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Volumn 10, Issue 6, 2008, Pages 646-654

A fusogenic segment of glycoprotein H from herpes simplex virus enhances transfection efficiency of cationic liposomes

Author keywords

Cationic liposome; Endosomal release; Fusogenic peptide; Non viral gene delivery

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; GLYCOPROTEIN; GLYCOPROTEIN H; LIPOSOME; LUCIFERASE;

EID: 46649091525     PISSN: 1099498X     EISSN: 15212254     Source Type: Journal    
DOI: 10.1002/jgm.1184     Document Type: Article
Times cited : (49)

References (31)
  • 1
    • 33846298058 scopus 로고    scopus 로고
    • Modifying the proliferative state of target cells to control DNA expression and identifying cell types transfected in vivo
    • Riddle KW, Kong HJ, Leach JK, et al. Modifying the proliferative state of target cells to control DNA expression and identifying cell types transfected in vivo. Mol Ther 2007; 15: 361-368.
    • (2007) Mol Ther , vol.15 , pp. 361-368
    • Riddle, K.W.1    Kong, H.J.2    Leach, J.K.3
  • 2
    • 33748290173 scopus 로고    scopus 로고
    • Gene therapy progress and prospects: Non-viral gene therapy by systemic delivery
    • Li SD, Huang L. Gene therapy progress and prospects: non-viral gene therapy by systemic delivery. Gene Ther 2006; 13: 1313-1319.
    • (2006) Gene Ther , vol.13 , pp. 1313-1319
    • Li, S.D.1    Huang, L.2
  • 3
    • 0036560326 scopus 로고    scopus 로고
    • Intracellular barriers to non-viral gene transfer
    • Lechardeur D, Lukacs GL. Intracellular barriers to non-viral gene transfer. Curr Gene Ther 2002; 2: 183-194.
    • (2002) Curr Gene Ther , vol.2 , pp. 183-194
    • Lechardeur, D.1    Lukacs, G.L.2
  • 4
    • 14744297069 scopus 로고    scopus 로고
    • Intracellular routing of plasmid DNA during non-viral gene transfer
    • Lechardeur D, Verkman AS, Lukacs GL. Intracellular routing of plasmid DNA during non-viral gene transfer. Advanced Drug Deliv Rev 2005; 57: 755-767.
    • (2005) Advanced Drug Deliv Rev , vol.57 , pp. 755-767
    • Lechardeur, D.1    Verkman, A.S.2    Lukacs, G.L.3
  • 5
    • 0031104992 scopus 로고    scopus 로고
    • Influence of membrane-active peptides on lipospermine/DNA complex mediated gene transfer
    • Kichler A, Mechtler K, Behr JP, et al. Influence of membrane-active peptides on lipospermine/DNA complex mediated gene transfer. Bioconjug Chem 1997; 8: 213-221.
    • (1997) Bioconjug Chem , vol.8 , pp. 213-221
    • Kichler, A.1    Mechtler, K.2    Behr, J.P.3
  • 6
    • 33847306540 scopus 로고    scopus 로고
    • Novel histidine-conjugated galactosylated cationic liposomes for efficient hepatocyte-selective gene transfer in human hepatoma HepG2 cells
    • Shigeta K, Kawakami S, Higuchi Y, et al. Novel histidine-conjugated galactosylated cationic liposomes for efficient hepatocyte-selective gene transfer in human hepatoma HepG2 cells. J Control Release 2007; 118: 262-270.
    • (2007) J Control Release , vol.118 , pp. 262-270
    • Shigeta, K.1    Kawakami, S.2    Higuchi, Y.3
  • 7
    • 46649117575 scopus 로고    scopus 로고
    • Cationic liposomes as non-viral carriers of gene medicines: Resolved issues, open questions, and future promises
    • Karmali PP, Chaudhuri A. Cationic liposomes as non-viral carriers of gene medicines: resolved issues, open questions, and future promises. Med Res Rev 2006.
    • (2006) Med Res Rev
    • Karmali, P.P.1    Chaudhuri, A.2
  • 8
    • 33745253111 scopus 로고    scopus 로고
    • Selective gene delivery for cancer therapy using cationic liposomes: In vivo proof applicability
    • Dass CR, Choong PF. Selective gene delivery for cancer therapy using cationic liposomes: in vivo proof applicability. J Control Release 2006; 113: 155-163.
    • (2006) J Control Release , vol.113 , pp. 155-163
    • Dass, C.R.1    Choong, P.F.2
  • 9
    • 33750515643 scopus 로고    scopus 로고
    • Cationic liposome-DNA complexes: From liquid crystal science to gene delivery applications
    • Safinya CR, Ewert K, Ahmad A, et al. Cationic liposome-DNA complexes: from liquid crystal science to gene delivery applications. Philos Trans 2006; 364: 2573-2596.
    • (2006) Philos Trans , vol.364 , pp. 2573-2596
    • Safinya, C.R.1    Ewert, K.2    Ahmad, A.3
  • 11
    • 0029019120 scopus 로고
    • Fusion of cationic liposomes with mammalian cells occurs after endocytosis
    • Wrobel I, Collins D. Fusion of cationic liposomes with mammalian cells occurs after endocytosis. Biochim Biophys Acta 1995; 1235: 296-304.
    • (1995) Biochim Biophys Acta , vol.1235 , pp. 296-304
    • Wrobel, I.1    Collins, D.2
  • 12
    • 0029056088 scopus 로고
    • Cellular and molecular barriers to gene transfer by a cationic lipid
    • Zabner J, Fasbender AJ, Moninger T, et al. Cellular and molecular barriers to gene transfer by a cationic lipid. J Biol Chem 1995; 270: 18997-19007.
    • (1995) J Biol Chem , vol.270 , pp. 18997-19007
    • Zabner, J.1    Fasbender, A.J.2    Moninger, T.3
  • 13
    • 0028097638 scopus 로고
    • DNA transfection mediated by cationic liposomes containing lipopolylysine: Characterization and mechanism of action
    • Zhou X, Huang L. DNA transfection mediated by cationic liposomes containing lipopolylysine: characterization and mechanism of action. Biochim Biophys Acta 1994; 1189: 195-203.
    • (1994) Biochim Biophys Acta , vol.1189 , pp. 195-203
    • Zhou, X.1    Huang, L.2
  • 14
    • 0342265531 scopus 로고    scopus 로고
    • Mechanisms of gene transfer mediated by lipoplexes associated with targeting ligands or pH-sensitive peptides
    • Simoes S, Slepushkin V, Pires P, et al. Mechanisms of gene transfer mediated by lipoplexes associated with targeting ligands or pH-sensitive peptides. Gene Ther 1999; 6: 1798-1807.
    • (1999) Gene Ther , vol.6 , pp. 1798-1807
    • Simoes, S.1    Slepushkin, V.2    Pires, P.3
  • 15
    • 27944441290 scopus 로고    scopus 로고
    • Unique features of a pH-sensitive fusogenic peptide that improves the transfection efficiency of cationic liposomes
    • Futaki S, Masui Y, Nakase I, et al. Unique features of a pH-sensitive fusogenic peptide that improves the transfection efficiency of cationic liposomes. J Gene Med 2005; 7: 1450-1458.
    • (2005) J Gene Med , vol.7 , pp. 1450-1458
    • Futaki, S.1    Masui, Y.2    Nakase, I.3
  • 16
    • 0031825183 scopus 로고    scopus 로고
    • Gene delivery by negatively charged ternary complexes of DNA, cationic liposomes and transferrin or fusigenic peptides
    • Simoes S, Slepushkin V, Gaspar R, et al. Gene delivery by negatively charged ternary complexes of DNA, cationic liposomes and transferrin or fusigenic peptides. Gene Ther 1998; 5: 955-964.
    • (1998) Gene Ther , vol.5 , pp. 955-964
    • Simoes, S.1    Slepushkin, V.2    Gaspar, R.3
  • 17
    • 0030010945 scopus 로고    scopus 로고
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region. J Biol Chem 1996; 271: 13417-13421.
    • (1996) J Biol Chem , vol.271 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3
  • 18
    • 0029968695 scopus 로고    scopus 로고
    • Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues
    • Delahunty MD, Rhee I, Freed EO, et al. Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: identification of critical glycine residues. Virology 1996; 218: 94-102.
    • (1996) Virology , vol.218 , pp. 94-102
    • Delahunty, M.D.1    Rhee, I.2    Freed, E.O.3
  • 19
    • 0029062097 scopus 로고
    • Requirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusion
    • Schaal H, Klein M, Gehrmann P, et al. Requirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusion. J Virol 1995; 69: 3308-3314.
    • (1995) J Virol , vol.69 , pp. 3308-3314
    • Schaal, H.1    Klein, M.2    Gehrmann, P.3
  • 20
    • 29744464073 scopus 로고    scopus 로고
    • Exploration of peptide motifs for potent non-viral gene delivery highly selective for dividing cells
    • Parker AL, Collins L, Zhang X, et al. Exploration of peptide motifs for potent non-viral gene delivery highly selective for dividing cells. J Gene Med 2005; 7: 1545-1554.
    • (2005) J Gene Med , vol.7 , pp. 1545-1554
    • Parker, A.L.1    Collins, L.2    Zhang, X.3
  • 21
    • 13944263161 scopus 로고    scopus 로고
    • The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family
    • Gianni T, Martelli PL, Casadio R, et al. The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family. J Virol 2005; 79: 2931-2940.
    • (2005) J Virol , vol.79 , pp. 2931-2940
    • Gianni, T.1    Martelli, P.L.2    Casadio, R.3
  • 22
    • 0031054450 scopus 로고    scopus 로고
    • Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H
    • Galdiero M, Whiteley A, Bruun B, et al. Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H. J Virol 1997; 71: 8.
    • (1997) J Virol , vol.71 , pp. 8
    • Galdiero, M.1    Whiteley, A.2    Bruun, B.3
  • 23
    • 0029860880 scopus 로고    scopus 로고
    • Characterization of herpes simplex virus type 1 recombinants with mutations in the cytoplasmic tail of glycoprotein H
    • Browne HM, Bruun BC, Minson AC. Characterization of herpes simplex virus type 1 recombinants with mutations in the cytoplasmic tail of glycoprotein H. J Gen Virol 1996; 77: 2569-2573.
    • (1996) J Gen Virol , vol.77 , pp. 2569-2573
    • Browne, H.M.1    Bruun, B.C.2    Minson, A.C.3
  • 24
    • 23244468581 scopus 로고    scopus 로고
    • Fusogenic domains in herpes simplex virus type 1 glycoprotein H
    • Galdiero S, Falanga A, Vitiello M, et al. Fusogenic domains in herpes simplex virus type 1 glycoprotein H. J Biol Chem 2005; 280: 28632-28643.
    • (2005) J Biol Chem , vol.280 , pp. 28632-28643
    • Galdiero, S.1    Falanga, A.2    Vitiello, M.3
  • 25
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck D, Hoekstra D, Pagano R. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 1981; 20: 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.1    Hoekstra, D.2    Pagano, R.3
  • 26
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 1983; 65: 55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 27
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith P, Krohn R, Hermanson G, et al. Measurement of protein using bicinchoninic acid. Anal Biochem 1985; 150: 76-85.
    • (1985) Anal Biochem , vol.150 , pp. 76-85
    • Smith, P.1    Krohn, R.2    Hermanson, G.3
  • 28
    • 5644229850 scopus 로고    scopus 로고
    • The many mechanisms of viral membrane fusion proteins
    • Earp LJ, Delos SE, Park HE, et al. The many mechanisms of viral membrane fusion proteins. Curr Top Microbiol Immunol 2005; 285: 25-66.
    • (2005) Curr Top Microbiol Immunol , vol.285 , pp. 25-66
    • Earp, L.J.1    Delos, S.E.2    Park, H.E.3
  • 29
    • 0037810986 scopus 로고    scopus 로고
    • Viral fusion proteins: Multiple regions contribute to membrane fusion
    • Peisajovich SG, Shai Y. Viral fusion proteins: multiple regions contribute to membrane fusion. Biochim Biophys Acta 2003; 1614: 122-129.
    • (2003) Biochim Biophys Acta , vol.1614 , pp. 122-129
    • Peisajovich, S.G.1    Shai, Y.2
  • 30
    • 0034628898 scopus 로고    scopus 로고
    • Paramyxovirus F1 protein has two fusion peptides: Implications for the mechanism of membrane fusion
    • Peisajovich SG, Samuel O, Shai Y. Paramyxovirus F1 protein has two fusion peptides: implications for the mechanism of membrane fusion. J Mol Biol 2000; 296: 1353-1365.
    • (2000) J Mol Biol , vol.296 , pp. 1353-1365
    • Peisajovich, S.G.1    Samuel, O.2    Shai, Y.3
  • 31
    • 33846813849 scopus 로고    scopus 로고
    • Fusogenic peptides enhance endosomal escape improving siRNA-induced silencing of oncogenes
    • Oliveira S, Rooy Iv, Kranenburg O, et al. Fusogenic peptides enhance endosomal escape improving siRNA-induced silencing of oncogenes. Int J Pharm 2007; 331: 211-214.
    • (2007) Int J Pharm , vol.331 , pp. 211-214
    • Oliveira, S.1    Rooy, I.2    Kranenburg, O.3


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