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SETBP1  -  SET binding protein 1

Homo sapiens

 
 
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Disease relevance of SETBP1

 

High impact information on SETBP1

  • We interpret these results in terms of the ability of SEC to activate T cells independently of MHC, in contrast to SEB [6].
  • Thus, unlike, SEB, SEA requires two separate binding sites for optimal activity, which may allow it to stabilize SEA interaction with T cell receptors, as well as to activate the antigen-presenting cell by cross-linking MHC class II [7].
  • The much weaker binding to SEB than to SEC1, 2, or 3 was surprising, especially since SEB was found to actually be 3- to 10-fold more effective, on a molar basis, than the other toxins in stimulating the parental T cell hybridoma [6].
  • The addition of SEB to these transfectants resulted in the downregulation of cell surface TCR expression, an increase in the concentration of intracellular calcium ions, the production of lymphokines, and reduced responsiveness to a subsequent challenge with SEB [8].
  • The disulfide linkage imparts considerable stability to these toxins as peptide cleavages within the loop of SEB were not associated with detectable loss of function, although cleavage in the conserved sequence outside the loop of SEA resulted in loss of mitogenic activity [9].
 

Chemical compound and disease context of SETBP1

  • To determine whether staphylococci causing bovine mastitis could cause human foodborne intoxication, the production of staphylococcal enterotoxins A through D (SEA, SEB, SEC, and SED) by 160 S. aureus isolates was evaluated with the use of a reverse passive latex agglutination enterotoxin kit [10].
 

Biological context of SETBP1

  • Fluorescent in situ hybridisation showed NUP98 and SET binding protein 1(SETBP1) fusion signals; other analyses showed that exon 12 of NUP98 was fused in-frame with exon 5 of SETBP1 [11].
  • RESULTS: The SETs SEA, SEB, SEC, and toxic shock syndrome toxin 1 significantly inhibited eosinophil apoptosis in a manner comparable with that of high concentrations of IL-3 [12].
  • In the present study, we have demonstrated that contrary to SEA, stimulation of the human monocytic cell line THP-1 with SEB or TSST-1 failed to induce interleukin-1 beta or tumor necrosis factor-alpha gene expression [13].
  • However, cross-linking of SEB or TSST-1 bound to MHC class II molecules with specific antibodies leads to cytokine gene expression, indicating that dimerization of class II molecules is a requirement for this superantigen-induced response [13].
  • Although staphylococcal enterotoxin A (SEA), B (SEB), and toxic shock syndrome toxin 1 (TSST-1) bind to major histocompatibility complex (MHC) class II molecules, they differ in their mode of binding [13].
 

Anatomical context of SETBP1

  • Fusion of NUP98 and the SET binding protein 1 (SETBP1) gene in a paediatric acute T cell lymphoblastic leukaemia with t(11;18)(p15;q12) [11].
  • To analyze the dominant B cell epitopes on the bacterial superantigen SEB (staphylococcal enterotoxin B), we constructed fusion proteins of SEB deletion mutants, and the reactivities of these recombinant proteins to i.v. IgG and healthy human sera were evaluated by means of immunoblotting [14].
  • Scatchard analysis of equilibrium binding data indicate that SEB binds to Ia+ human cell lines with a 10-fold lower affinity than TSST-1 [15].
  • Blood and lung lymphocytes were also assessed for their responsiveness to different superantigenic stimuli represented by staphylococcal enterotoxins (SEA, SEB, SEC1, SEC2, SED and SEE) [16].
  • In support of this concept, we observed that proliferation of naive cells to anti-CD3 mAb and SEA or SEB (but not to anti-CD2 mAb pairs) was consistently enhanced by pre-activation of monocytes present in the culture [17].
 

Associations of SETBP1 with chemical compounds

  • The amino terminus of the purified streptococcal superantigen was more homologous to the amino termini of staphylococcal enterotoxins B, C1, and C3 (SEB, SEC1, and SEC3), than to those of pyrogenic exotoxins A, B, C or other streptococcal toxins [18].
  • The mutant, in which residues 226-229 of SEB were exchanged for residues 209-212 of streptococcal pyrogenic exotoxin A, reduced the reactivity with the C-terminal region-specific IgG purified by affinity chromatography [14].
  • SEA, but neither SEB nor TSST-1 impedes avidin access to a biotin group attached to the amino terminus of HA 307-319 [19].
  • Furthermore, H-7 inhibited the expression of the monokine mRNA induced by SEB, suggesting the involvement of protein kinase C (PKC) in the signaling pathway [20].
  • Preincubation of the enzyme with UDP-D-glucose stimulated incorporation from UDP-D-[14C]xylose, suggesting an 'imprecise' mechanism of biosynthesis, as defined by Waldron & Brett [(1985) in Biochemistry of Plant Cell Walls (Brett, C. T. & Hillman, J. R., eds.) (SEB Semin. Ser. 28), pp. 79-97, Cambridge University Press, Cambridge] [21].
 

Analytical, diagnostic and therapeutic context of SETBP1

  • Intra-observer variability: results of LVM measurements obtained in cadaver hearts by observer 1 and in in vivo studies by observer 2 were y = 1.001 x -1.34, r = 0.99, SEB = 6 g and y = 0.99 x +3.78, r = 0.99, SEE = 19 g, respectively [22].
  • Production of SEB and TSST-1 in the culture supernatants from 344 Staphylococcus aureus isolates was quantitated by noncompetitive ELISA (lower detection limit, 0.5 ng/mL for both assays) [23].
  • We previously showed that monolayers of human T84 epithelial cells display altered ion transport and permeability after coculture with Staphylococcus aureus enterotoxin B (SEB, a model superantigen)-activated immune cells, where interferon-gamma and tumor necrosis factor-alpha were key mediators in the pathophysiology [24].
  • We conclude that IL-10 can reduce the epithelial functional changes caused by SEB-activated immune cells and this data adds further support for IL-10 immunotherapy in the treatment of intestinal secretory or inflammatory disorders [24].
  • Ham spiked with 5 or 40 micrograms SEB per 100 g food resulted in biosensor readings indicative of 11 or 69% recovery of the toxin, respectively [25].

References

  1. Correction of X-linked chronic granulomatous disease by gene therapy, augmented by insertional activation of MDS1-EVI1, PRDM16 or SETBP1. Ott, M.G., Schmidt, M., Schwarzwaelder, K., Stein, S., Siler, U., Koehl, U., Glimm, H., Kühlcke, K., Schilz, A., Kunkel, H., Naundorf, S., Brinkmann, A., Deichmann, A., Fischer, M., Ball, C., Pilz, I., Dunbar, C., Du, Y., Jenkins, N.A., Copeland, N.G., Lüthi, U., Hassan, M., Thrasher, A.J., Hoelzer, D., von Kalle, C., Seger, R., Grez, M. Nat. Med. (2006) [Pubmed]
  2. The CD4 molecule is not always required for the T cell response to bacterial enterotoxins. Sékaly, R.P., Croteau, G., Bowman, M., Scholl, P., Burakoff, S., Geha, R.S. J. Exp. Med. (1991) [Pubmed]
  3. Presence of IgE antibodies to staphylococcal exotoxins on the skin of patients with atopic dermatitis. Evidence for a new group of allergens. Leung, D.Y., Harbeck, R., Bina, P., Reiser, R.F., Yang, E., Norris, D.A., Hanifin, J.M., Sampson, H.A. J. Clin. Invest. (1993) [Pubmed]
  4. T-cell epitope analysis using subtracted expression libraries (TEASEL): application to a 38-kDA autoantigen recognized by T cells from an insulin-dependent diabetic patient. Neophytou, P.I., Roep, B.O., Arden, S.D., Muir, E.M., Duinkerken, G., Kallan, A., de Vries, R.R., Hutton, J.C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  5. Direct demonstration of cytokine synthesis heterogeneity among human memory/effector T cells by flow cytometry. Picker, L.J., Singh, M.K., Zdraveski, Z., Treer, J.R., Waldrop, S.L., Bergstresser, P.R., Maino, V.C. Blood (1995) [Pubmed]
  6. Superantigen binding to a T cell receptor beta chain of known three-dimensional structure. Malchiodi, E.L., Eisenstein, E., Fields, B.A., Ohlendorf, D.H., Schlievert, P.M., Karjalainen, K., Mariuzza, R.A. J. Exp. Med. (1995) [Pubmed]
  7. Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II. Hudson, K.R., Tiedemann, R.E., Urban, R.G., Lowe, S.C., Strominger, J.L., Fraser, J.D. J. Exp. Med. (1995) [Pubmed]
  8. Major histocompatibility complex independent clonal T cell anergy by direct interaction of Staphylococcus aureus enterotoxin B with the T cell antigen receptor. Hewitt, C.R., Lamb, J.R., Hayball, J., Hill, M., Owen, M.J., O'Hehir, R.E. J. Exp. Med. (1992) [Pubmed]
  9. Dissociation of the stimulatory activities of staphylococcal enterotoxins for T cells and monocytes. Grossman, D., Cook, R.G., Sparrow, J.T., Mollick, J.A., Rich, R.R. J. Exp. Med. (1990) [Pubmed]
  10. Enterotoxin production by Staphylococcus aureus isolated from mastitic cows. Cenci-Goga, B.T., Karama, M., Rossitto, P.V., Morgante, R.A., Cullor, J.S. J. Food Prot. (2003) [Pubmed]
  11. Fusion of NUP98 and the SET binding protein 1 (SETBP1) gene in a paediatric acute T cell lymphoblastic leukaemia with t(11;18)(p15;q12). Panagopoulos, I., Kerndrup, G., Carlsen, N., Strömbeck, B., Isaksson, M., Johansson, B. Br. J. Haematol. (2007) [Pubmed]
  12. Staphylococcal exotoxins exert proinflammatory effects through inhibition of eosinophil apoptosis, increased surface antigen expression (CD11b, CD45, CD54, and CD69), and enhanced cytokine-activated oxidative burst, thereby triggering allergic inflammatory reactions. Wedi, B., Wieczorek, D., Stünkel, T., Breuer, K., Kapp, A. J. Allergy Clin. Immunol. (2002) [Pubmed]
  13. Synergistic effect between CD40 and class II signals overcome the requirement for class II dimerization in superantigen-induced cytokine gene expression. Mehindate, K., al-Daccak, R., Damdoumi, F., Mourad, W. Eur. J. Immunol. (1996) [Pubmed]
  14. B cell epitope mapping of the bacterial superantigen staphylococcal enterotoxin B: the dominant epitope region recognized by intravenous IgG. Nishi, J.I., Kanekura, S., Takei, S., Kitajima, I., Nakajima, T., Wahid, M.R., Masuda, K., Yoshinaga, M., Maruyama, I., Miyata, K. J. Immunol. (1997) [Pubmed]
  15. Staphylococcal enterotoxin B and toxic shock syndrome toxin-1 bind to distinct sites on HLA-DR and HLA-DQ molecules. Scholl, P.R., Diez, A., Geha, R.S. J. Immunol. (1989) [Pubmed]
  16. Skewing of the T-cell receptor repertoire in the lung of patients with HIV-1 infection. Trentin, L., Zambello, R., Facco, M., Sancetta, R., Cerutti, A., Milani, A., Tassinari, C., Crivellaro, C., Cipriani, A., Agostini, C., Semenzato, G. AIDS (1996) [Pubmed]
  17. Hyporesponsiveness of "naive" (CD45RA+) human T cells to multiple receptor-mediated stimuli but augmentation of responses by co-stimuli. Horgan, K.J., Van Seventer, G.A., Shimizu, Y., Shaw, S. Eur. J. Immunol. (1990) [Pubmed]
  18. A novel superantigen isolated from pathogenic strains of Streptococcus pyogenes with aminoterminal homology to staphylococcal enterotoxins B and C. Mollick, J.A., Miller, G.G., Musser, J.M., Cook, R.G., Grossman, D., Rich, R.R. J. Clin. Invest. (1993) [Pubmed]
  19. Inhibition of antigen-specific T cell activation by staphylococcal enterotoxins. Dowd, J.E., Jenkins, R.N., Karp, D.R. J. Immunol. (1995) [Pubmed]
  20. HLA class II molecule-mediated signal transduction mechanism responsible for the expression of interleukin-1 beta and tumor necrosis factor-alpha genes induced by a staphylococcal superantigen. Matsuyama, S., Koide, Y., Yoshida, T.O. Eur. J. Immunol. (1993) [Pubmed]
  21. A xylosyltransferase involved in the synthesis of a protein-associated xyloglucan in suspension-cultured dwarf-French-bean (Phaseolus vulgaris) cells and its interaction with a glucosyltransferase. Campbell, R.E., Brett, C.T., Hillman, J.R. Biochem. J. (1988) [Pubmed]
  22. Determination of left ventricular mass with electron beam computed tomography in deformed, hypertrophic human hearts. Mousseaux, E., Beygui, F., Fornès, P., Chatellier, G., Hagège, A., Desnos, M., Lecomte, D., Gaux, J.C. Eur. Heart J. (1994) [Pubmed]
  23. Detection of staphylococcal enterotoxin B among toxic shock syndrome (TSS)- and non-TSS-associated Staphylococcus aureus isolates. Lee, V.T., Chang, A.H., Chow, A.W. J. Infect. Dis. (1992) [Pubmed]
  24. Epithelial ion transport and barrier abnormalities evoked by superantigen-activated immune cells are inhibited by interleukin-10 but not interleukin-4. Lu, J., Philpott, D.J., Saunders, P.R., Perdue, M.H., Yang, P.C., McKay, D.M. J. Pharmacol. Exp. Ther. (1998) [Pubmed]
  25. Quantitating staphylococcal enterotoxin B in diverse media using a portable fiber-optic biosensor. Tempelman, L.A., King, K.D., Anderson, G.P., Ligler, F.S. Anal. Biochem. (1996) [Pubmed]
 
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