메뉴 건너뛰기




Volumn 29, Issue 1, 2010, Pages 94-103

The Marsupenaeus japonicus voltage-dependent anion channel (MjVDAC) protein is involved in white spot syndrome virus (WSSV) pathogenesis

Author keywords

Marsupenaeus japonicus; Mitochondrial membrane permeabilization; Voltage dependent anion channel; White spot syndrome virus; WSSV pathogenesis

Indexed keywords

DECAPODA (CRUSTACEA); EUKARYOTA; MARSUPENAEUS JAPONICUS; SHRIMP WHITE SPOT SYNDROME VIRUS;

EID: 77955058678     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.02.020     Document Type: Article
Times cited : (44)

References (33)
  • 2
    • 0036396817 scopus 로고    scopus 로고
    • Transcriptional analysis of the DNA polymerase gene of shrimp white spot syndrome virus
    • Chen L.L., Wang H.C., Huang C.J., Peng S.E., Chen Y.G., Lin S.J., et al. Transcriptional analysis of the DNA polymerase gene of shrimp white spot syndrome virus. Virology 2002, 301:136-147.
    • (2002) Virology , vol.301 , pp. 136-147
    • Chen, L.L.1    Wang, H.C.2    Huang, C.J.3    Peng, S.E.4    Chen, Y.G.5    Lin, S.J.6
  • 3
    • 10644220204 scopus 로고    scopus 로고
    • The unique stacked rings in the nucleocapsid of the white spot syndrome virus virion are formed by the major structural protein VP664, the largest viral structural protein ever found
    • Leu L.H., Tsai J.M., Wang H.C., Wang A.H., Wang C.H., Kou G.H., et al. The unique stacked rings in the nucleocapsid of the white spot syndrome virus virion are formed by the major structural protein VP664, the largest viral structural protein ever found. J Virol 2005, 79:140-149.
    • (2005) J Virol , vol.79 , pp. 140-149
    • Leu, L.H.1    Tsai, J.M.2    Wang, H.C.3    Wang, A.H.4    Wang, C.H.5    Kou, G.H.6
  • 4
    • 33644781714 scopus 로고    scopus 로고
    • Identification of the nucleocapsid, tegument, and envelope proteins of the shrimp white spot syndrome virus virion
    • Tsai J.H., Wang H.C., Leu J.H., Wang A.H., Zhuang Y., Walker P.J., et al. Identification of the nucleocapsid, tegument, and envelope proteins of the shrimp white spot syndrome virus virion. J Virol 2006, 80:3021-3029.
    • (2006) J Virol , vol.80 , pp. 3021-3029
    • Tsai, J.H.1    Wang, H.C.2    Leu, J.H.3    Wang, A.H.4    Zhuang, Y.5    Walker, P.J.6
  • 5
    • 34247510197 scopus 로고    scopus 로고
    • Identification of icp11, the most highly expressed gene of shrimp white spot syndrome virus (WSSV)
    • Wang H.C., Wang H.C., Kou G.H., Lo C.F., Huang H.P. Identification of icp11, the most highly expressed gene of shrimp white spot syndrome virus (WSSV). Dis Aquat Org 2007, 74:179-189.
    • (2007) Dis Aquat Org , vol.74 , pp. 179-189
    • Wang, H.C.1    Wang, H.C.2    Kou, G.H.3    Lo, C.F.4    Huang, H.P.5
  • 6
    • 58549094285 scopus 로고    scopus 로고
    • White spot syndrome virus protein ICP11: a histone-binding DNA mimic that disrupts nucleosome assembly
    • Wang H.C., Wang H.C., Ko T.P., Lee Y.M., Leu J.H., Ho C.H., et al. White spot syndrome virus protein ICP11: a histone-binding DNA mimic that disrupts nucleosome assembly. Proc Natl Acad Sci USA 2008, 105:20758-20763.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20758-20763
    • Wang, H.C.1    Wang, H.C.2    Ko, T.P.3    Lee, Y.M.4    Leu, J.H.5    Ho, C.H.6
  • 7
    • 33947732449 scopus 로고    scopus 로고
    • Protein expression profiling of the shrimp cellular response to white spot syndrome virus infection
    • Wang H.C., Wang H.C., Leu J.H., Kou G.H., Wang A.H., Lo C.F. Protein expression profiling of the shrimp cellular response to white spot syndrome virus infection. Dev Comp Immunol 2007, 31:672-686.
    • (2007) Dev Comp Immunol , vol.31 , pp. 672-686
    • Wang, H.C.1    Wang, H.C.2    Leu, J.H.3    Kou, G.H.4    Wang, A.H.5    Lo, C.F.6
  • 9
    • 33645823657 scopus 로고    scopus 로고
    • The expression level of the voltage-dependent anion channel controls life and death of the cell
    • Abu-Hamad S., Sivan S., Shoshan-Barmatz V. The expression level of the voltage-dependent anion channel controls life and death of the cell. Proc Natl Acad Sci USA 2006, 103:5787-5792.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5787-5792
    • Abu-Hamad, S.1    Sivan, S.2    Shoshan-Barmatz, V.3
  • 10
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: role of cytosolic proteins and mitochondrial lipids
    • Rostovtseva T.K., Bezrukov S.M. VDAC regulation: role of cytosolic proteins and mitochondrial lipids. J Bioenerg Biomembr 2008, 40:163-170.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 11
    • 0042381676 scopus 로고    scopus 로고
    • The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis
    • Vyssokikh M.Y., Brdiczka D. The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis. Acta Biochim Pol 2003, 50:389-404.
    • (2003) Acta Biochim Pol , vol.50 , pp. 389-404
    • Vyssokikh, M.Y.1    Brdiczka, D.2
  • 12
    • 34249824628 scopus 로고    scopus 로고
    • Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism
    • Lemasters J.J. Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism. J Gastroenterol Hepatol 2007, (Suppl. 1):S31-S37.
    • (2007) J Gastroenterol Hepatol , Issue.SUPPL 1
    • Lemasters, J.J.1
  • 13
    • 0035881713 scopus 로고    scopus 로고
    • Viral and bacterial proteins regulating apoptosis at the mitochondrial level
    • Boya P., Roques B., Kroemer G. Viral and bacterial proteins regulating apoptosis at the mitochondrial level. EMBO J 2001, 20:4325-4331.
    • (2001) EMBO J , vol.20 , pp. 4325-4331
    • Boya, P.1    Roques, B.2    Kroemer, G.3
  • 14
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J 1999, 341:233-249.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 15
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore?
    • Halestrap A.P. What is the mitochondrial permeability transition pore?. J Mol Cell Cardiol 2009, 46:821-831.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 16
    • 34447299940 scopus 로고    scopus 로고
    • Characterization and expression analysis of Paralichthys olivaceus voltage-dependent anion channel (VDAC) gene in response to virus infection
    • Lü A.J., Dong C.W., Du C.S., Zhang Q.Y. Characterization and expression analysis of Paralichthys olivaceus voltage-dependent anion channel (VDAC) gene in response to virus infection. Fish Shellfish Immunol 2007, 23:601-613.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 601-613
    • Lü, A.J.1    Dong, C.W.2    Du, C.S.3    Zhang, Q.Y.4
  • 17
    • 77951059450 scopus 로고    scopus 로고
    • Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1
    • Zamarin D., García-Sastre A., Xiao X., Wang R., Palese P. Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog 2007, 1:e4.
    • (2007) PLoS Pathog , vol.1
    • Zamarin, D.1    García-Sastre, A.2    Xiao, X.3    Wang, R.4    Palese, P.5
  • 18
    • 0342905085 scopus 로고    scopus 로고
    • Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel, HVDAC3, and alters its transmembrane potential
    • Rahmani Z., Huh K.W., Lasher R., Siddiqui A. Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel, HVDAC3, and alters its transmembrane potential. J Virol 2002, 74:2840-2846.
    • (2002) J Virol , vol.74 , pp. 2840-2846
    • Rahmani, Z.1    Huh, K.W.2    Lasher, R.3    Siddiqui, A.4
  • 19
    • 0038158319 scopus 로고    scopus 로고
    • Hepatitis B virus X protein induces cell death by causing loss of mitochondrial membrane potential
    • Shirakata Y., Koike K. Hepatitis B virus X protein induces cell death by causing loss of mitochondrial membrane potential. J Biol Chem 2003, 278:22071-22078.
    • (2003) J Biol Chem , vol.278 , pp. 22071-22078
    • Shirakata, Y.1    Koike, K.2
  • 20
    • 34250015780 scopus 로고    scopus 로고
    • Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon
    • Leu J.H., Chang C.C., Wu J.L., Hsu C.W., Hirono I., Aoki T., et al. Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon. BMC Genomics 2007, 16:120.
    • (2007) BMC Genomics , vol.16 , pp. 120
    • Leu, J.H.1    Chang, C.C.2    Wu, J.L.3    Hsu, C.W.4    Hirono, I.5    Aoki, T.6
  • 21
    • 36349011345 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an inhibitor of apoptosis protein (IAP) from the tiger shrimp, Penaeus monodon
    • Leu J.H., Kuo Y.C., Kou G.H., Lo C.F. Molecular cloning and characterization of an inhibitor of apoptosis protein (IAP) from the tiger shrimp, Penaeus monodon. Dev Comp Immunol 2007, 32:121-133.
    • (2007) Dev Comp Immunol , vol.32 , pp. 121-133
    • Leu, J.H.1    Kuo, Y.C.2    Kou, G.H.3    Lo, C.F.4
  • 22
    • 37349060626 scopus 로고    scopus 로고
    • Essential function of transglutaminase and clotting protein in shrimp immunity
    • Maningas M.B., Kondo H., Hirono I., Saito-Taki I., Aoki T. Essential function of transglutaminase and clotting protein in shrimp immunity. Mol Immunol 2008, 45:1269-1275.
    • (2008) Mol Immunol , vol.45 , pp. 1269-1275
    • Maningas, M.B.1    Kondo, H.2    Hirono, I.3    Saito-Taki, I.4    Aoki, T.5
  • 23
    • 0035283190 scopus 로고    scopus 로고
    • Ion channels in the outer membranes of chloroplasts and mitochondria: open doors or regulated gates?
    • Bölter B., Soll J. Ion channels in the outer membranes of chloroplasts and mitochondria: open doors or regulated gates?. EMBO J 2001, 20:935-940.
    • (2001) EMBO J , vol.20 , pp. 935-940
    • Bölter, B.1    Soll, J.2
  • 24
    • 0034468766 scopus 로고    scopus 로고
    • Functional characterization of the conserved " GLK" motif in mitochondrial porin from Neurospora crassa
    • Runke G., Maier E., O'Neil J.D., Benz R., Court D.A. Functional characterization of the conserved " GLK" motif in mitochondrial porin from Neurospora crassa. J Bioenerg Biomembr 2000, 32:563-570.
    • (2000) J Bioenerg Biomembr , vol.32 , pp. 563-570
    • Runke, G.1    Maier, E.2    O'Neil, J.D.3    Benz, R.4    Court, D.A.5
  • 25
    • 0028818855 scopus 로고
    • Lysine residues at Positions 234 and 236 in yeast porin are involved in its assembly into the mitochondrial outer membrane
    • Smith M.D., Petrak M., Boucher P.D., Barton K.N., Carter L., Reddy G., et al. Lysine residues at Positions 234 and 236 in yeast porin are involved in its assembly into the mitochondrial outer membrane. J Biol Chem 1995, 270:28331-28336.
    • (1995) J Biol Chem , vol.270 , pp. 28331-28336
    • Smith, M.D.1    Petrak, M.2    Boucher, P.D.3    Barton, K.N.4    Carter, L.5    Reddy, G.6
  • 27
    • 23044441770 scopus 로고    scopus 로고
    • Mitochondrial voltage-dependent anion channel gene family in Drosophila melanogaster: complex patterns of evolution, genomic organization, and developmental expression
    • Graham B.H., Craigen W.J. Mitochondrial voltage-dependent anion channel gene family in Drosophila melanogaster: complex patterns of evolution, genomic organization, and developmental expression. Mol Genet Metab 2005, 85:308-317.
    • (2005) Mol Genet Metab , vol.85 , pp. 308-317
    • Graham, B.H.1    Craigen, W.J.2
  • 28
    • 0031783363 scopus 로고    scopus 로고
    • Human mitochondrial transmembrane metabolite carriers: tissue distribution and its implication for mitochondrial disorders
    • Huizing M., Ruitenbeek W., van den Heuvel L.P., Dolce V., Iacobazzi V., Smeitink J.A., et al. Human mitochondrial transmembrane metabolite carriers: tissue distribution and its implication for mitochondrial disorders. J Bioenerg Biomembr 1998, 30:277-284.
    • (1998) J Bioenerg Biomembr , vol.30 , pp. 277-284
    • Huizing, M.1    Ruitenbeek, W.2    van den Heuvel, L.P.3    Dolce, V.4    Iacobazzi, V.5    Smeitink, J.A.6
  • 29
    • 64149098051 scopus 로고    scopus 로고
    • Lack of evidence for Litopenaeus vannamei Toll receptor (lToll) involvement in activation of sequence-independent antiviral immunity in shrimp
    • Labreuche Y., O'Leary N.A., de la Vega E., Veloso A., Gross P.S., Chapman R.W., et al. Lack of evidence for Litopenaeus vannamei Toll receptor (lToll) involvement in activation of sequence-independent antiviral immunity in shrimp. Dev Comp Immunol 2009, 33:806-810.
    • (2009) Dev Comp Immunol , vol.33 , pp. 806-810
    • Labreuche, Y.1    O'Leary, N.A.2    de la Vega, E.3    Veloso, A.4    Gross, P.S.5    Chapman, R.W.6
  • 30
    • 33846368080 scopus 로고    scopus 로고
    • Double-stranded RNA and antiviral immunity in marine shrimp: inducible host mechanisms and evidence for the evolution of viral counter-responses
    • Robalino J., Bartlett T.C., Chapman R.W., Gross P.S., Browdy C.L., Warr G.W. Double-stranded RNA and antiviral immunity in marine shrimp: inducible host mechanisms and evidence for the evolution of viral counter-responses. Dev Comp Immunol 2007, 31:539-547.
    • (2007) Dev Comp Immunol , vol.31 , pp. 539-547
    • Robalino, J.1    Bartlett, T.C.2    Chapman, R.W.3    Gross, P.S.4    Browdy, C.L.5    Warr, G.W.6
  • 31
    • 33846478653 scopus 로고    scopus 로고
    • White spot syndrome virus annexes a shrimp STAT to enhance expression of the immediate-early gene ie1
    • Liu W.J., Chang Y.S., Wang A.H., Kou G.H., Lo C.F. White spot syndrome virus annexes a shrimp STAT to enhance expression of the immediate-early gene ie1. J Virol 2007, 81:1461-1471.
    • (2007) J Virol , vol.81 , pp. 1461-1471
    • Liu, W.J.1    Chang, Y.S.2    Wang, A.H.3    Kou, G.H.4    Lo, C.F.5
  • 33
    • 67349235529 scopus 로고    scopus 로고
    • Key regions of VDAC1 functioning in apoptosis induction and regulation by hexokinase
    • Shoshan-Barmatz V., Zakar M., Rosenthal K., Abu-Hamad S. Key regions of VDAC1 functioning in apoptosis induction and regulation by hexokinase. Biochim Biophys Acta 2009, 787:421-430.
    • (2009) Biochim Biophys Acta , vol.787 , pp. 421-430
    • Shoshan-Barmatz, V.1    Zakar, M.2    Rosenthal, K.3    Abu-Hamad, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.