1970. Staphylococcal leukocidin, p. 327– 355. In T. C. Montie,, S. Kadis,, and S. J. Ajl (ed.), Microbial Toxins. Academic Press, New York, N.Y.
135. Yamaguchi, T.,, T. Hayashi,, H. Takami,, K. Nakasone,, M. Ohnishi,, K. Nakayama,, S. Yamada,, H. Komatsuzawa,, and M. Sugai. 2000. Phage conversion of exfoliative toxin A production in Staphylococcus aureus. Mol. Microbiol. 38: 694– 705.
136. Yamaguchi, T.,, T. Hayashi,, H. Takami,, M. Ohnishi,, T. Murata,, K. Nakayama,, K. Asakawa,, M. Ohara,, H. Komatsuzawa,, and M. Sugai. 2001. Complete nucleotide sequence of a Staphylococcus aureus exfoliative toxin B plasmid and identification of a novel ADP-ribosyltransferase, EDIN-C. Infect. Immun. 69: 7760– 7771.
137. Yamaguchi, T.,, K. Nishifuji,, M. Sasaki,, Y. Fudaba,, M. Aepfelbacher,, T. Takata,, M. Ohara,, H. Komatsuzawa,, M. Amagai,, and M. Sugai. 2002. Identification of the Staphylococcus aureus etd pathogenicity island which encodes a novel exfoliative toxin, ETD, and EDIN-B. Infect. Immun. 70: 5835– 5845.
138. Yoshizawa, Y.,, J. Sakurada,, S. Sakurai,, K. Machida,, I. Kondo,, and S. Masuda. 2000. An exfoliative toxin A-converting phage isolated from Staphylococcus aureus strain ZM. Microbiol. Immunol. 44: 189– 191.
139. Zhang, S.,, J. J. Iandolo,, and G. C. Stewart. 1998. The enterotoxin D plasmid of Staphylococcus aureus encodes a second enterotoxin determinant ( sej). FEMS Microbiol. Lett. 168: 227– 233.
140. Zou, D.,, J. Kaneko,, S. Narita,, and Y. Kamio. 2000. Prophage,ϕPV83-pro, carrying panton-valentine leukocidin genes, on the Staphylococcus aureus P83 chromosome: comparative analysis of the genome structures of ϕPV83-pro, ϕPVL, ϕ11, and other phages. Biosci. Biotechnol. Biochem. 64: 2631– 2643.

Tables

Staphylococcus aureus Exotoxins
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555816513.chap38-1,webId=/content/author/10.1128/9781555816513.chap38-1,properties={foaf_givenname=Gregory A., foaf_name=Gregory A. Bohach, foaf_surname=Bohach}]]
Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38
/content/10.1128/9781555816513.chap38.tab38-1
TABLE 1

Reported, confirmed, or potential staphylococcal PTSAgs

SE nomenclature used in this table is that recommended by the International Nomenclature Committee for Staphylococcal Superantigens ( ). Toxins either lacking activity or not yet tested for emetic activity in the primate oral feeding assay are designated staphylococcal enterotoxin-like toxins (SEls), according to standard nomenclature ( ).

ND, not determined or reported.

Weakly emetic ( ).

Nonemetic.

Originally designated SEK ( ).

Originally designated SEL ( ).

Originally designated SEM ( ).

T-cell stimulation reportedly results from Vα stimulation ( ).

10.1128/9781555816513/tab38-1_thmb.gif
10.1128/9781555816513/tab38-1.gif
Generic image for table
TABLE 1

Reported, confirmed, or potential staphylococcal PTSAgs

SE nomenclature used in this table is that recommended by the International Nomenclature Committee for Staphylococcal Superantigens ( ). Toxins either lacking activity or not yet tested for emetic activity in the primate oral feeding assay are designated staphylococcal enterotoxin-like toxins (SEls), according to standard nomenclature ( ).

ND, not determined or reported.

Weakly emetic ( ).

Nonemetic.

Originally designated SEK ( ).

Originally designated SEL ( ).

Originally designated SEM ( ).

T-cell stimulation reportedly results from Vα stimulation ( ).

Citation: Bohach G. 2006. Exotoxins, p 464-477. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch38

Back to top
This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error