Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Iandolo, J.J. Genetic analysis of extracellular toxins of Staphylococcus aureus. Annu. Rev. Microbiol. 43, 375 (1989).
Tao, M., H. Yamashita, K. Watanabe and T. Nagatake. Possible virulence factors of Staphylococcus aureusin amouse septic model. FEMS Immunology 23, 135 (1999).
Johnson, H., J. Russell and C. Pontzer. Staphylococcal enterotoxin microbial superantigens. FASEB J. 5, 2706 (1991).
Betley, M., D. Borst and L. Regassa. in Biological significance of superantigens (ed. B. Fleischer) p. 1 (Karger, Basel, 1992).
Zhang, S., J. J. Iandolo and G. C. Stewart. The enterotoxin D plasmid of Staphylococcus aureus encodes a second enterotoxin determinant (sej). FEMS Microbiol. Lett. 168, 227 (1998).
Bergdoll, M. in Food bourne infections and intoxications (eds. H. Riemann & F. L. Bryan) pp. 444 (Academic Press, New York, 1979).
Leonard, B., P. Lee, M. Jenkins and P. Schlievert. Cell and receptor requirements for Streptococcal pyrogenic exotoxin T cell mitogenicity. Infect. Immun. 59, 1210 (1991).
Abe, R., J. Forrester, F. Nakahara, J. Lafferty, B. Kotzin and D. Leung. Selective stimulation of human T cells with streptococcal erythrogenic toxins A and B. J. Immunol. 146, 3747 (1991).
Bayles, K. and J. Iandolo. Genetic and molecular analysis of the gene encoding staphylococcal enterotoxin D. J. Bacteriol. 171, 4799 (1989).
Su, Y. C. and A. C. L. Wong. Identification and purification of a new staphylococcal enterotoxin J. Applied and Environmental Microbiology 61, 1438 (1995).
Warren, J., D. Leatherman and J. Metzger. Evidence for cell-receptor activity in lymphocyte stimulation by staphylococcal enterotoxin. J. Immunol. 115, 49 (1975).
Smith, B. and H. Johnson. The effect of staphylococcal enterotoxins on the primary in vitro immune response. J. Immunol. 115, 575 (1975).
Leung, D. Y. M., B. T. Huber and P. M. Schlievert (eds.) Superantigens: Molecular Biology, Immunology, and Relevance to Human Disease (Marcel Dekker, Inc., New York, 1997).
Thibodeau, J. and R.-P. Sekaly (eds.) Bacterial Superantigens: Structure, Function and Therapeutic Potential (Springe-Verlag, Heidelberg, 1995).
Papageorgiou, A. C., H. S. Tranter and K. R. Acharya. Crystal structure of microbial surperantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors. J. Mol. Biol. 277, 61 (1998).
Papageorgiou, A.C., C.M. Collins, D.M. Gutman, J.B. Kline, S.M. O’Brien, H.S. Tranter and K. R. Acharya. Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeAl) by MHC class II molecules and T-cell receptors. EMBO J 18, 9 (1999).
Carlsson, R., H. Fischer and H. Sjogren. Binding of staphlyococcal enterotoxin A to accessory cells is a requirement for its ability to activate human T cells. J. Immunol. 140, 2484 (1988).
Fleischer, B. and H. Schrezenmeier. T cell stimulation by staphylococcal enterotoxins. Clonally variable response and requirement for major histocompatibility complex class II molecules on accessory or target cells. J. Exp. Med. 167, 1697 (1988).
Chapes, S., S. Hoynowski, K. Woods, J. Armstrong, A. Beharka and J. Iandolo. Staphylococcus-mediated T cell activation and spontaneous natural killer cell activity in the absence of major histocompatibility complex class II molecules. Infect. Immun. 61, 4013 (1993).
Hamad, A. R., A. Herman, P. Marrack and J. Kappler. Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B. J. Exp. Med. 180, 615 (1994).
Rovira, P., M. Buckle, J. P. Abastado, W. J. Peumans and P. Truffa-Bachi. Major histocompatibility class I molecules present Urtica dioica agglutinin, a superantigen of vegetal origin, to T lymphocytes. Eur:J. Immunol. 29, 1571 (1999).
Ikejima, T., C. Dinarello, D. Gill and S. Wolff. Induction of human interleukin-1 by a product of Staphylococcus aureus associated with toxic shock syndrome. J. Clin. Invest. 73, 1312 (1984).
Parsonnet, J., R. Hickman, D. Eardley and G. Pier. Induction of human interleukin-1 by toxic-shock-syndrome toxin-I. J. Infect. Dis. 151, 514 (1985).
Parsonnet, J., Z. Gillis and G. Pier. Induction of interleukin-1 by strains of Staphylococcus aureus from patients with nonmenstrual toxic shock syndrome. J. Infect. Dis. 154, 55 (1986).
Beezhold, D., G. Best, P. Bonventre and M. Thompson. Synergistic induction of interleukin-1 by endotoxin and toxic shock syndrome toxin-1 using rat macrophages. Infect. Immun. 55, 2865 (1987).
Fast, D., P. Schlievert and R. Nelson. Toxic shock syndrome-associated staphlococcal and streptococcal pyrogneic toxins are potent inducers of tumor necrosis factor. Infect. Immun. 57, 291 (1989).
Fleming, S. D., J. J. Iandolo and S. K. Chapes. Murine macrophage activation by staphylococcal exotoxins. Infect. Immun. 59, 4049 (1991).
Fast, D., B. Shannon, M. Herriott, M. Kennedy, J. Rummage and R. Leu. Staphylococcal exotoxins stimulate nitric oxidedependent murine macrophage tumoricidal activity. Infect. Immun. 59, 2987 (1990).
Trede, N., R. Geha and T. Chatila. Transcriptional activation of IL-1β and tumor necrosis factor genes by MHC class II ligands. J. Immunol. 146, 2310 (1991).
Isobe, K. I. and L. Nakashima. Feedback suppression of staphylococcal enterotoxin-stimulated T-lymphocyte proliferation by macrophages through inductive nitric oxide synthesis. Infect. Immun. 60, 4832 (1992).
Bratton, D. L., K. R. May, J. M. Kailey, D. E. Doherty and D. Y. Leung. Staphylococcal toxic shock syndrome toxin-1 inhibits monocyte apoptosis. J. Allergy Clin. Immunol. 103, 895 (1999).
Mancia, L., J. Wahlstrom, B. Schiller, L. Chini, G. Elinder, P. D’Argenio, D. Gigliotti, H. Wigzell, P. Rossi and J. Grunewald. Characterization of the T-cell receptor V-beta repertoire in Kawasaki disease. Scand. J. Immunol. 48, 443 (1998).
Soos, J. M., J. Schiffenbauer, B. A. Torres and H. M. Johnson. Superantigens as virulence factors in autoimmunity and immunodeficiency diseases. Medical Hypotheses 48, 253 (1997).
Fischer, P., M. M. Uttenreuther-Fischer and G. Gaedicke. Superantigens in the aetiology of Kawasaki disease. Lancet. 348, 202 (1996).
Lueng, D. Y. M. Superantigens related to Kawasaki syndrome. Springer Seminars in Immunopath. 17, 385 (1996).
Inocencio, J. and R. Hirsch. The role of T cells in Kawasaki disease. Critical Reviews in Immunol. 15, 349 (1995).
Curtis, N., R. Zheng, J. Lamb and M. Levin. Evidence for a superantigen mediated process in Kawasaki disease. Arch. Dis. in Childhood 72, 308 (1995).
Rowley, A. H. and T. S. Stanford. Letter to the editor-reply. Pediatric Res. 43, 291 (1998).
Choi, I.-H., Y.-J. Chwae, W.-3. Shim, D.-S. Kim, D.-H. Kwon, J.-D. Kim and S.-J. Kim. Clonal expansion of CD8+T cells in Kawasaki disease. J. Immunol. 159, 481 (1997).
St-Pierre, Y., N. Nabavi, Z. Ghogawala, L. Glimcher and T. Watts. A fuctional role for signal transduction via the cytoplasmic domains of MHC class II proteins. J.Immunol. 143, 808 (I989).
Fuleihan, R., W. Mourad, R. Geha and T. Chatila. Engagement of MHC-Class II molecules by staphylococcal exotoxins delivers a comitogenic signal to human B cells. J. Immunol. 146, 1661 (1991).
Chen, Z., J. McGuire, K. Leach and J. Cambier. Transmembrane signaling through B cell MHC class II molecules: Anti-Ia antibodies induce protein kinase C translocation to the nuclear fraction. J. Immunol. 138, 2345 (1987).
Mooney, N., C. Grillot-Courvalin, C. Hivroz, L. Y. Ju and D. Charron. Early biochemical events after MHC class 11-mediated signaling on human B lymphocytes. J. Immunol. 145, 2070 (1990).
Chatila, T. and R. Geha. Signal transduction bymicrobial superantigens via MHC class II molecules. Immunol. Rev. 131, 43 (1993).
Mono, T., R. Geha and T. Chatila. Engagement of MHC classI Imoleculesby staphylo-coccal superantigens activatessrc-typeprotein tyrosine kinases. Eur: J. Immunol. 24, 651 (1994).
Matsuyama, S., Y. Koide and T. Yoshida. HLA classI Imolecule-mediated signaltrans-duction mechanism responsible for the expression of interleukin-1 β and tumornecro-sis factor-α genes induced by a staphylococcal superantigen. Eur J. Immunol. 23, 3194 (1993).
Mourad, W., K. Mehindate, T. Schall and S. McColl. Engagement of major histocom-patibility complex class II molecules by superantigens induces inflammatory cytokine gene expression in human rheumatoid fibroblast-like synoviocytes. J. Exp. Med. 175, 613 (1992).
Guo, W., W. Mourad, D. Charron and R. Al-Daccak. Ligation of MHC class II molecules differentially upregulates TNF β gene expression in B cell lines of different MHC class II haplotypes. Hum. Immunol. 60, 312 (1999).
Ruco, L. and M. Meltzer. Macrophage activation for tumor cytotoxicity: development of macrophage cytotoxic activity requires completion of a sequence of short-lived intermediary reactions. J. Immunol. 121, 2035 (1978).
Pace, J., S. Russell, B. Torres, H. Johnson and P. Gray. Recombinant mouse gamma interferon induces the priming step in macrophage activation for tumor cell killing. J. Immunol. 130, 130–2011 (1983).
Boehm, U., T. Klamp, M. Groot and J. C. Howard. in Annual Review of Immunology (eds. W. E. Paul, C. G. Fathman & H. Metzger) pp. 749 (Annual Reviews Inc., Palo Alto, (1997).
Marrack, P., M. Blackman, E. Kushnir and J. Kappler. Thetoxicity of staphylococcal enterotox in B in mice is mediated by T ceIls. J. Exp. Med. 171, 455 (1990).
Miethke, T., C. Wahl, K. Heeg, B. Echtenacher, P. Krammer and H. Wagner. T cell-mediated lethal shock triggered in mice by the superantigen Staphylococcal Enterotoxin B: Criticalroleof tumornecrosis factor. J. Exp. Med. 175, 91 (1992).
Koesling, M., O. Rott and B. Fleischer. Macrophages are dispensable for superantigen-mediated stimulation and anergy induction of peripheral T cell in vivo. Cell. Immunol. 157, 29 (1994).
Bonventre, P., H. Heeg, C. Edwards II and C. Cullen. A mutation at histidine residue 135 of toxic shock syndrome toxin yields an immunogenic protein with minimal toxicity. Ifect. Immun. 63, 509 (1995).
Hoffman, M., M. Tremaine, J. Mansfield and M. Betley. Biochemical and mutational analysis of the histidine residues of staphylococcal enterotoxin A. Infect. Immun. 64, 885 (1996).
Woody, M. A., T. Krakauer, R. G. Ulrich and B. G. Stiles. Differential immune responses to staphylococcal enterotoxin B mutations in a hydrophobic loop dominating the interface with majorhistocompatibility complex class II receptors. J. Infectious Diseases 177, 1013 (1998).
Alber, G., D. Hammer and B. Fleischer. Relationship between enterotoxic-and T lymphocyte-stimulating activity. J. Immunol. 144, 4501 (1990).
Harris, T., D. Grossman, J. Kappler, P. Marrack, R. Rich and M. Betley. Lack of complete correlation between emetic and T-cell-stimulatory activities of staphylococcal enterotoxins. Infet. immun. 61, 3175 (1993).
Chapes, S. K. and A. A. Beharka. Lipopolysaccharide is required for the lethal effects of enterotoxin B after D-galactosamine sensitization. J. Endotoxin Res. 2, 263 (1995).
Beharka, A. A., J. W. Armstrong and S. K. Chapes. Macrophage cell lines derived from major histocompatibility complex 11-negative mice. In Vitro Cell. Dev. Biol. 34, 499 (1998).
Chapes, S. K., A. Beharka, M. Hart, M. Smeltzer and J. J. Iandolo. Differential RNA regulationby staphylococcal enterotoxins A and B inmurine macrophages. J. Leukoc. Biol. 55, 523 (1994).
Kotb, M., H. Ohnishi, G. Majumdar, S. Hackett, A. Bryant, G. Higgins and D. Stevens. Temporal relationship of cytokine release by peripheral blood mononuclear cells stimulated by the streptococcal superantigen pep M5. Infect. Immun. 61, 1194 (1993).
Rink, L., J. Luhm, M. Koester and H. Kirchner. Induction of a cytokine network by superantigens with parallel TH1 and TH2 stimulation. J. Interferon and Cytokine Res. 16, 41 (1996).
See, R., W. Kum, A. Chang, S. Goh and A. Chow. Induction of tumor necrosis factor and interleukin-1 by purified staphylococcal toxic shock syndrome toxin 1 requires the presence of both monocytes and T lymphocytes. Infect. Immun. 60, 2612 (1992).
Grossman, D., J. Lamphear, J. Mollick, M. Betley and R. Rich. Dual roles for class II major histocompatibility complex molecules in staphylococcal enterotoxin-induced cytokine production and in vivo toxicity. Infect. Immun. 60, 5190 (1992).
Bright, J. J., Z. Xin and S. Sriram. Superantigens augment antigen-specific Thl responses by inducing IL-12 production in macrophages. J. Leukoc. Biol. 65, 665 (1999).
Beharka, A. A., J. Iandolo and S. K. Chapes. Description of protein kinase activation in murine macrophages by Staphylococcus aureus superantigens. J. Leukoc. Biol. Supplement 1994, 22 (1994).
O’Farrell, P. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007 (1975).
Nielsen, M. B., N. Odum, J. Gerwien, A. Svejgaard, K. Bendtzen, S. Bregentholt, C. Ropke, C. Geisler, M. Dohlsten and K. Kaltoft. Staphylococcal enterotoxin-A directly stimulates signal transduction and interferongamma production in psoriatic T-cell lines. TissueAntigens 52, 530 (1998).
Mollick, J., R. Cook and R. Rich. Class II MHC molecules are specific receptors for staphylococcus enterotoxin A. Science 244, 817 (1989).
Scholl, P., A. Diez, W. Mourad, J. Parsonnet, R. Geha and T. Chatila. Toxic shock syndrometoxin1binds tomajor histocompatibility complex class II molecules. Proc. Natl. Acad. Sci. USA 86, 4210 (1989).
Herrmann, T., R. Accolla and H. MacDonald. Different staphylococcal enterotoxins bind preferentially to distinct major histocompatibility complex class II isotypes. Eur. J. Immunol. 19, 2171 (1989).
Fraser, J. High-affinity binding of staphylococcal enterotoxins A and B to HLA-DR. Nature 339, 221 (1989).
Russell, J., C. Pontzer and H. Johnson. Bothalpha-helices along the major histocompatibility complex binding cleft arerequired for staphylococcal enterotoxin A function. Proc. Natl. Acad. Sci. USA 88, 7228 (1991).
Karp, D. and E. Long. Identification of HLA-DR1 β chain residues critical for binding Staphylococcal enterotoxins A and E. J. Exp. Med. 175, 415 (1992).
Herman, A., N. Labrecque, J. Thibodeau, P. Marrack, J. Kappler and R. P. Sekaly. Identification of the staphylococcal enterotoxin A superantigen binding sitein the α 1 domain of the human histocompatibility antigen HLA-DR. Proc. Natl. Acad. Sci. USA 88, 9954 (1991).
Dellabona, P., J. Peccoud, J. Kappler, P. Marrack, C. Benoist and D. Mathis. Superantigens interact with MHC class II molecules outside of the antigen groove. Cell 62, 1115 (1990).
Fraser, J., R. Urban, J. Strominger and H. Robinson. Zinc regulates the function of two superantigens. proc. Natl. Acad. Sci. USA 89, 5507 (1992).
Hudson, K., R. Tiedemann, R. Urban, S. Lowe, J. Strominger and J. Fraser. Staphylo-coccal enterotoxin A has two cooperative binding sites on major histocompatibility complex class 11. J. Exp. Med. 182, 711 (1995).
Abrahmsen, L., M. Dohlsten, S. Segren, P. Bjork, E. Jonsson and T. Kalland. Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A. EMBO J. 14, 2978 (1995).
Schad, E., I. Zaitseva, V. Zaitsev, M. Dohlsten, T. Kalland, P. Schlievert, D. Ohlendorf and L. Svensson. Crystal structure of thesuperantigen staphylococcal enterotoxin type A. EMBO J. 14, 3292 (1995).
Papageorgiou, A., K. Acharya, R. Shapiro, E. Passalacqua, R. Brehm and H. Tranter. Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site. Structure 3, 769 (1995).
Schad, E. M., A. C. Papageorgiou, L. A. Svensson and K. R. Archarya. A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity. J. Mol. Biol. 269, 270 (1997).
Chintagumpala, M., J. Mollick and R. Rich. Staphylococcal toxins bind to different sites on HLA-DR. J. Immunol. 147, 3876 (1991).
Buxser, S., P. Bonventre and D. Archer. Specific receptor binding of staphylococcal enterotoxins by murinesplenic lymphocytes. Infect. Immun. 33, 827 (1981).
Beharka, A. A, J. Armstrong, J. J. Iandolo and S. K. Chapes. Binding and activation of major histocompatibility complex class II-deficient macrophages by staphylococcal exotoxins. Infect. Immun. 62, 3907 (1994).
Dowd, J., R. Jenkins and D. R. Karp. Inhibition of antigen-specific T cell activation by staphylococcal enterotoxins. J. Immunol. 154, 1024 (1995).
Kim, J., R. Urban, J. Strominger and D. Wiley. Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DRl. Science 266, 1870 (1994).
Thibodeau, J., I. Cloutier, P. Lavoie, N. Labrecque, W. Mourad, T. Jardetzky and R. Sekaly. Subsets of HLA-DR1 molecules defined by SEB and TSST-1 binding. Science 266, 1874 (1994).
Jardetzky, T., J. Brown, J. Gorga, L. Stern, R. Urban, Y-I. Chi, C. Stauffacher, J. Strominger and D. Wiley. Threedimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature 368, 711 (1994).
Pontzer, C., J. Russell and H. Johnson. Localization of animmune functional site on staphylococcal enterotoxin A using the synthetic peptide approach. J. Immunol. 143, 280 (1989).
Griggs, N., C. Pontzer, M. Jarpe and H. Johnson. Mapping of multiple binding domains of the superantigen staphylococcal enterotoxin A for HLA. J. Immunol. 148, 2516 (1992).
Mollick, J, R. McMasters, D. Grossman and R. Rich. Localization of a site on bacterial superantigens that determines T cell receptor β chain specificity. J. Exp. Med. 177, 283 (1993).
Harris, T. and M. Betley. Biological activities of staphylococcal enterotoxin type A mutants with N-terminal substitutions. Infect. Immun. 63, 2133 (1995).
Hedlund, G., M. Dohlsten, T. Herrmann, G. Buell, P. Lando, S. Segren, J. Schrimsher, H. Macdonald, H. Sjogren and T. Kalland. A recombinant C-terminal fragment of staphylococcal enterotoxin A binds to human MHC class II products but does not activate T cells. J. Immunol. 147, 4082 (1991).
Mehindate, K., J. Thibodeau, M. Dohlsten, T. Kalland, R.-P. Sekaly and W. Mourad. Cross-linking of major histocompatibility complex class II molecules by staphylococcal enterotoxin A superantigen is a requirement for inflammatory cytokine gene expression. J. Exp. Med. 182, 1573 (1995).
Beharka, A. A., J. J. Iandolo and S. K. Chapes. Staphylococcal enterotoxins bind H-2Db molecules on macrophages. proc. Natl. Acad. Sci. USA. 92, 6294 (1995).
Chapes, S. K. and A. R. Herpich. Complex high affinity interactions occur between MHC I and superantigens. J. Leukoc. Biol. 64, 587 (1998).
Iandolo, J. J. and S. K. Chapes. in Superantigens: Relevance to Human Disease and Basic Biology (eds. D. Leung, B. Huber & P. Schlievert) p. 231 (Marcel Dekker, Inc., New York, 1996).
Stiles, B.G., S. Bavari, T. Krakauer and R.G. Ulrich. Toxicity of staphylococcal enterotoxins potentiated by lipopolysaccharide: Major histocompatibility complex class II molecules dependency and cytokine release. Infect. Immun. 61, 5333 (1993).
Houlden, B., S. Widacki and J. Bluestone. Signal transduction through class I MHC by a monoclonal antibody that detects multiple murine and human class I molecules. J. Immunol. 146, 425 (1991).
Bregenholt, S., M. Ropke, S. Skov and M.H. Claesson. Ligation of MHC class I molecules on peripheral blood T lymphocytes induces new phenotypes and functions. J Immunol. 157, 993 (1996).
Wright, A. D. and S. K. Chapes. Staphylococcal enterotoxin A bound to MHC class I requirescross linking for theinductionof TNF-α Submitted for Publication (1999).
Hasko, G., L. Virag, G. Egnaczyk, A. L. Salzman and C. Szabo. The crucial role of IL-10 in the suppression of the immunological response in mice exposed to staphylococcal enterotoxin B. Eur. J. Immunol. 28, 1417 (1998).
Adams, D. and T. Hamilton. The cell biology of macrophage activation. Ann. Rev. Immunol. 2, 283 (1984).
Unanue, E. The regulation of lymphocyte functions by themacrophage. Immunol. h. 40, 227 (1978).
Du, X., P. Thompson, E. K. L. Chan, J. Ledesma, B. Roe, S. Clifton, S. N. Vogel and B. Beutler. Genetic and physical mapping of the Ips locus: identification of the toll-4 receptor as a candidate gene in the critical region. Blood Cells Mol. Dis. 24, 340 (1998).
Hoshino R, 0. Takeuchi, T. Kawai, H. Sanjo, T. Ogawa, Y Takeda, K. Takeda and S. Akira. Cutting Edge: Toll-Like Receptor 4 (TLR4)-Deficient Mice Are Hyporesponsive to Lipopolysaccharide: Evidence for TLR4 as the Lps Gene Product. J. Immunol. 162,3749 (1999).
Poltorak, A. et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085 (1998).
Qureshi, S. T., L. Larivi#re, G. Leveque, S. Clermont, K. J. Moore, P. Gros and D. Malo. Endotoxin-tolerant Mice Have Mutations in Toll-like Receptor 4 (Tlr4). J. Exp. Med. 189, 615 (1999).
Watson, J., M. Largen and K. McAdam. Genetic control of endotoxic responses in mice. J. Exp. Med. 147, 39 (1978).
Muzio, M., G. Natoli, S. Saccani, M. Levrero and A. Mantovani. The human toll signaling pathway: divergence of nuclear factor kappa B and JNK/SAPK activation upstream of tumor necrosis factor receptor-associated factor 6 (TRAF6). J Exp. Med. 187, 2097 (1998).
Vogel, S. N. and D. Fertsch. Macrophages from endotoxin-hyporesponsive (Lpsd) C3H/HeJ mice are permissive for vesicular stomatitis virus because of reduced levels of endogenous interferon: possible mechanism for natural resistance to virus infection. J. Virol. 61, 812 (1987).
Barber, S., P.-Y. Perera and S. N. Vogel. Defective ceramide response in C3H/HeJ (Lps d) macrophages. J. Immunol. 155, 2303 (1995).
Thieblemont, N. and S. D. Wright. Mice genetically hyporesponsive to lipopolysaccharide (LPS) exhibit a defect in endocytic uptake of LPS and ceramide. J. Exp. Med. 185, 2095 (1997).
Kraatz, J., L. Clair, J.L. Rodriguez and M.A. West. In vitro macrophage endotoxin tolerance: defective In vitro macrophage map kinase signal transduction after LPS treatment is not present in macrophages from C3H/HeJ endotoxin resistant mice. Shock 11, 58 (1999).
Plant, J. and A. Glynn. Genetics of resistance to infection with Salmonella typhimurium in mice. J. Infecct. Dis. 133, 72 (1976).
Plant, J. and A. Glynn. Locating Salmonella resistance gene on mouse chromosome 1. Clin. Exp. Immunol. 37, 1 (1979).
Bradley, D. Genetic control of Leishmania populations within the host. II. Genetic control of acute susceptibility of mice to L. donovani infection. Clin. Exp Immunol. 30, 130 (1977).
Vidal, S., P. Gros and E. Skamene. Natural resistance to infection with intracellular parasites: molecular genetics identifies Nramp1 as the Bcg/Ity/Lsh locus. J. Leukoc. Biol. 58, 382 (1995).
Vidal, S., M. Tremblay, G. Govoni, S. Gauthier, G. Sebastiani, D. Malo, E. Skamene, M. Olivier, S. Jothy and P. Gros. The Zty/Lsh/Bcg locus: natural resistance to infection with intracellular parasites is abrogated by disruption of the Nramp1 gene. J. Exp Med. 182, 655 (1995).
Gruenheid, S., M. Cellier, S. Vidal and P. Gros. Identification and characterization of a second mouse Nramp gene. Genomics 25, 514 (1995).
Vidal, S. M., D. Malo, K. Vogan, E. Skamene and P. Gros. Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg Cell 73, 469 (1993).
Gruenheid, S., E. Pinner, M. Desjardins and P. Gros. Natural resistance to infection with intracellular pathogens: the Nramp1 protein is recruited to the membrane of the phagosome. J. Exp Med. 185, 717 (1997).
Hackam, D.J., O.D. Rotstein, W.-J. Zhang, S. Gruenheid, P. Gros and S. Grinstein. Host resistance to intracellular infection: Mutation of natural resistance-associated macrophage protein 1 (Nramp 1) impairs phagosomal acidification. J. Exp Med. 188, 351 (1998).
Blackwell, J., T. Roach, S. Atkinson, J. Ajioka, C. Barton and M. A. Shaw. Genetic regulation of macrophage priming activation: The Lsh gene story. Immunol. Lett. 30,241 (1991).
Blackwell, J. M. and S. Searle. Genetic regulation of macrophage activation: understanding the function of Nramp1 (=Ity/Lsh/Bcg). Immunol. Lett. 65, 73 (1999).
Kuhn, D. E., B. D. Baker, W. P. Lafuse and B. S. Zwilling. Differential Iron Transport into phagosomes isolated from RAW264.7 macrophage cell lines transfected with Nramp1Gly169 or Nramp1Asp169. J. Leukoc. Biol. 66, 113 (1999).
Bjorkman, P., M. Saper, B. Samraoui, W. Bennett, J. Strominger and D. Wiley. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329,506 (1987).
Brown, J., T. Jardetzky, J. Gorga, L. Stern, R. Urban, J. Strominger and D. Wiley. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364, 33 (1993).
Fremont, D. H., W. A. Hendrickson, P. Marrack and J. Kappler. Structures of an MHC Class II molecule with covalently bound single peptides. Science 272, 1001 (1996).
Fremont, D. H., M. Matsumura, E. A. Stura, P. A. Peterson and I. A. Wilson. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science 257, 919 (1992).
Matsumura, M., D. H. Fremont, P. A. Peterson and I. A. Wilson. Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257, 927 (1992).
Wright, A. D. and S. K. Chapes. LPS sensitivity in recombinant mice lacking functional alleles at MHC II, Lps, and Nramp1 Genes. Submitted for Publication (1999).
Wright, A. D. and S. K. Chapes. Macrophages defective for Nramp1, Lps and MHC II suppress IFN-γ production. Submitted for Publication (1999).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Kluwer Academic Publishers
About this chapter
Cite this chapter
Chapes, S.K., Wright, A.D., Beharka, A.A. (2001). Superantigen Activation of Macrophages. In: Honeyman, A.L., Friedman, H., Bendinelli, M. (eds) Staphylococcus aureus Infection and Disease. Infectious Agents and Pathogenesis. Springer, Boston, MA. https://doi.org/10.1007/0-306-46848-4_5
Download citation
DOI: https://doi.org/10.1007/0-306-46848-4_5
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-46591-8
Online ISBN: 978-0-306-46848-3
eBook Packages: Springer Book Archive