메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Influenza a virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

INFLAMMASOME; MITOCHONDRIAL PROTEIN; PB1 F2 PROTEIN; POLYPEPTIDE; PROTEIN VARIANT; TOM40 CHANNEL; UNCLASSIFIED DRUG; VIRUS PROTEIN; CARRIER PROTEIN; DDX58 PROTEIN, HUMAN; DEAD BOX PROTEIN; NLRP3 PROTEIN, HUMAN; PB1-F2 PROTEIN, INFLUENZA A VIRUS; RECOMBINANT PROTEIN; TOM40 PROTEIN HUMAN;

EID: 84907319179     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5713     Document Type: Article
Times cited : (177)

References (46)
  • 3
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang, C. & Youle, R. J. The role of mitochondria in apoptosis. Annu. Rev. Genet. 43, 95-118 (2009).
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 4
    • 2542495840 scopus 로고    scopus 로고
    • Calcium and mitochondria
    • DOI 10.1016/j.febslet.2004.03.071, PII S001457930400376X
    • Gunter, T. E., Yule, D. I., Gunter, K. K., Eliseev, R. A. & Salter, J. D. Calcium and mitochondria. FEBS Lett. 567, 96-102 (2004). (Pubitemid 38686430)
    • (2004) FEBS Letters , vol.567 , Issue.1 , pp. 96-102
    • Gunter, T.E.1    Yule, D.I.2    Gunter, K.K.3    Eliseev, R.A.4    Salter, J.D.5
  • 5
    • 23844482151 scopus 로고    scopus 로고
    • Mitochondrial calcium signalling in cell death
    • Leo, S., Bianchi, K., Brini, M. & Rizzuto, R. Mitochondrial calcium signalling in cell death. FEBS J. 272, 4013-4022 (2005).
    • (2005) FEBS J. , vol.272 , pp. 4013-4022
    • Leo, S.1    Bianchi, K.2    Brini, M.3    Rizzuto, R.4
  • 6
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: More Than Just a Powerhouse
    • DOI 10.1016/j.cub.2006.06.054, PII S0960982206017817
    • McBride, H. M., Neuspiel, M. & Wasiak, S. Mitochondria: more than just a powerhouse. Curr. Biol. 16, R551-R560 (2006). (Pubitemid 44066793)
    • (2006) Current Biology , vol.16 , Issue.14
    • McBride, H.M.1    Neuspiel, M.2    Wasiak, S.3
  • 7
    • 77955351652 scopus 로고    scopus 로고
    • New insights into the role of mitochondria in aging: Mitochondrial dynamics and more
    • Seo, A. Y. et al. New insights into the role of mitochondria in aging: mitochondrial dynamics and more. J. Cell Sci. 123, 2533-2542 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 2533-2542
    • Seo, A.Y.1
  • 9
    • 79957597757 scopus 로고    scopus 로고
    • Mitochondria in innate immune responses
    • West, A. P., Shadel, G. S. & Ghosh, S. Mitochondria in innate immune responses. Nat. Rev. Immunol. 11, 389-402 (2011).
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 389-402
    • West, A.P.1    Shadel, G.S.2    Ghosh, S.3
  • 10
    • 84871807864 scopus 로고
    • Mitochondrial-mediated antiviral immunity
    • Koshiba, T. Mitochondrial-mediated antiviral immunity. Biochim. Biophys. Acta 1833, 225-232 (2013).
    • (1833) Biochim. Biophys. Acta , pp. 225-232
    • Koshiba, T.1
  • 11
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3
    • DOI 10.1016/j.cell.2005.08.012, PII S0092867405008160
    • Seth, R. B., Sun, L., Ea, C. K. & Chen, Z. J. Identification and characterization of MAVS, a mitochondrial antiviral signalling protein that activates NF-kB and IRF3. Cell 122, 669-682 (2005). (Pubitemid 41242633)
    • (2005) Cell , vol.122 , Issue.5 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.-K.3    Chen, Z.J.4
  • 12
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou, R., Yazdi, A. S., Menu, P. & Tschopp, J. A role for mitochondria in NLRP3 inflammasome activation. Nature 469, 221-225 (2011).
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 13
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • Nakahira, K. et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat. Immunol. 12, 222-230 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 222-230
    • Nakahira, K.1
  • 14
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • Shimada, K. et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity 36, 401-414 (2012).
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1
  • 15
    • 80052177827 scopus 로고    scopus 로고
    • Mitoxosome: A mitochondrial platform for cross-talk between cellular stress and antiviral signalling
    • Tal, M. C. & Iwasaki, A. Mitoxosome: a mitochondrial platform for cross-talk between cellular stress and antiviral signalling. Immunol. Rev. 243, 215-234 (2011).
    • (2011) Immunol. Rev. , vol.243 , pp. 215-234
    • Tal, M.C.1    Iwasaki, A.2
  • 16
    • 79551716551 scopus 로고    scopus 로고
    • Mitochondrial membrane potential is required for MAVS-mediated antiviral signalling
    • Koshiba, T., Yasukawa, K., Yanagi, Y. & Kawabata, S. Mitochondrial membrane potential is required for MAVS-mediated antiviral signalling. Sci. Signal. 4, ra7 (2011).
    • (2011) Sci. Signal. , vol.4 , pp. 7
    • Koshiba, T.1    Yasukawa, K.2    Yanagi, Y.3    Kawabata, S.4
  • 17
    • 84887086945 scopus 로고    scopus 로고
    • Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection
    • Ichinohe, T., Yamazaki, T., Koshiba, T. & Yanagi, Y. Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection. Proc. Natl Acad. Sci. USA 110, 17963-17968 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 17963-17968
    • Ichinohe, T.1    Yamazaki, T.2    Koshiba, T.3    Yanagi, Y.4
  • 19
    • 84876793270 scopus 로고    scopus 로고
    • An insight into the PB1F2 protein and its multifunctional role in enhancing the pathogenicity of the influenza A viruses
    • Chakrabarti, A. K. & Pasricha, G. An insight into the PB1F2 protein and its multifunctional role in enhancing the pathogenicity of the influenza A viruses. Virology 440, 97-104 (2013).
    • (2013) Virology , vol.440 , pp. 97-104
    • Chakrabarti, A.K.1    Pasricha, G.2
  • 20
    • 0038001672 scopus 로고    scopus 로고
    • The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function
    • DOI 10.1128/JVI.77.13.7214-7224.2003
    • Gibbs, J. S., Malide, D., Hornung, F., Bennink, J. R. & Yewdell, J. W. The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function. J. Virol. 77, 7214-7224 (2003). (Pubitemid 36734490)
    • (2003) Journal of Virology , vol.77 , Issue.13 , pp. 7214-7224
    • Gibbs, J.S.1    Malide, D.2    Hornung, F.3    Bennink, J.R.4    Yewdell, J.W.5
  • 21
    • 10044257654 scopus 로고    scopus 로고
    • Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria
    • DOI 10.1016/j.febslet.2004.11.017, PII S001457930401381X
    • Yamada, H., Chounan, R., Higashi, Y., Kurihara, N. & Kido, H. Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria. FEBS Lett. 578, 331-336 (2004). (Pubitemid 39601802)
    • (2004) FEBS Letters , vol.578 , Issue.3 , pp. 331-336
    • Yamada, H.1    Chounan, R.2    Higashi, Y.3    Kurihara, N.4    Kido, H.5
  • 22
    • 77951059450 scopus 로고    scopus 로고
    • Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1
    • Zamarin, D., Garca-Sastre, A., Xiao, X., Wang, R. & Palese, P. Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog. 1, e4 (2005).
    • (2005) PLoS Pathog. , vol.1
    • Zamarin, D.1    Garca-Sastre, A.2    Xiao, X.3    Wang, R.4    Palese, P.5
  • 23
    • 79955431205 scopus 로고    scopus 로고
    • Impact of amino acid mutations in PB2 PB1-F2 and NS1 on the replication and pathogenicity of pandemic (H1N1) 2009 influenza viruses
    • Ozawa, M. et al. Impact of amino acid mutations in PB2, PB1-F2, and NS1 on the replication and pathogenicity of pandemic (H1N1) 2009 influenza viruses. J. Virol. 85, 4596-4601 (2011).
    • (2011) J. Virol. , vol.85 , pp. 4596-4601
    • Ozawa, M.1
  • 24
    • 36049034216 scopus 로고    scopus 로고
    • A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence
    • DOI 10.1371/journal.ppat.0030141
    • Conenello, G. M., Zamarin, D., Perrone, L. A., Tumpey, T. & Palese, P. A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence. PLoS Pathog. 3, 1414-1421 (2007). (Pubitemid 350085606)
    • (2007) PLoS Pathogens , vol.3 , Issue.10 , pp. 1414-1421
    • Conenello, G.M.1    Zamarin, D.2    Perrone, L.A.3    Tumpey, T.4    Palese, P.5
  • 25
    • 17844394478 scopus 로고    scopus 로고
    • Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    • DOI 10.1038/sj.emboj.7600614
    • Otera, H., Ohsakaya, S., Nagaura, Z., Ishihara, N. & Mihara, K. Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space. EMBO J. 24, 1375-1386 (2005). (Pubitemid 40593058)
    • (2005) EMBO Journal , vol.24 , Issue.7 , pp. 1375-1386
    • Otera, H.1    Ohsakaya, S.2    Nagaura, Z.-I.3    Ishihara, N.4    Mihara, K.5
  • 26
    • 84874346601 scopus 로고    scopus 로고
    • A structural perspective of the MAVS-regulatory mechanism on the mitochondrial outer membrane using bioluminescence resonance energy transfer
    • Sasaki, O. et al. A structural perspective of the MAVS-regulatory mechanism on the mitochondrial outer membrane using bioluminescence resonance energy transfer. Biochim. Biophys. Acta 1833, 1017-1027 (2013).
    • (2013) Biochim. Biophys. Acta , pp. 1017-1027
    • Sasaki, O.1
  • 27
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • Neupert, W. & Brunner, M. The protein import motor of mitochondria. Nat. Rev. Mol. Cell Biol. 3, 555-565 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 28
    • 38049016969 scopus 로고    scopus 로고
    • A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments
    • Otera, H. et al. A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments. J. Cell Biol. 179, 1355-1363 (2007).
    • (2007) J. Cell Biol. , vol.179 , pp. 1355-1363
    • Otera, H.1
  • 29
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • DOI 10.1038/sj.emboj.7601184, PII 7601184
    • Ishihara, N., Fujita, Y., Oka, T. & Mihara, K. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25, 2966-2977 (2006). (Pubitemid 44106750)
    • (2006) EMBO Journal , vol.25 , Issue.13 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 30
    • 84898603457 scopus 로고    scopus 로고
    • Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics
    • Baker, M. J. et al. Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics. EMBO J. 33, 578-593 (2014).
    • (2014) EMBO J. , vol.33 , pp. 578-593
    • Baker, M.J.1
  • 31
    • 70350468688 scopus 로고    scopus 로고
    • Mitofusin 2 inhibits mitochondrial antiviral signalling
    • Yasukawa, K. et al. Mitofusin 2 inhibits mitochondrial antiviral signalling. Sci. Signal. 2, ra47 (2009).
    • (2009) Sci. Signal. , vol.2 , pp. 47
    • Yasukawa, K.1
  • 32
    • 84865095316 scopus 로고    scopus 로고
    • Influenza virus protein PB1-F2 inhibits the induction of type i interferon by binding to MAVS and decreasing mitochondrial membrane potential
    • Varga, Z. T., Grant, A., Manicassamy, B. & Palese, P. Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential. J. Virol. 86, 8359-8366 (2012).
    • (2012) J. Virol. , vol.86 , pp. 8359-8366
    • Varga, Z.T.1    Grant, A.2    Manicassamy, B.3    Palese, P.4
  • 33
    • 84876237736 scopus 로고    scopus 로고
    • The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation
    • Subramanian, N., Natarajan, K., Clatworthy, M. R., Wang, Z. & Germain, R. N. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell 153, 348-361 (2013).
    • (2013) Cell , vol.153 , pp. 348-361
    • Subramanian, N.1    Natarajan, K.2    Clatworthy, M.R.3    Wang, Z.4    Germain, R.N.5
  • 34
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • Latz, E., Xiao, T. S. & Stutz, A. Activation and regulation of the inflammasomes. Nat. Rev. Immunol. 13, 397-411 (2013).
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 35
    • 0344585401 scopus 로고    scopus 로고
    • Apoptosis-Associated Speck-Like Protein Containing a Caspase Recruitment Domain Is a Regulator of Procaspase-1 Activation
    • Stehlik, C. et al. Apoptosis-associated speck-like protein containing a caspase recruitment domain is a regulator of procaspase-1 activation. J. Immunol. 171, 6154-6163 (2003). (Pubitemid 37467238)
    • (2003) Journal of Immunology , vol.171 , Issue.11 , pp. 6154-6163
    • Stehlik, C.1    Lee, S.H.2    Dorfleutner, A.3    Stassinopoulos, A.4    Sagara, J.5    Reed, J.C.6
  • 36
    • 84855830938 scopus 로고    scopus 로고
    • Measles virus v protein inhibits NLRP3 inflammasome-mediated interleukin-1b secretion
    • Komune, N., Ichinohe, T., Ito, M. & Yanagi, Y. Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1b secretion. J. Virol. 85, 13019-13026 (2011).
    • (2011) J. Virol. , vol.85 , pp. 13019-13026
    • Komune, N.1    Ichinohe, T.2    Ito, M.3    Yanagi, Y.4
  • 38
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • DOI 10.1038/nature04193, PII N04193
    • Meylan, E. et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437, 1167-1172 (2005). (Pubitemid 41509355)
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 40
    • 75949098312 scopus 로고    scopus 로고
    • Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway
    • Castanier, C., Garcin, D., Vazquez, A. & Arnoult, D. Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway. EMBO Rep. 11, 133-138 (2010).
    • (2010) EMBO Rep. , vol.11 , pp. 133-138
    • Castanier, C.1    Garcin, D.2    Vazquez, A.3    Arnoult, D.4
  • 41
    • 67049089786 scopus 로고    scopus 로고
    • SLP-2 is required for stress-induced mitochondrial hyperfusion
    • Tondera, D. et al. SLP-2 is required for stress-induced mitochondrial hyperfusion. EMBO J. 28, 1589-1600 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1589-1600
    • Tondera, D.1
  • 43
    • 84866146963 scopus 로고    scopus 로고
    • Naturally occurring swine influenza A virus PB1-F2 phenotypes that contribute to superinfection with Gram-positive respiratory pathogens
    • Weeks-Gorospe, J. N. et al. Naturally occurring swine influenza A virus PB1-F2 phenotypes that contribute to superinfection with Gram-positive respiratory pathogens. J. Virol. 86, 9035-9043 (2012).
    • (2012) J. Virol. , vol.86 , pp. 9035-9043
    • Weeks-Gorospe, J.N.1
  • 44
    • 60549112774 scopus 로고    scopus 로고
    • Inflammasome recognition of influenza virus is essential for adaptive immune responses
    • Ichinohe, T., Lee, H. K., Ogura, Y., Flavell, R. & Iwasaki, A. Inflammasome recognition of influenza virus is essential for adaptive immune responses. J. Exp. Med. 206, 79-87 (2009).
    • (2009) J. Exp. Med. , vol.206 , pp. 79-87
    • Ichinohe, T.1    Lee, H.K.2    Ogura, Y.3    Flavell, R.4    Iwasaki, A.5
  • 45
    • 84866156921 scopus 로고    scopus 로고
    • Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome
    • Ito, M., Yanagi, Y. & Ichinohe, T. Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome. PLoS Pathog. 8, e1002857 (2012).
    • (2012) PLoS Pathog. , vol.8
    • Ito, M.1    Yanagi, Y.2    Ichinohe, T.3
  • 46
    • 77955883390 scopus 로고    scopus 로고
    • Monoclonal antibodies against the PB1-F2 protein of H1N1 influenza A virus
    • Nordmann, A., Wixler, L., Ludwig, S. & Wixler, V. Monoclonal antibodies against the PB1-F2 protein of H1N1 influenza A virus. Hybridoma (Larchmt) 29, 321-326 (2010).
    • (2010) Hybridoma (Larchmt) , vol.29 , pp. 321-326
    • Nordmann, A.1    Wixler, L.2    Ludwig, S.3    Wixler, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.