메뉴 건너뛰기




Volumn 74, Issue 1, 2000, Pages 564-572

α-Glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE INHIBITOR;

EID: 0033988280     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.1.564-572.2000     Document Type: Article
Times cited : (182)

References (36)
  • 1
    • 0029162425 scopus 로고
    • Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and paniculate form
    • Allison, S. L., K. Stadler, C. W. Mandl, C. Kunz, and F. X. Heinz. 1995. Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and paniculate form. J. Virol. 69:5816-5820.
    • (1995) J. Virol. , vol.69 , pp. 5816-5820
    • Allison, S.L.1    Stadler, K.2    Mandl, C.W.3    Kunz, C.4    Heinz, F.X.5
  • 2
    • 0028304762 scopus 로고
    • NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: In vitro and in vivo studies
    • Amberg, S. M., A. Nestorowicz, D. W. McCourt, and C. M. Rice. 1994. NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies. J. Virol. 68:3794-3802.
    • (1994) J. Virol. , vol.68 , pp. 3794-3802
    • Amberg, S.M.1    Nestorowicz, A.2    McCourt, D.W.3    Rice, C.M.4
  • 3
    • 0031809225 scopus 로고    scopus 로고
    • Treatment of chronic hepadnavirus infection in a woodchuck animal model with an inhibitor of protein folding and trafficking
    • Block, T. M., X. Lu, A. Mehta, B. S. Blumberg, B. Tennant, M. Ebling, B. Korba, D. M. Lansky, G. S. Jacob, and R. A. Dwek. 1998. Treatment of chronic hepadnavirus infection in a woodchuck animal model with an inhibitor of protein folding and trafficking. Nat. Med. 4:610-614.
    • (1998) Nat. Med. , vol.4 , pp. 610-614
    • Block, T.M.1    Lu, X.2    Mehta, A.3    Blumberg, B.S.4    Tennant, B.5    Ebling, M.6    Korba, B.7    Lansky, D.M.8    Jacob, G.S.9    Dwek, R.A.10
  • 5
  • 6
    • 0000445568 scopus 로고    scopus 로고
    • Molecular biology of dengue viruses
    • D. J. Gubler and G. Kuno (ed.), CAB International, New York, N.Y.
    • Chang, G. J. 1997. Molecular biology of dengue viruses, p. 175-198. In D. J. Gubler and G. Kuno (ed.), Dengue and dengue hemorrhagic fever. CAB International, New York, N.Y.
    • (1997) Dengue and Dengue Hemorrhagic Fever , pp. 175-198
    • Chang, G.J.1
  • 7
    • 0029948547 scopus 로고    scopus 로고
    • Human isolates of dengue type 1 virus induce apoptosis in mouse neuroblastoma cells
    • Desprès, P., M. Flamand, P. E. Ceccaldi, and V. Deubel. 1996. Human isolates of dengue type 1 virus induce apoptosis in mouse neuroblastoma cells. J. Virol. 70:4090-4096.
    • (1996) J. Virol. , vol.70 , pp. 4090-4096
    • Desprès, P.1    Flamand, M.2    Ceccaldi, P.E.3    Deubel, V.4
  • 8
    • 0031964231 scopus 로고    scopus 로고
    • Apoptosis in the mouse central nervous system in response to infection with mouse-neurovirulent dengue viruses
    • Desprès, P., M. P. Frenkiel, P. E. Ceccaldi, C. Duarte Dos Santos, and V. Deubel. 1998. Apoptosis in the mouse central nervous system in response to infection with mouse-neurovirulent dengue viruses. J. Virol. 72:823-829.
    • (1998) J. Virol. , vol.72 , pp. 823-829
    • Desprès, P.1    Frenkiel, M.P.2    Ceccaldi, P.E.3    Duarte Dos Santos, C.4    Deubel, V.5
  • 9
    • 0027304942 scopus 로고
    • Differences between cell membrane fusion activities of two dengue type-1 isolates reflect modifications of viral structure
    • Desprès, P., M. P. Frenkiel, and V. Deubel. 1993. Differences between cell membrane fusion activities of two dengue type-1 isolates reflect modifications of viral structure. Virology 196:209-219.
    • (1993) Virology , vol.196 , pp. 209-219
    • Desprès, P.1    Frenkiel, M.P.2    Deubel, V.3
  • 10
    • 0028865478 scopus 로고
    • Effects of anti-e2 monoclonal antibody on sindhis virus replication in AT3 cells expressing bcl-2
    • Desprès, P., J. W. Griffin, and D. E. Griffin. 1995. Effects of anti-E2 monoclonal antibody on Sindhis virus replication in AT3 cells expressing bcl-2. J. Virol. 69:7006-7014.
    • (1995) J. Virol. , vol.69 , pp. 7006-7014
    • Desprès, P.1    Griffin, J.W.2    Griffin, D.E.3
  • 11
    • 0029112274 scopus 로고
    • The α-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding
    • Fischer, P. B., M. Collin, G. B. Karlsson, W. James, T. D. Butters, S. J. Davis, S. Gordon, R. A. Dwek, and F. M. Platt. 1995. The α-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding. J. Virol. 69:5791-5797.
    • (1995) J. Virol. , vol.69 , pp. 5791-5797
    • Fischer, P.B.1    Collin, M.2    Karlsson, G.B.3    James, W.4    Butters, T.D.5    Davis, S.J.6    Gordon, S.7    Dwek, R.A.8    Platt, F.M.9
  • 12
    • 0028039833 scopus 로고
    • Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice
    • Fonseca, B. A., S. Pincus, R. E. Shope, E. Paoletti, and P. W. Mason. 1994. Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice. Vaccine 12:279-285.
    • (1994) Vaccine , vol.12 , pp. 279-285
    • Fonseca, B.A.1    Pincus, S.2    Shope, R.E.3    Paoletti, E.4    Mason, P.W.5
  • 13
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D. N., B. Foellmer, and A. Helenius. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 14
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D. N., B. Foellmer, and A. Helenius. 1996. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15:2961-2968.
    • (1996) EMBO J. , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 15
    • 0028252393 scopus 로고
    • The interaction of the flavivirus envelope proteins: Implications for virus entry and release
    • Heinz, F. X., G. Auer, K. Stiasny. H. Holzmann, C. Mandl, F. Guirakhoo, and C. Kunz. 1994. The interaction of the flavivirus envelope proteins: implications for virus entry and release. Arch. Virol. 9:339-348.
    • (1994) Arch. Virol. , vol.9 , pp. 339-348
    • Heinz, F.X.1    Auer, G.2    Stiasny, K.3    Holzmann, H.4    Mandl, C.5    Guirakhoo, F.6    Kunz, C.7
  • 17
    • 0028037768 scopus 로고
    • The envelope glycoproteins of dengue 1 and dengue 2 viruses grown in mosquito cells differ in their utilization of potential glycosylation sites
    • Johnson, A. J., F. Guirakhoo, and J. T. Roehrig. 1994. The envelope glycoproteins of dengue 1 and dengue 2 viruses grown in mosquito cells differ in their utilization of potential glycosylation sites. Virology 203:241-249.
    • (1994) Virology , vol.203 , pp. 241-249
    • Johnson, A.J.1    Guirakhoo, F.2    Roehrig, J.T.3
  • 18
    • 0027478991 scopus 로고
    • Proper maturation of the japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein
    • Konishi, E., and P. W. Mason. 1993. Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein. J. Virol. 67:1672-1675.
    • (1993) J. Virol. , vol.67 , pp. 1672-1675
    • Konishi, E.1    Mason, P.W.2
  • 19
    • 0027264853 scopus 로고
    • Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3
    • Lobigs, M. 1993. Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3. Proc. Natl. Acad. Sci. USA 90:6218-6222.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6218-6222
    • Lobigs, M.1
  • 20
    • 0030964918 scopus 로고    scopus 로고
    • Aberrant trafficking of hepatitis b virus glycoproteins in cells in which N-glycan processing is inhibited
    • Lu, X., A. Mehta, M. Dadmarz, R. Dwek, B. S. Blumberg, and T. M. Block. 1997. Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited. Proc. Natl. Acad. Sci. USA 94:2380-2385.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2380-2385
    • Lu, X.1    Mehta, A.2    Dadmarz, M.3    Dwek, R.4    Blumberg, B.S.5    Block, T.M.6
  • 21
    • 0032560488 scopus 로고    scopus 로고
    • α-Glucosidase inhibitors as potential broad based anti-viral agents
    • Mehta, A., N. Zitzmann, P. M. Rudd, T. M. Block, and R. A. Dwek. 1998. α-Glucosidase inhibitors as potential broad based anti-viral agents. FEBS Lett. 430:17-22.
    • (1998) FEBS Lett. , vol.430 , pp. 17-22
    • Mehta, A.1    Zitzmann, N.2    Rudd, P.M.3    Block, T.M.4    Dwek, R.A.5
  • 22
    • 0029865151 scopus 로고    scopus 로고
    • Ecdysone-inducible gene expression in mammalian cells and transgenic mice
    • No, D., T. P. Yao, and R. M. Evans. 1996. Ecdysone-inducible gene expression in mammalian cells and transgenic mice. Proc. Natl. Acad. Sci. USA 93:3346-3351.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3346-3351
    • No, D.1    Yao, T.P.2    Evans, R.M.3
  • 23
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken, A., and B. Moss. 1996. Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271:97-103.
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 24
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson, J. R., A. Ora, P. N. Van, and A. Helenius. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 6:1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 25
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 26
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), Lippincott-Raven Publishers, Philadelphia, Pa.
    • Rice, C. M. 1996. Flaviviridae: the viruses and their replication, p. 931-959. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 931-959
    • Rice, C.M.1
  • 27
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler, K., S. L. Allison, J. Schalich, and F. X. Heinz. 1997. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71:8475-8481.
    • (1997) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 28
    • 0028822211 scopus 로고
    • Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
    • Stocks, C. E., and M. Lobigs. 1995. Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro. J. Virol. 69:8123-8126.
    • (1995) J. Virol. , vol.69 , pp. 8123-8126
    • Stocks, C.E.1    Lobigs, M.2
  • 29
    • 0031935890 scopus 로고    scopus 로고
    • Signal peptidase cleavage at the flavivirus C-prM junction: Dependence on the viral ns2b-3 protease for efficient processing requires determinants in C, the signal peptide, and prM
    • Stocks, C. E., and M. Lobigs. 1998. Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM. J. Virol. 72:2141-2149.
    • (1998) J. Virol. , vol.72 , pp. 2141-2149
    • Stocks, C.E.1    Lobigs, M.2
  • 30
    • 0031733824 scopus 로고    scopus 로고
    • Lectins as chaperones in glycoprotein folding
    • Trombetta, E. S., and A. Helenius. 1998. Lectins as chaperones in glycoprotein folding. Curr. Opin. Struct. Biol. 8:587-592.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 587-592
    • Trombetta, E.S.1    Helenius, A.2
  • 31
    • 0033053594 scopus 로고    scopus 로고
    • PrM- and cell-binding domains of dengue virus E protein
    • Wang, S., R. He, and R. Anderson. 1999. PrM- and cell-binding domains of dengue virus E protein. J. Virol. 73:2547-2551.
    • (1999) J. Virol. , vol.73 , pp. 2547-2551
    • Wang, S.1    He, R.2    Anderson, R.3
  • 32
    • 0031975746 scopus 로고    scopus 로고
    • Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis b virus middle envelope protein particles
    • Werr, M., and R. Prange. 1998. Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles. J. Virol. 72:778-782.
    • (1998) J. Virol. , vol.72 , pp. 778-782
    • Werr, M.1    Prange, R.2
  • 33
    • 0028916051 scopus 로고
    • Formation of the flavivirus envelope: Role of the viral NS2B-NS3 protease
    • Yamshchikov, V. F., and R. W. Compans. 1995. Formation of the flavivirus envelope: role of the viral NS2B-NS3 protease. J. Virol. 69:1995-2003.
    • (1995) J. Virol. , vol.69 , pp. 1995-2003
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 34
    • 0027308196 scopus 로고
    • Regulation of the late events in flavivirus protein processing and maturation
    • Yamshchikov, V. F., and R. W. Compans. 1993. Regulation of the late events in flavivirus protein processing and maturation. Virology 192:38-51.
    • (1993) Virology , vol.192 , pp. 38-51
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 35
    • 0030923806 scopus 로고    scopus 로고
    • Upregulation of signalase processing and induction of prM-E secretion by the flavivirus NS2B-NS3 protease: Roles of protease components
    • Yamshchikov, V. F., D. W. Trent, and R. W. Compans. 1997. Upregulation of signalase processing and induction of prM-E secretion by the flavivirus NS2B-NS3 protease: roles of protease components. J. Virol. 71:4364-4371.
    • (1997) J. Virol. , vol.71 , pp. 4364-4371
    • Yamshchikov, V.F.1    Trent, D.W.2    Compans, R.W.3
  • 36
    • 0029798646 scopus 로고    scopus 로고
    • Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding
    • Zheng, Z., E. Maidji, S. Tugizov, and L. Pereira. 1996. Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding. J. Virol. 70:8029-8040.
    • (1996) J. Virol. , vol.70 , pp. 8029-8040
    • Zheng, Z.1    Maidji, E.2    Tugizov, S.3    Pereira, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.