메뉴 건너뛰기




Volumn 33, Issue 2, 2015, Pages 298-306

Activation of the NLRP3 inflammasome by vault nanoparticles expressing a chlamydial epitope

Author keywords

Chlamydia; Inflammasomes; Lysosomes; Vaults

Indexed keywords

BACTERIAL VACCINE; CATHEPSIN B; CD4 ANTIGEN; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; MEMBRANE PROTEIN; NANOPARTICLE; POLYMORPHIC MEMBRANE PROTEIN G VAULT VACCINE; PROTEIN KINASE SYK; RECOMBINANT VACCINE; SHORT HAIRPIN RNA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VAULT NANOPARTICLE; CARRIER PROTEIN; EPITOPE; IMMUNOLOGICAL ADJUVANT; NLRP3 PROTEIN, MOUSE; OUTER MEMBRANE PROTEIN; PMPG PROTEIN, CHLAMYDIA TRACHOMATIS; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE; SYK PROTEIN, HUMAN; SYK PROTEIN, MOUSE;

EID: 84922360493     PISSN: 0264410X     EISSN: 18732518     Source Type: Journal    
DOI: 10.1016/j.vaccine.2014.11.028     Document Type: Article
Times cited : (22)

References (53)
  • 1
  • 2
    • 84922367935 scopus 로고
    • Effect of acute pelvic inflammatory disease on fertility
    • Westrom L. Effect of acute pelvic inflammatory disease on fertility. Obstet Gynecol Surv 1975, 30:552-553.
    • (1975) Obstet Gynecol Surv , vol.30 , pp. 552-553
    • Westrom, L.1
  • 3
    • 0026705285 scopus 로고
    • Pelvic inflammatory disease and fertility: a cohort study of 1,844 women with laparoscopically verified disease and 657 control women with normal laparoscopic results
    • Westrom L., Joesoef R., Reynolds G., Hagdu A., Thompson S.E. Pelvic inflammatory disease and fertility: a cohort study of 1,844 women with laparoscopically verified disease and 657 control women with normal laparoscopic results. Sex Transm Dis 1992, 19:185-192.
    • (1992) Sex Transm Dis , vol.19 , pp. 185-192
    • Westrom, L.1    Joesoef, R.2    Reynolds, G.3    Hagdu, A.4    Thompson, S.E.5
  • 4
    • 0028171116 scopus 로고
    • Laparoscopic study on the microbiology and severity of acute pelvic inflammatory disease
    • Heinonen P.K., Miettinen A. Laparoscopic study on the microbiology and severity of acute pelvic inflammatory disease. Eur J Obstet Gynecol Reprod Biol 1994, 57:85-89.
    • (1994) Eur J Obstet Gynecol Reprod Biol , vol.57 , pp. 85-89
    • Heinonen, P.K.1    Miettinen, A.2
  • 5
    • 79952679718 scopus 로고    scopus 로고
    • Management of Chlamydia trachomatis genital tract infection: screening and treatment challenges
    • Taylor B.D., Haggerty C.L. Management of Chlamydia trachomatis genital tract infection: screening and treatment challenges. Infect Drug Resist 2011, 4:19-29.
    • (2011) Infect Drug Resist , vol.4 , pp. 19-29
    • Taylor, B.D.1    Haggerty, C.L.2
  • 7
    • 0028805751 scopus 로고
    • Gene knockout mice establish a primary protective role for major histocompatibility complex class II-restricted responses in Chlamydia trachomatis genital tract infection
    • Morrison R.P., Feilzer K., Tumas D.B. Gene knockout mice establish a primary protective role for major histocompatibility complex class II-restricted responses in Chlamydia trachomatis genital tract infection. Infect Immun 1995, 63:4661-4668.
    • (1995) Infect Immun , vol.63 , pp. 4661-4668
    • Morrison, R.P.1    Feilzer, K.2    Tumas, D.B.3
  • 8
    • 0032830635 scopus 로고    scopus 로고
    • Role of gamma interferon in controlling murine chlamydial genital tract infection
    • Ito J.I., Lyons J.M. Role of gamma interferon in controlling murine chlamydial genital tract infection. Infect Immun 1999, 67:5518-5521.
    • (1999) Infect Immun , vol.67 , pp. 5518-5521
    • Ito, J.I.1    Lyons, J.M.2
  • 9
    • 0035083050 scopus 로고    scopus 로고
    • Resolution of secondary Chlamydia trachomatis genital tract infection in immune mice with depletion of both CD4+ and CD8+ T cells
    • Morrison S.G., Morrison R.P. Resolution of secondary Chlamydia trachomatis genital tract infection in immune mice with depletion of both CD4+ and CD8+ T cells. Infect Immun 2001, 69:2643-2649.
    • (2001) Infect Immun , vol.69 , pp. 2643-2649
    • Morrison, S.G.1    Morrison, R.P.2
  • 10
    • 0034444896 scopus 로고    scopus 로고
    • Immunity to murine Chlamydia trachomatis genital tract reinfection involves B cells and CD4(+) T cells but not CD8(+) T cells
    • Morrison S.G., Su H., Caldwell H.D., Morrison R.P. Immunity to murine Chlamydia trachomatis genital tract reinfection involves B cells and CD4(+) T cells but not CD8(+) T cells. Infect Immun 2000, 68:6979-6987.
    • (2000) Infect Immun , vol.68 , pp. 6979-6987
    • Morrison, S.G.1    Su, H.2    Caldwell, H.D.3    Morrison, R.P.4
  • 11
  • 12
    • 0031011321 scopus 로고    scopus 로고
    • Chlamydia trachomatis genital tract infection of antibody-deficient gene knockout mice
    • Su H., Feilzer K., Caldwell H.D., Morrison R.P. Chlamydia trachomatis genital tract infection of antibody-deficient gene knockout mice. Infect Immun 1997, 65:1993-1999.
    • (1997) Infect Immun , vol.65 , pp. 1993-1999
    • Su, H.1    Feilzer, K.2    Caldwell, H.D.3    Morrison, R.P.4
  • 13
    • 0023933501 scopus 로고
    • Resolution of chlamydial genital infection in B-cell-deficient mice and immunity to reinfection
    • Ramsey K.H., Soderberg L.S., Rank R.G. Resolution of chlamydial genital infection in B-cell-deficient mice and immunity to reinfection. Infect Immun 1988, 56:1320-1325.
    • (1988) Infect Immun , vol.56 , pp. 1320-1325
    • Ramsey, K.H.1    Soderberg, L.S.2    Rank, R.G.3
  • 14
    • 0037174993 scopus 로고    scopus 로고
    • The La RNA-binding protein interacts with the vault RNA and is a vault-associated protein
    • Kickhoefer V.A., Poderycki M.J., Chan E.K.L., Rome L.H. The La RNA-binding protein interacts with the vault RNA and is a vault-associated protein. J Biol Chem 2002, 277:41282-41286.
    • (2002) J Biol Chem , vol.277 , pp. 41282-41286
    • Kickhoefer, V.A.1    Poderycki, M.J.2    Chan, E.K.L.3    Rome, L.H.4
  • 15
    • 0023003549 scopus 로고
    • Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA
    • Kedersha N.L., Rome L.H. Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA. J Cell Biol 1986, 103:699-709.
    • (1986) J Cell Biol , vol.103 , pp. 699-709
    • Kedersha, N.L.1    Rome, L.H.2
  • 16
    • 3142751435 scopus 로고    scopus 로고
    • The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling
    • Kolli S., Zito C.I., Mossink M.H., Wiemer E.A., Bennett A.M. The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling. J Biol Chem 2004, 279:29374-29385.
    • (2004) J Biol Chem , vol.279 , pp. 29374-29385
    • Kolli, S.1    Zito, C.I.2    Mossink, M.H.3    Wiemer, E.A.4    Bennett, A.M.5
  • 18
    • 21344472578 scopus 로고    scopus 로고
    • Major vault protein, in concert with constitutively photomorphogenic 1, negatively regulates c-Jun-mediated activator protein 1 transcription in mammalian cells
    • Yi C., Li S., Chen X., Wiemer E.A., Wang J., Wei N., et al. Major vault protein, in concert with constitutively photomorphogenic 1, negatively regulates c-Jun-mediated activator protein 1 transcription in mammalian cells. Cancer Res 2005, 65:5835-5840.
    • (2005) Cancer Res , vol.65 , pp. 5835-5840
    • Yi, C.1    Li, S.2    Chen, X.3    Wiemer, E.A.4    Wang, J.5    Wei, N.6
  • 19
    • 33644973273 scopus 로고    scopus 로고
    • The major vault protein is responsive to and interferes with interferon-gamma-mediated STAT1 signals
    • Steiner E., Holzmann K., Pirker C., Elbling L., Micksche M., Sutterluty H., et al. The major vault protein is responsive to and interferes with interferon-gamma-mediated STAT1 signals. J Cell Sci 2006, 119:459-469.
    • (2006) J Cell Sci , vol.119 , pp. 459-469
    • Steiner, E.1    Holzmann, K.2    Pirker, C.3    Elbling, L.4    Micksche, M.5    Sutterluty, H.6
  • 20
    • 33644944176 scopus 로고    scopus 로고
    • Crosstalk between Src and major vault protein in epidermal growth factor-dependent cell signalling
    • Kim E., Lee S., Mian M.F., Yun S.U., Song M., Yi K.S., et al. Crosstalk between Src and major vault protein in epidermal growth factor-dependent cell signalling. FEBS J 2006, 273:793-804.
    • (2006) FEBS J , vol.273 , pp. 793-804
    • Kim, E.1    Lee, S.2    Mian, M.F.3    Yun, S.U.4    Song, M.5    Yi, K.S.6
  • 23
    • 24744471429 scopus 로고    scopus 로고
    • Human vault-associated non-coding RNAs bind to mitoxantrone, a chemotherapeutic compound
    • Gopinath S.C., Matsugami A., Katahira M., Kumar P.K. Human vault-associated non-coding RNAs bind to mitoxantrone, a chemotherapeutic compound. Nucleic Acids Res 2005, 33:4874-4881.
    • (2005) Nucleic Acids Res , vol.33 , pp. 4874-4881
    • Gopinath, S.C.1    Matsugami, A.2    Katahira, M.3    Kumar, P.K.4
  • 25
    • 0035968311 scopus 로고    scopus 로고
    • Assembly of vault-like particles in insect cells expressing only the major vault protein
    • Stephen A.G. Assembly of vault-like particles in insect cells expressing only the major vault protein. J Biol Chem 2001, 276:23217-23220.
    • (2001) J Biol Chem , vol.276 , pp. 23217-23220
    • Stephen, A.G.1
  • 26
    • 84863828500 scopus 로고    scopus 로고
    • Vault nanocapsules as adjuvants favor cell-mediated over antibody-mediated immune responses following immunization of mice
    • Kar U.K., Jiang J., Champion C.I., Salehi S., Srivastava M., Sharma S., et al. Vault nanocapsules as adjuvants favor cell-mediated over antibody-mediated immune responses following immunization of mice. PLOS ONE 2012, 7:e38553.
    • (2012) PLOS ONE , vol.7 , pp. e38553
    • Kar, U.K.1    Jiang, J.2    Champion, C.I.3    Salehi, S.4    Srivastava, M.5    Sharma, S.6
  • 27
    • 84906672521 scopus 로고    scopus 로고
    • Bioengineered vaults: self-assembling protein shell-lipophilic core nanoparticles for drug delivery
    • Buehler D.C., Marsden M.D., Shen S.H., Toso D.B., Wu X., Loo J.A., et al. Bioengineered vaults: self-assembling protein shell-lipophilic core nanoparticles for drug delivery. ACS Nano 2014, 8:7723-7732.
    • (2014) ACS Nano , vol.8 , pp. 7723-7732
    • Buehler, D.C.1    Marsden, M.D.2    Shen, S.H.3    Toso, D.B.4    Wu, X.5    Loo, J.A.6
  • 28
    • 58149502680 scopus 로고    scopus 로고
    • Vaults and the major vault protein: novel roles in signal pathway regulation and immunity
    • Berger W., Steiner E., Grusch M., Elbling L., Micksche M. Vaults and the major vault protein: novel roles in signal pathway regulation and immunity. Cell Mol Life Sci 2009, 66:43-61.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 43-61
    • Berger, W.1    Steiner, E.2    Grusch, M.3    Elbling, L.4    Micksche, M.5
  • 30
    • 33747191203 scopus 로고    scopus 로고
    • The inflammasome first line of the immune response to cell stress
    • Ogura Y., Sutterwala F.S., Flavell R.A. The inflammasome first line of the immune response to cell stress. Cell 2006, 126:659-662.
    • (2006) Cell , vol.126 , pp. 659-662
    • Ogura, Y.1    Sutterwala, F.S.2    Flavell, R.A.3
  • 31
    • 33845497181 scopus 로고    scopus 로고
    • Inflammatory caspases and inflammasomes: master switches of inflammation
    • Martinon F., Tschopp J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ 2006, 14:10-22.
    • (2006) Cell Death Differ , vol.14 , pp. 10-22
    • Martinon, F.1    Tschopp, J.2
  • 33
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen I.C., Scull M.A., Moore C.B., Holl E.K., McElvania-TeKippe E., Taxman D.J., et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 2009, 30:556-565.
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3    Holl, E.K.4    McElvania-TeKippe, E.5    Taxman, D.J.6
  • 34
    • 70349334298 scopus 로고    scopus 로고
    • A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome
    • Munoz-Planillo R., Franchi L., Miller L.S., Nunez G. A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome. J Immunol 2009, 183:3942-3948.
    • (2009) J Immunol , vol.183 , pp. 3942-3948
    • Munoz-Planillo, R.1    Franchi, L.2    Miller, L.S.3    Nunez, G.4
  • 35
    • 84875169169 scopus 로고    scopus 로고
    • Alarmins, inflammasomes and immunity
    • Saïd-Sadier N., Ojcius D.M. Alarmins, inflammasomes and immunity. Biomed J 2012, 35:437-449.
    • (2012) Biomed J , vol.35 , pp. 437-449
    • Saïd-Sadier, N.1    Ojcius, D.M.2
  • 37
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon F., Petrilli V., Mayor A., Tardivel A., Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 2006, 440:237-241.
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 38
    • 70449448992 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome
    • Duncan J.A., Gao X., Huang M.T., O'Connor B.P., Thomas C.E., Willingham S.B., et al. Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome. J Immunol 2009, 182:6460-6469.
    • (2009) J Immunol , vol.182 , pp. 6460-6469
    • Duncan, J.A.1    Gao, X.2    Huang, M.T.3    O'Connor, B.P.4    Thomas, C.E.5    Willingham, S.B.6
  • 39
    • 33644985564 scopus 로고    scopus 로고
    • Critical role for NALP3/CIAS1/cryopyrin in innate and adaptive immunity through its regulation of caspase-1
    • Sutterwala F.S., Ogura Y., Szczepanik M., Lara-Tejero M., Lichtenberger G.S., Grant E.P., et al. Critical role for NALP3/CIAS1/cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 2006, 24:317-327.
    • (2006) Immunity , vol.24 , pp. 317-327
    • Sutterwala, F.S.1    Ogura, Y.2    Szczepanik, M.3    Lara-Tejero, M.4    Lichtenberger, G.S.5    Grant, E.P.6
  • 40
    • 1642285783 scopus 로고    scopus 로고
    • NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder
    • Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J. NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 2004, 20:319-325.
    • (2004) Immunity , vol.20 , pp. 319-325
    • Agostini, L.1    Martinon, F.2    Burns, K.3    McDermott, M.F.4    Hawkins, P.N.5    Tschopp, J.6
  • 41
    • 66749174867 scopus 로고    scopus 로고
    • The inflammasomes: guardians of the body
    • Martinon F., Mayor A., Tschopp J. The inflammasomes: guardians of the body. Annu Rev Immunol 2009, 27:229-265.
    • (2009) Annu Rev Immunol , vol.27 , pp. 229-265
    • Martinon, F.1    Mayor, A.2    Tschopp, J.3
  • 44
    • 84870250210 scopus 로고    scopus 로고
    • Innate immune responses to Chlamydia pneumoniae infection: role of TLRs, NLRs, and the inflammasome
    • Shimada K., Crother T.R., Arditi M. Innate immune responses to Chlamydia pneumoniae infection: role of TLRs, NLRs, and the inflammasome. Microbes Infect 2012, 14:1301-1307.
    • (2012) Microbes Infect , vol.14 , pp. 1301-1307
    • Shimada, K.1    Crother, T.R.2    Arditi, M.3
  • 46
    • 33749340049 scopus 로고    scopus 로고
    • The vault exterior shell is a dynamic structure that allows incorporation of vault-associated proteins into its interior
    • Poderycki M.J., Kickhoefer V.A., Kaddis C.S., Raval-Fernandes S., Johansson E., Zink J.I., et al. The vault exterior shell is a dynamic structure that allows incorporation of vault-associated proteins into its interior. Biochemistry 2006, 45:12184-12193.
    • (2006) Biochemistry , vol.45 , pp. 12184-12193
    • Poderycki, M.J.1    Kickhoefer, V.A.2    Kaddis, C.S.3    Raval-Fernandes, S.4    Johansson, E.5    Zink, J.I.6
  • 48
    • 7044253299 scopus 로고    scopus 로고
    • The infecting dose of Chlamydia muridarum modulates the innate immune response and ascending infection
    • Maxion H.K., Liu W., Chang M.-H., Kelly K.A. The infecting dose of Chlamydia muridarum modulates the innate immune response and ascending infection. Infect Immun 2004, 72:6330-6340.
    • (2004) Infect Immun , vol.72 , pp. 6330-6340
    • Maxion, H.K.1    Liu, W.2    Chang, M.-H.3    Kelly, K.A.4
  • 49
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B: functional relationships established for key mediators of apoptosis
    • Thornberry N.A., Rano T.A., Peterson E.P., Rasper D.M., Timkey T., Garcia-Calvo M., et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B: functional relationships established for key mediators of apoptosis. J Biol Chem 1997, 272:17907-17911.
    • (1997) J Biol Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5    Garcia-Calvo, M.6
  • 51
    • 55349123588 scopus 로고    scopus 로고
    • Receptor-independent, direct membrane binding leads to cell-surface lipid sorting and Syk kinase activation in dendritic cells
    • Ng G., Sharma K., Ward S.M., Desrosiers M.D., Stephens L.A., Schoel W.M., et al. Receptor-independent, direct membrane binding leads to cell-surface lipid sorting and Syk kinase activation in dendritic cells. Immunity 2008, 29:807-818.
    • (2008) Immunity , vol.29 , pp. 807-818
    • Ng, G.1    Sharma, K.2    Ward, S.M.3    Desrosiers, M.D.4    Stephens, L.A.5    Schoel, W.M.6
  • 52
    • 69249142633 scopus 로고    scopus 로고
    • Activated dectin-1 localizes to lipid raft microdomains for signaling and activation of phagocytosis and cytokine production in dendritic cells
    • Xu S., Huo J., Gunawan M., Su I.-H., Lam K.-P. Activated dectin-1 localizes to lipid raft microdomains for signaling and activation of phagocytosis and cytokine production in dendritic cells. J Biol Chem 2009, 284:22005-22011.
    • (2009) J Biol Chem , vol.284 , pp. 22005-22011
    • Xu, S.1    Huo, J.2    Gunawan, M.3    Su, I.-H.4    Lam, K.-P.5
  • 53
    • 77952887713 scopus 로고    scopus 로고
    • The SYK tyrosine kinase: a crucial player in diverse biological functions
    • Mócsai A., Ruland J., Tybulewicz V.L.J. The SYK tyrosine kinase: a crucial player in diverse biological functions. Nat Rev Immunol 2010, 10:387-402.
    • (2010) Nat Rev Immunol , vol.10 , pp. 387-402
    • Mócsai, A.1    Ruland, J.2    Tybulewicz, V.L.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.