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Volumn 91, Issue 11, 2010, Pages 2677-2686

The classical swine fever virus N-terminal protease Npro binds to cellular HAX-1

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DOUBLE STRANDED RNA; HAX 1 PROTEIN; INTERFERON REGULATORY FACTOR 3; PROTEASOME; PROTEINASE; UNCLASSIFIED DRUG; HAX1 PROTEIN, HUMAN; N(PRO) PROTEIN, SWINE FEVER VIRUS; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN; VIRUS PROTEIN;

EID: 78049359266     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.022897-0     Document Type: Article
Times cited : (27)

References (47)
  • 1
    • 0036884863 scopus 로고    scopus 로고
    • The 3′ untranslated region of human vimentin mRNA interacts with protein complexes containing eEF-1γ and HAX-1
    • Al-Maghrebi, M., Brule, H., Padkina, M., Allen, C., Holmes, W. M. & Zehner, Z. E. (2002). The 3′ untranslated region of human vimentin mRNA interacts with protein complexes containing eEF-1γ and HAX-1. Nucleic Acids Res 30, 5017-5028.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5017-5028
    • Al-Maghrebi, M.1    Brule, H.2    Padkina, M.3    Allen, C.4    Holmes, W.M.5    Zehner, Z.E.6
  • 2
    • 0036720818 scopus 로고    scopus 로고
    • Inhibition of beta interferon transcription by noncytopathogenic bovine viral diarrhea virus is through an interferon regulatory factor 3-dependent mechanism
    • Baigent, S. J., Zhang, G., Fray, M. D., Flick-Smith, H., Goodbourn, S. & McCauley, J. W. (2002). Inhibition of beta interferon transcription by noncytopathogenic bovine viral diarrhea virus is through an interferon regulatory factor 3-dependent mechanism. J Virol 76, 8979-8988.
    • (2002) J Virol , vol.76 , pp. 8979-8988
    • Baigent, S.J.1    Zhang, G.2    Fray, M.D.3    Flick-Smith, H.4    Goodbourn, S.5    McCauley, J.W.6
  • 3
    • 2942700205 scopus 로고    scopus 로고
    • Differential activation of interferon regulatory factors-3 and -7 by non-cytopathogenic and cytopathogenic bovine viral diarrhoea virus
    • Baigent, S. J., Goodbourn, S. & McCauley, J. W. (2004). Differential activation of interferon regulatory factors-3 and -7 by non-cytopathogenic and cytopathogenic bovine viral diarrhoea virus. Vet Immunol Immunopathol 100, 135-144.
    • (2004) Vet Immunol Immunopathol , vol.100 , pp. 135-144
    • Baigent, S.J.1    Goodbourn, S.2    McCauley, J.W.3
  • 4
    • 70349422338 scopus 로고    scopus 로고
    • Hepatitis C virus core protein and cellular protein HAX-1 promotes 5-fluorouracil mediated hepatocyte growth inhibition
    • Banerjee, A., Saito, K., Meyer, K., Banerjee, S., Ait-Goughoulte, M., Ray, R. B. & Ray, R. (2009). Hepatitis C virus core protein and cellular protein HAX-1 promotes 5-fluorouracil mediated hepatocyte growth inhibition. J Virol 83, 9663-9671.
    • (2009) J Virol , vol.83 , pp. 9663-9671
    • Banerjee, A.1    Saito, K.2    Meyer, K.3    Banerjee, S.4    Ait-Goughoulte, M.5    Ray, R.B.6    Ray, R.7
  • 6
    • 1842832211 scopus 로고    scopus 로고
    • Classical swine fever virus induces proinflammatory cytokines and tissue factor expression and inhibits apoptosis and interferon synthesis during the establishment of long-term infection of porcine vascular endothelial cells
    • Bensaude, E., Turner, J. L. E., Wakeley, P. R., Sweetman, D. A., Pardieu, C., Drew, T. W., Wileman, T. & Powel, P. P. (2004). Classical swine fever virus induces proinflammatory cytokines and tissue factor expression and inhibits apoptosis and interferon synthesis during the establishment of long-term infection of porcine vascular endothelial cells. J Gen Virol 85, 1029-1037.
    • (2004) J Gen Virol , vol.85 , pp. 1029-1037
    • Bensaude, E.1    Turner, J.L.E.2    Wakeley, P.R.3    Sweetman, D.A.4    Pardieu, C.5    Drew, T.W.6    Wileman, T.7    Powel, P.P.8
  • 8
    • 40449124712 scopus 로고    scopus 로고
    • Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons
    • Chao, J.-R., Parganas, E., Boyd, K., Hong, C. Y., Opferman, J. T. & Ihle, J. N. (2008). Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons. Nature 452, 98-102.
    • (2008) Nature , vol.452 , pp. 98-102
    • Chao, J.-R.1    Parganas, E.2    Boyd, K.3    Hong, C.Y.4    Opferman, J.T.5    Ihle, J.N.6
  • 9
    • 0034908274 scopus 로고    scopus 로고
    • Establishment of persistent infection with non-cytopathic bovine viral diarrhoea virus in cattle is associated with a failure to induce type I interferon
    • Charleston, B., Fray, M. D., Baigent, S., Carr, B. V. & Morrison, W. I. (2001). Establishment of persistent infection with non-cytopathic bovine viral diarrhoea virus in cattle is associated with a failure to induce type I interferon. J Gen Virol 82, 1893-1897.
    • (2001) J Gen Virol , vol.82 , pp. 1893-1897
    • Charleston, B.1    Fray, M.D.2    Baigent, S.3    Carr, B.V.4    Morrison, W.I.5
  • 10
    • 34548566398 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus
    • Chen, Z., Rijnbrand, R., Jangra, R. K., Devaraj, S. G., Qu, L., Ma, Y., Lemon, S. M. & Li, K. (2007). Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus. Virology 366, 277-292.
    • (2007) Virology , vol.366 , pp. 277-292
    • Chen, Z.1    Rijnbrand, R.2    Jangra, R.K.3    Devaraj, S.G.4    Qu, L.5    Ma, Y.6    Lemon, S.M.7    Li, K.8
  • 13
    • 0034958129 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible component of the B-cell receptor signalling pathway
    • Dufva, M., Olsson, M. & Rymo, L. (2001). Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible component of the B-cell receptor signalling pathway. J Gen Virol 82, 1581-1587.
    • (2001) J Gen Virol , vol.82 , pp. 1581-1587
    • Dufva, M.1    Olsson, M.2    Rymo, L.3
  • 14
    • 69949093432 scopus 로고    scopus 로고
    • HAX-1: A multifunctional protein with emerging roles in human disease
    • Fadeel, B. & Grzybowska, E. (2009). HAX-1: a multifunctional protein with emerging roles in human disease. Biochim Biophys Acta 1790, 1139-1148.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1139-1148
    • Fadeel, B.1    Grzybowska, E.2
  • 15
    • 49849094556 scopus 로고    scopus 로고
    • Identification of Intracellular proteins associated with the EBV-encoded nuclear antigen 5 using an efficient TAP procedure and FT-ICR mass spectrometry
    • Forsman, A., Ruetschi, U., Ekholm, J. & Rymo, L. (2008). Identification of Intracellular proteins associated with the EBV-encoded nuclear antigen 5 using an efficient TAP procedure and FT-ICR mass spectrometry. J Proteome Res 7, 2309-2319.
    • (2008) J Proteome Res , vol.7 , pp. 2309-2319
    • Forsman, A.1    Ruetschi, U.2    Ekholm, J.3    Rymo, L.4
  • 16
    • 0034636015 scopus 로고    scopus 로고
    • The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton
    • Gallagher, A. R., Cedzich, A., Gretz, N., Somlo, S. & Witzgall, R. (2000). The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton. Proc Natl Acad Sci U S A 97, 4017-4022.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4017-4022
    • Gallagher, A.R.1    Cedzich, A.2    Gretz, N.3    Somlo, S.4    Witzgall, R.5
  • 17
    • 0034604033 scopus 로고    scopus 로고
    • Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
    • Hacki, J., Egger, L., Monney, L., Conus, S., Rosse, T., Fellay, I. & Borner, C. (2000). Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene 19, 2286-2295.
    • (2000) Oncogene , vol.19 , pp. 2286-2295
    • Hacki, J.1    Egger, L.2    Monney, L.3    Conus, S.4    Rosse, T.5    Fellay, I.6    Borner, C.7
  • 18
    • 33747396191 scopus 로고    scopus 로고
    • Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition
    • Han, Y., Chen, Y. S., Liu, Z., Bodyak, N., Rigor, D., Bisping, E., Pu, W. T. & Kang, P. M. (2006). Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition. Circ Res 99, 415-423.
    • (2006) Circ Res , vol.99 , pp. 415-423
    • Han, Y.1    Chen, Y.S.2    Liu, Z.3    Bodyak, N.4    Rigor, D.5    Bisping, E.6    Pu, W.T.7    Kang, P.M.8
  • 19
    • 33751232040 scopus 로고    scopus 로고
    • pro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation
    • pro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation. J Virol 80, 11723-11732.
    • (2006) J Virol , vol.80 , pp. 11723-11732
    • Hilton, L.1    Moganeradj, K.2    Zhang, G.3    Chen, Y.H.4    Randall, R.E.5    McCauley, J.W.6    Goodbourn, S.7
  • 21
    • 13944271706 scopus 로고    scopus 로고
    • Establishment of a subgenomic replicon for bovine viral diarrhea virus in Huh-7 cells and modulation of interferon-regulated factor 3-mediated antiviral response
    • Horscroft, N., Bellows, D., Ansari, I., Lai, V. C., Dempsey, S., Liang, D., Donis, R., Zhong, W. & Hong, Z. (2005). Establishment of a subgenomic replicon for bovine viral diarrhea virus in Huh-7 cells and modulation of interferon-regulated factor 3-mediated antiviral response. J Virol 79, 2788-2796.
    • (2005) J Virol , vol.79 , pp. 2788-2796
    • Horscroft, N.1    Bellows, D.2    Ansari, I.3    Lai, V.C.4    Dempsey, S.5    Liang, D.6    Donis, R.7    Zhong, W.8    Hong, Z.9
  • 22
    • 70449713378 scopus 로고    scopus 로고
    • Hax1 lacks BH modules and is peripherally associated to heavy membranes: Implications for Omi/HtrA2 and PARL activity in the regulation of mitochondrial stress and apoptosis
    • Jeyaraju, D. V., Cisbani, G., De Brito, O. M., Koonin, E. V. & Pellegrini, L. (2009). Hax1 lacks BH modules and is peripherally associated to heavy membranes: implications for Omi/HtrA2 and PARL activity in the regulation of mitochondrial stress and apoptosis. Cell Death Differ 16, 1622-1629.
    • (2009) Cell Death Differ , vol.16 , pp. 1622-1629
    • Jeyaraju, D.V.1    Cisbani, G.2    De Brito, O.M.3    Koonin, E.V.4    Pellegrini, L.5
  • 24
    • 0033779920 scopus 로고    scopus 로고
    • Interaction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: Implication of cytoplasmic function of EBNA-LP
    • Kawaguchi, Y., Nakajima, K., Igarashi, M., Morita, T., Tanaka, M., Suzuki, M., Yokoyama, A., Matsuda, G., Kato, K. & other authors (2000). Interaction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: implication of cytoplasmic function of EBNA-LP. J Virol 74, 10104-10111.
    • (2000) J Virol , vol.74 , pp. 10104-10111
    • Kawaguchi, Y.1    Nakajima, K.2    Igarashi, M.3    Morita, T.4    Tanaka, M.5    Suzuki, M.6    Yokoyama, A.7    Matsuda, G.8    Kato, K.9
  • 28
    • 44349165022 scopus 로고    scopus 로고
    • Existence of multiple isoforms of HS1-associated protein X-1 in murine and human tissues
    • Lees, D. M., Hart, I. R. & Marshall, J. F. (2008). Existence of multiple isoforms of HS1-associated protein X-1 in murine and human tissues. J Mol Biol 379, 645-655.
    • (2008) J Mol Biol , vol.379 , pp. 645-655
    • Lees, D.M.1    Hart, I.R.2    Marshall, J.F.3
  • 29
    • 34548347634 scopus 로고    scopus 로고
    • Classical swine fever and other pestiviruses
    • 9th edn, Edited by B. E. Straw, J. J. Zimmerman, S. D'Allaire & D. J. Taylor. Ames, IA: Blackwell
    • Le Potier, M., Mesplede, A. & Vannier, P. (2006). Classical swine fever and other pestiviruses. In Diseases of Swine, 9th edn, pp. 309-322. Edited by B. E. Straw, J. J. Zimmerman, S. D'Allaire & D. J. Taylor. Ames, IA: Blackwell.
    • (2006) Diseases of Swine , pp. 309-322
    • Le Potier, M.1    Mesplede, A.2    Vannier, P.3
  • 30
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • 5th edn, Edited by D. M. Knipe & P. M. Howley. Philadelphia, PA: LW&W
    • Lindenbach, B. D., Thiel, H. J. & Rice, C. M. (2007). Flaviviridae: the viruses and their replication. In Fields Virology, 5th edn, pp. 1101-1152. Edited by D. M. Knipe & P. M. Howley. Philadelphia, PA: LW&W.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 31
    • 0037242712 scopus 로고    scopus 로고
    • Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) forms complexes with a cellular anti-apoptosis protein Bcl-2 or its EBV counterpart BHRF1 through HS1-associated protein X-1
    • Matsuda, G., Nakajima, K., Kawaguchi, Y., Yamanashi, Y. & Hirai, K. (2003). Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) forms complexes with a cellular anti-apoptosis protein Bcl-2 or its EBV counterpart BHRF1 through HS1-associated protein X-1. Microbiol Immunol 47, 91-99.
    • (2003) Microbiol Immunol , vol.47 , pp. 91-99
    • Matsuda, G.1    Nakajima, K.2    Kawaguchi, Y.3    Yamanashi, Y.4    Hirai, K.5
  • 32
    • 36849085461 scopus 로고    scopus 로고
    • An anti-apoptotic protein, Hax-1, inhibits the HIV-1 rev function by altering its sub-cellular localization
    • Modem, S. & Reddy, R. T. (2008). An anti-apoptotic protein, Hax-1, inhibits the HIV-1 rev function by altering its sub-cellular localization. J Cell Physiol 214, 14-19.
    • (2008) J Cell Physiol , vol.214 , pp. 14-19
    • Modem, S.1    Reddy, R.T.2
  • 34
    • 77949656460 scopus 로고    scopus 로고
    • Pestiviruses: How to outmaneuver your hosts
    • Peterhans, E. & Schweizer, M. (2010). Pestiviruses: how to outmaneuver your hosts. Vet Microbiol 142, 18-25.
    • (2010) Vet Microbiol , vol.142 , pp. 18-25
    • Peterhans, E.1    Schweizer, M.2
  • 35
    • 12144280835 scopus 로고    scopus 로고
    • Transmission of classical swine fever. A review
    • Ribbens, S., Dewulf, J., Koenen, F., Laevens, H. & Kruif, A. (2004). Transmission of classical swine fever. A review. Vet Q 26, 146-155.
    • (2004) Vet Q , vol.26 , pp. 146-155
    • Ribbens, S.1    Dewulf, J.2    Koenen, F.3    Laevens, H.4    Kruif, A.5
  • 36
    • 0031937630 scopus 로고    scopus 로고
    • African swine fever virus is wrapped by the endoplasmic reticulum
    • Rouiller, I., Brookes, S. M., Hyatt, A. D., Windsor, M. & Wileman, T. (1998). African swine fever virus is wrapped by the endoplasmic reticulum. J Virol 72, 2373-2387.
    • (1998) J Virol , vol.72 , pp. 2373-2387
    • Rouiller, I.1    Brookes, S.M.2    Hyatt, A.D.3    Windsor, M.4    Wileman, T.5
  • 37
    • 0035211935 scopus 로고    scopus 로고
    • Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis
    • Rudner, J., Lepple-Wienhues, A., Budach, W., Berschauer, J., Friedrich, B., Wesselborg, S., Schulze-Osthoff, K. & Belka, C. (2001). Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis. J Cell Sci 114, 4161-4172.
    • (2001) J Cell Sci , vol.114 , pp. 4161-4172
    • Rudner, J.1    Lepple-Wienhues, A.2    Budach, W.3    Berschauer, J.4    Friedrich, B.5    Wesselborg, S.6    Schulze-Osthoff, K.7    Belka, C.8
  • 39
    • 24944492937 scopus 로고    scopus 로고
    • proof classical swine fever virus is an antagonist of double-stranded RNA-mediated apoptosis and IFN-α/β induction
    • pro of classical swine fever virus is an antagonist of double-stranded RNA-mediated apoptosis and IFN-α/β induction. Virology 340, 265-276.
    • (2005) Virology , vol.340 , pp. 265-276
    • Ruggli, N.1    Bird, B.H.2    Liu, L.3    Bauhofer, O.4    Tratschin, J.D.5    Hofmann, M.A.6
  • 40
    • 0035037324 scopus 로고    scopus 로고
    • Noncytopathic bovine viral diarrhea virus inhibits double-stranded RNA-induced apoptosis and interferon synthesis
    • Schweizer, M. & Peterhans, E. (2001). Noncytopathic bovine viral diarrhea virus inhibits double-stranded RNA-induced apoptosis and interferon synthesis. J Virol 75, 4692-4698.
    • (2001) J Virol , vol.75 , pp. 4692-4698
    • Schweizer, M.1    Peterhans, E.2
  • 42
    • 0036140439 scopus 로고    scopus 로고
    • K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function
    • Sharp, T. V., Wang, H. W., Koumi, A., Hollyman, D., Endo, Y., Ye, H., Du, M. Q. & Boshoff, C. (2002). K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function. J Virol 76, 802-816.
    • (2002) J Virol , vol.76 , pp. 802-816
    • Sharp, T.V.1    Wang, H.W.2    Koumi, A.3    Hollyman, D.4    Endo, Y.5    Ye, H.6    Du, M.Q.7    Boshoff, C.8
  • 43
    • 33747440004 scopus 로고    scopus 로고
    • HAX-1 represses postmitochondrial caspase-9 activation and cell death during hypoxia-reoxygenation
    • Shaw, J. & Kirshenbaum, L. A. (2006). HAX-1 represses postmitochondrial caspase-9 activation and cell death during hypoxia-reoxygenation. Circ Res 99, 336-338.
    • (2006) Circ Res , vol.99 , pp. 336-338
    • Shaw, J.1    Kirshenbaum, L.A.2
  • 44
    • 0031569110 scopus 로고    scopus 로고
    • HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases
    • Suzuki, Y., Demoliere, C., Kitamura, D., Takeshita, H., Deuschle, U. & Watanabe, T. (1997). HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases. J Immunol 158, 2736-2744.
    • (1997) J Immunol , vol.158 , pp. 2736-2744
    • Suzuki, Y.1    Demoliere, C.2    Kitamura, D.3    Takeshita, H.4    Deuschle, U.5    Watanabe, T.6
  • 47
    • 0035822817 scopus 로고    scopus 로고
    • Evidence that HAX-1 is an interleukin-1α N-terminal binding protein
    • Yin, H., Morioka, H., Towle, C. A., Vidal, M., Watanabe, T. & Weissbach, L. (2001). Evidence that HAX-1 is an interleukin-1α N-terminal binding protein. Cytokine 15, 122-137.
    • (2001) Cytokine , vol.15 , pp. 122-137
    • Yin, H.1    Morioka, H.2    Towle, C.A.3    Vidal, M.4    Watanabe, T.5    Weissbach, L.6


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