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Volumn 412, Issue 1, 2011, Pages 83-90

Dengue virus PrM/M proteins fail to show pH-dependent ion channel activity in Xenopus oocytes

Author keywords

Dengue virus; Ion channels; M protein; PrM; Xenopus oocytes

Indexed keywords

AMANTADINE; EPITOPE; ION CHANNEL; PROTEIN M; PROTEIN M2; PROTEIN PRM; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 79952538098     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.12.050     Document Type: Article
Times cited : (5)

References (33)
  • 1
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305(3):567-580.
    • (2001) J. Mol. Biol. , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.L.4
  • 4
    • 0036557845 scopus 로고    scopus 로고
    • Basic charge clusters and predictions of membrane protein topology
    • Juretic D., Zoranic L., Zucic D. Basic charge clusters and predictions of membrane protein topology. J. Chem. Inf. Model. 2002, 42(620-632).
    • (2002) J. Chem. Inf. Model. , vol.42 , Issue.620-632
    • Juretic, D.1    Zoranic, L.2    Zucic, D.3
  • 5
    • 0036462411 scopus 로고    scopus 로고
    • PH Homeostasis of cellular organelles
    • Demereaux N. pH Homeostasis of cellular organelles. News Physiol. Sci. 2002, 17:1-5.
    • (2002) News Physiol. Sci. , vol.17 , pp. 1-5
    • Demereaux, N.1
  • 6
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: applications to topology prediction
    • Tusnády G.E., Simon I. Principles governing amino acid composition of integral membrane proteins: applications to topology prediction. J. Mol. Biol. 1998, 283:489-506.
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 7
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnády G.E., Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnády, G.E.1    Simon, I.2
  • 9
    • 0031930410 scopus 로고    scopus 로고
    • Identification of a major determinant of mouse neurovirulence of dengue virus type 2 using stably cloned genomic-length cDNA
    • Gualano R., Pryor M., MR C., Wright P., Davidson A. Identification of a major determinant of mouse neurovirulence of dengue virus type 2 using stably cloned genomic-length cDNA. J. Gen. Virol. 1998, 79:437-446.
    • (1998) J. Gen. Virol. , vol.79 , pp. 437-446
    • Gualano, R.1    Pryor, M.M.R.C.2    Wright, P.3    Davidson, A.4
  • 10
    • 0036468861 scopus 로고    scopus 로고
    • Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century
    • Gubler D.J. Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol. 2002, 10(2):100-103.
    • (2002) Trends Microbiol. , vol.10 , Issue.2 , pp. 100-103
    • Gubler, D.J.1
  • 11
    • 0028181687 scopus 로고
    • Influenza A virus M2 ion channel protein: a structure-function analysis
    • Holsinger L.J., Nichani D., Pinto L.H., Lamb R.A. Influenza A virus M2 ion channel protein: a structure-function analysis. J. Virol. 1994, 68(3):1551-1563.
    • (1994) J. Virol. , vol.68 , Issue.3 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 12
    • 49449093199 scopus 로고    scopus 로고
    • Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel
    • Jing X., Ma C., Ohigashi Y., Oliveira F.A., Jardetzky T.S., Pinto L.H., Lamb R.A. Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel. Proc. Natl Acad. Sci. USA 2008, 105(31):10967-10972.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.31 , pp. 10967-10972
    • Jing, X.1    Ma, C.2    Ohigashi, Y.3    Oliveira, F.A.4    Jardetzky, T.S.5    Pinto, L.H.6    Lamb, R.A.7
  • 13
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: structure and maturation
    • Li L., Lok S.M., Yu I.M., Zhang Y., Kuhn R.J., Chen J., Rossmann M.G. The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 2008, 319(5871):1830-1834.
    • (2008) Science , vol.319 , Issue.5871 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 14
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Lippincott-Raven, Philadelphia, D. Knipe, P. Howley (Eds.)
    • Lindenbach B.D., Thiel H.J., Rice C.M. Flaviviridae: the viruses and their replication. Fields Virology 2007, Lippincott-Raven, Philadelphia. 5th ed. D. Knipe, P. Howley (Eds.).
    • (2007) Fields Virology
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 15
    • 0036094683 scopus 로고    scopus 로고
    • Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum
    • Lorenz I.C., Allison S.L., Heinz F.X., Helenius A. Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum. J. Virol. 2002, 76(11):5480-5491.
    • (2002) J. Virol. , vol.76 , Issue.11 , pp. 5480-5491
    • Lorenz, I.C.1    Allison, S.L.2    Heinz, F.X.3    Helenius, A.4
  • 16
    • 33747617366 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release
    • Lu W., Zheng B.J., Xu K., Schwarz W., Du L., Wong C.K., Chen J., Duan S., Deubel V., Sun B. Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release. Proc. Natl Acad. Sci. USA 2006, 103(33):12540-12545.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.33 , pp. 12540-12545
    • Lu, W.1    Zheng, B.J.2    Xu, K.3    Schwarz, W.4    Du, L.5    Wong, C.K.6    Chen, J.7    Duan, S.8    Deubel, V.9    Sun, B.10
  • 19
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto L.H., Holsinger L.J., Lamb R.A. Influenza virus M2 protein has ion channel activity. Cell 1992, 69(3):517-528.
    • (1992) Cell , vol.69 , Issue.3 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 20
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza A and B viruses
    • Pinto L.H., Lamb R.A. The M2 proton channels of influenza A and B viruses. J. Biol. Chem. 2006, 281(14):8997-9000.
    • (2006) J. Biol. Chem. , vol.281 , Issue.14 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 21
    • 22044441322 scopus 로고    scopus 로고
    • Dengue virus M protein C-terminal peptide (DVM-C) forms ion channels
    • Premkumar A., Horan C.R., Gage P.W. Dengue virus M protein C-terminal peptide (DVM-C) forms ion channels. J. Membr. Biol. 2005, 204:33-38.
    • (2005) J. Membr. Biol. , vol.204 , pp. 33-38
    • Premkumar, A.1    Horan, C.R.2    Gage, P.W.3
  • 22
    • 0030973121 scopus 로고    scopus 로고
    • The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer
    • Sakaguchi T., Tu Q., Pinto L.H., Lamb R.A. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer. Proc. Natl Acad. Sci. USA 1997, 94(10):5000-5005.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , Issue.10 , pp. 5000-5005
    • Sakaguchi, T.1    Tu, Q.2    Pinto, L.H.3    Lamb, R.A.4
  • 23
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert U., Ferrer-Montiel A.V., Oblatt-Montal M., Henklein P., Strebel K., Montal M. Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 1996, 398(1):12-18.
    • (1996) FEBS Lett. , vol.398 , Issue.1 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 24
    • 0025078661 scopus 로고
    • Use of Xenopus oocytes for the functional expression of plasma membrane proteins
    • Sigel E. Use of Xenopus oocytes for the functional expression of plasma membrane proteins. J. Membr. Biol. 1990, 117(3):201-221.
    • (1990) J. Membr. Biol. , vol.117 , Issue.3 , pp. 201-221
    • Sigel, E.1
  • 25
    • 15944402496 scopus 로고    scopus 로고
    • The Xenopus oocyte: system for the study of functional expression and modulation of proteins
    • Sigel E., Minier F. The Xenopus oocyte: system for the study of functional expression and modulation of proteins. Mol. Nutr. Food Res. 2005, 49(3):228-234.
    • (2005) Mol. Nutr. Food Res. , vol.49 , Issue.3 , pp. 228-234
    • Sigel, E.1    Minier, F.2
  • 26
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
    • Tang Y., Zaitseva F., Lamb R.A., Pinto L.H. The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J. Biol. Chem. 2002, 277(42):39880-39886.
    • (2002) J. Biol. Chem. , vol.277 , Issue.42 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 27
    • 0037125949 scopus 로고    scopus 로고
    • Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus
    • Tian C., Tobler K., Lamb R.A., Pinto L.H., Cross T.A. Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus. Biochemistry 2002, 41(37):11294-11300.
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11294-11300
    • Tian, C.1    Tobler, K.2    Lamb, R.A.3    Pinto, L.H.4    Cross, T.A.5
  • 28
    • 0023809470 scopus 로고
    • The synthetic precursor specific region of pre-pro-parathyroid hormone forms ion channels in lipid bilayers
    • Tosteson M.T., Caulfield M.P., Levy J.J., Rosenblatt M., Tosteson D.C. The synthetic precursor specific region of pre-pro-parathyroid hormone forms ion channels in lipid bilayers. Biosci. Rep. 1988, 8(2):173-183.
    • (1988) Biosci. Rep. , vol.8 , Issue.2 , pp. 173-183
    • Tosteson, M.T.1    Caulfield, M.P.2    Levy, J.J.3    Rosenblatt, M.4    Tosteson, D.C.5
  • 29
    • 20444385829 scopus 로고    scopus 로고
    • Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus
    • Venkataraman P., Lamb R.A., Pinto L.H. Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus. J. Biol. Chem. 2005, 280(22):21463-21472.
    • (2005) J. Biol. Chem. , vol.280 , Issue.22 , pp. 21463-21472
    • Venkataraman, P.1    Lamb, R.A.2    Pinto, L.H.3
  • 30
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block
    • Wang C., Takeuchi K., Pinto L.H., Lamb R.A. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J. Virol. 1993, 67(9):5585-5594.
    • (1993) J. Virol. , vol.67 , Issue.9 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 31
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • Yu I.M., Holdaway H.A., Chipman P.R., Kuhn R.J., Rossmann M.G., Chen J. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J. Virol. 2009, 83(23):12101-12107.
    • (2009) J. Virol. , vol.83 , Issue.23 , pp. 12101-12107
    • Yu, I.M.1    Holdaway, H.A.2    Chipman, P.R.3    Kuhn, R.J.4    Rossmann, M.G.5    Chen, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.