Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants

Nature

Volumn 453, Issue 7198, 2008, Pages 1122-1126

  Eisenbarth, Stephanie C ^a   Colegio, Oscar R ^a   O'Connor Jr , William ^a   Sutterwala, Fayyaz S ^a,b   Flavell, Richard A ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADJUVANT; ALUMINUM; FREUND ADJUVANT; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; NACHT DOMAIN LEUCINE RICH REPEAT AND PYD CONTAINING PROTEIN 3; PROTEIN;

ALUMINUM; DRUG; ENZYME ACTIVITY; IMMUNE RESPONSE; VACCINE;

ADAPTIVE IMMUNITY; ANIMAL EXPERIMENT; ANTIBODY PRODUCTION; ANTIBODY RESPONSE; APOPTOSIS; ARTICLE; CONTROLLED STUDY; CYTOKINE PRODUCTION; ENZYME ACTIVATION; HUMORAL IMMUNITY; IMMUNOSTIMULATION; INNATE IMMUNITY; MACROPHAGE; MOUSE; NONHUMAN; PRIORITY JOURNAL;

ANIMALIA; MUS;

EID: 45749111446     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06939     Document Type: Article

References (30)

1. Gavin, A. L. et al. Adjuvant-enhanced antibody responses in the absence of toll-like receptor signaling. Science 314, 1936-1938 (2006).
2. Piggott, D. A. et al. MyD88-dependent induction of allergic Th2 responses to intranasal antigen. J. Clin. Invest. 115, 459-467 (2005).
3. Glenny, A. T., Pope, C. G., Waddington, H. & Wallace, U. The antigenic value of toxoid precipitated by potassium alum. J. Pathol. Bacteriol. 29, 31-40 (1926).
4. Lindblad, E. B. Aluminium compounds for use in vaccines. Immunol. Cell Biol. 82, 497-505 (2004).
5. Medzhitov, R. Recognition of microorganisms and activation of the immune response. Nature 449, 819-826 (2007).
6. Mariathasan, S. & Monack, D. M. Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation. Nature Rev. Immunol. 7, 31-40 (2007).
7. Sutterwala, F. S., Ogura, Y. & Flavell, R. A. The inflammasome in pathogen recognition and inflammation. J. Leukoc. Biol. 82, 259-264 (2007).
8. Sutterwala, F. S. et al. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 24, 317-327 (2006).
9. Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237-241 (2006).
10. Shi, Y., Evans, J. E. & Rock, K. L. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425, 516-521 (2003).
11. Chen, C. J. et al. Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nature Med. 13, 851-856 (2007).
12. Rimaniol, A. C. et al. Aluminum hydroxide adjuvant induces macrophage differentiation towards a specialized antigen-presenting cell type. Vaccine 22, 3127-3135 (2004).
13. Li, H., Nookala, S. & Re, F. Aluminum hydroxide adjuvants activate caspase-1 and induce IL-1β and IL-18 release. J. Immunol. 178, 5271-5276 (2007).
14. Mannhalter, J. W., Neychev, H. O., Zlabinger, G. J., Ahmad, R. & Eibl, M. M. Modulation of the human immune response by the non-toxic and non-pyrogenic adjuvant aluminium hydroxide: effect on antigen uptake and antigen presentation. Clin. Exp. Immunol. 61, 143-151 (1985).
15. + T cell differentiation by aluminum-containing adjuvants. Vaccine 25, 4575-4585 (2007).
16. Sutterwala, F. S. et al. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J. Exp. Med. 204, 3235-3245 (2007).
17. Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218 (2004).
18. 7 receptors. J. Biol. Chem. 276, 125-132 (2001).
19. Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228-232 (2006).
20. Petrilli, V. et al. Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ. 14, 1583-1589 (2007).
21. Pelegrin, P. & Surprenant, A. Pannexin-1 couples to maitotoxin- and nigericin-induced interleukin-1β release through a dye uptake-independent pathway. J. Biol. Chem. 282, 2386-2394 (2007).
22. Chang, M. et al. Degree of antigen adsorption in the vaccine or interstitial fluid and its effect on the antibody response in rabbits. Vaccine 19, 2884-2889 (2001).
23. Toda, Y. et al. Autocrine induction of the human pro-IL-1β gene promoter by IL-1β in monocytes. J. Immunol. 168, 1984-1991 (2002).
24. Jordan, M. B., Mills, D. M., Kappler, J., Marrack, P. & Cambier, J. C. Promotion of B cell immune responses via an alum-induced myeloid cell population. Science 304, 1808-1810 (2004).
25. Kaye, J. et al. Growth of a cloned helper T cell line induced by a monoclonal antibody specific for the antigen receptor: interleukin 1 is required for the expression of receptors for interleukin 2. J. Immunol. 133, 1339-1345 (1984).
26. Dunne, A. & O'Neill, L. A. The interleukin-1 receptor/Toll-like receptor superfamily: signal transduction during inflammation and host defense. Sci. STKE 2003, re3 (2003).
27. + T cells, IL-4 and STAT6. Nature Immunol. 1, 132-137 (2000).
28. Nakae, S., Asano, M., Horai, R., Sakaguchi, N. & Iwakura, Y. IL-1 enhances T cell-dependent antibody production through induction of CD40 ligand and OX40 on T cells. J. Immunol. 167, 90-97 (2001).
29. Adachi, O. et al. Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function. Immunity 9, 143-150 (1998).
30. Davis, C. N. et al. MyD88-dependent and -independent signaling by IL-1 in neurons probed by bifunctional Toll/IL-1 receptor domain/BB-loop mimetics. Proc. Natl Acad. Sci. USA 103, 2953-2958 (2006).