메뉴 건너뛰기




Volumn 87, Issue 7, 2013, Pages 3640-3654

5-(perylen-3-yl)ethynyl-arabino-uridine (aUY11), an arabino-based rigid amphipathic fusion inhibitor, targets virion envelope lipids to inhibit fusion of influenza virus, hepatitis C virus, and other enveloped viruses

Author keywords

[No Author keywords available]

Indexed keywords

5 (PERYLEN 3 YL)ETHYNYLARABINOURIDINE; ANTIVIRUS AGENT; AUY 11; LIPID; LIPOSOME; NUCLEOSIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84875507361     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02882-12     Document Type: Article
Times cited : (63)

References (58)
  • 2
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild CT, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ. 1994. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U. S. A. 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 6
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik LV, Kozlov MM. 2003. Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72:175-207.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 7
    • 0031012628 scopus 로고    scopus 로고
    • An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids
    • Chernomordik LV, Leikina E, Frolov VA, Bronk P, Zimmerberg J. 1997. An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids. J. Cell Biol. 136:81-93.
    • (1997) J. Cell Biol. , vol.136 , pp. 81-93
    • Chernomordik, L.V.1    Leikina, E.2    Frolov, V.A.3    Bronk, P.4    Zimmerberg, J.5
  • 8
    • 0028864309 scopus 로고
    • Inhibition of influenza-induced membrane fusion by lysophosphatidylcholine
    • Gunther-Ausborn S, Praetor A, Stegmann T. 1995. Inhibition of influenza-induced membrane fusion by lysophosphatidylcholine. J. Biol. Chem. 270:29279-29285.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29279-29285
    • Gunther-Ausborn, S.1    Praetor, A.2    Stegmann, T.3
  • 9
    • 0034617991 scopus 로고    scopus 로고
    • Rabies virus-induced membrane fusion pathway
    • Gaudin Y. 2000. Rabies virus-induced membrane fusion pathway. J. Cell Biol. 150:601-612.
    • (2000) J. Cell Biol. , vol.150 , pp. 601-612
    • Gaudin, Y.1
  • 14
    • 0036893332 scopus 로고    scopus 로고
    • Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication
    • Blight KJ, McKeating JA, Rice CM. 2002. Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J. Virol. 76: 13001-13014.
    • (2002) J. Virol. , vol.76 , pp. 13001-13014
    • Blight, K.J.1    McKeating, J.A.2    Rice, C.M.3
  • 15
    • 75449106558 scopus 로고    scopus 로고
    • During lytic infections, herpes simplex virus type 1 DNA is in complexes with the properties of unstable nucleosomes
    • Lacasse JJ, Schang LM. 2010. During lytic infections, herpes simplex virus type 1 DNA is in complexes with the properties of unstable nucleosomes. J. Virol. 84:1920-1933.
    • (2010) J. Virol. , vol.84 , pp. 1920-1933
    • Lacasse, J.J.1    Schang, L.M.2
  • 18
    • 0024347619 scopus 로고
    • Membrane "fluidity" as detected by diphenylhexatriene probes
    • Lentz BR. 1989. Membrane "fluidity" as detected by diphenylhexatriene probes. Chem. Phys. Lipids 50:171-190.
    • (1989) Chem. Phys. Lipids , vol.50 , pp. 171-190
    • Lentz, B.R.1
  • 19
    • 77954044356 scopus 로고    scopus 로고
    • Peptide inhibitors of denguevirus entry target a late-stage fusion intermediate
    • doi:10.1371/journal.ppat.1000851.
    • Schmidt AG, Yang PL, Harrison SC. 2010. Peptide inhibitors of denguevirus entry target a late-stage fusion intermediate. PLoS Pathog. 6:e1000851. doi:10.1371/journal.ppat.1000851.
    • (2010) PLoS Pathog. , vol.6
    • Schmidt, A.G.1    Yang, P.L.2    Harrison, S.C.3
  • 20
    • 28044459176 scopus 로고    scopus 로고
    • The broad anti-viral agent glycyrrhizin directly modulates the fluidity of plasma membrane and HIV-1 envelope
    • Harada S. 2005. The broad anti-viral agent glycyrrhizin directly modulates the fluidity of plasma membrane and HIV-1 envelope. Biochem. J. 392:191-199.
    • (2005) Biochem. J. , vol.392 , pp. 191-199
    • Harada, S.1
  • 21
    • 0029045414 scopus 로고
    • The relationship between membrane fluidity and permeabilities to water, solutes, ammonia, and protons
    • Lande MB, Donovan JM, Zeidel ML. 1995. The relationship between membrane fluidity and permeabilities to water, solutes, ammonia, and protons. J. Gen. Physiol. 106:67-84.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 67-84
    • Lande, M.B.1    Donovan, J.M.2    Zeidel, M.L.3
  • 23
    • 0018225465 scopus 로고
    • Fluidity parameters of lipid regions determined by fluorescence polarization
    • Shinitzky M, Barenholz Y. 1978. Fluidity parameters of lipid regions determined by fluorescence polarization. Biochim. Biophys. Acta 515: 367-394.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 367-394
    • Shinitzky, M.1    Barenholz, Y.2
  • 24
    • 0001283095 scopus 로고
    • Kinetic effects in the differential scanning calorimetry cooling scans of phosphatidylethanolamines
    • Epand RM, Epand RF. 1988. Kinetic effects in the differential scanning calorimetry cooling scans of phosphatidylethanolamines. Chem. Phys. Lipids 49:101-104.
    • (1988) Chem. Phys. Lipids , vol.49 , pp. 101-104
    • Epand, R.M.1    Epand, R.F.2
  • 25
    • 0022977468 scopus 로고
    • Virus replication inhibitory peptide inhibits the conversion of phospholipid bilayers to the hexagonal phase
    • Epand RM. 1986. Virus replication inhibitory peptide inhibits the conversion of phospholipid bilayers to the hexagonal phase. Biosci. Rep. 6:647-653.
    • (1986) Biosci. Rep. , vol.6 , pp. 647-653
    • Epand, R.M.1
  • 27
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution
    • Wilson IA, Skehel JJ, Wiley DC. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution. Nature 289: 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 28
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95:409-417.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 29
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC, Skehel JJ. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 30
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371: 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 32
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • Kielian M. 2006. Class II virus membrane fusion proteins. Virology 344: 38-47.
    • (2006) Virology , vol.344 , pp. 38-47
    • Kielian, M.1
  • 33
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • Roche S, Rey RA, Gaudin Y, Bressanelli S. 2007. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 315: 843-848.
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, R.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 34
    • 0026018237 scopus 로고
    • Reversible conformational changes and fusion activity of rabies virus glycoprotein
    • Gaudin Y, Tuffereau C, Segretain D, Knossow M, Flamand A. 1991. Reversible conformational changes and fusion activity of rabies virus glycoprotein. J. Virol. 65:4853-4859.
    • (1991) J. Virol. , vol.65 , pp. 4853-4859
    • Gaudin, Y.1    Tuffereau, C.2    Segretain, D.3    Knossow, M.4    Flamand, A.5
  • 35
    • 35748931458 scopus 로고    scopus 로고
    • Lipids as modulators of membrane fusion mediated by viral fusion proteins
    • Teissier E, Pecheur EI. 2007. Lipids as modulators of membrane fusion mediated by viral fusion proteins. Eur. Biophys. J. 36:887-899.
    • (2007) Eur. Biophys. J. , vol.36 , pp. 887-899
    • Teissier, E.1    Pecheur, E.I.2
  • 36
    • 0030586161 scopus 로고    scopus 로고
    • Non-bilayer lipids and biological fusion intermediates
    • Chernomordik L. 1996. Non-bilayer lipids and biological fusion intermediates. Chem. Phys. Lipids 81:203-213.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 203-213
    • Chernomordik, L.1
  • 38
    • 3543095614 scopus 로고    scopus 로고
    • Effect of membrane curvature-modifying lipids on membrane fusion by tick-borne encephalitis virus
    • Stiasny K, Heinz FX. 2004. Effect of membrane curvature-modifying lipids on membrane fusion by tick-borne encephalitis virus. J. Virol. 78: 8536-8542.
    • (2004) J. Virol. , vol.78 , pp. 8536-8542
    • Stiasny, K.1    Heinz, F.X.2
  • 39
    • 0027441876 scopus 로고
    • Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger
    • Vogel SS, Leikina EA, Chernomordik LV. 1993. Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger. J. Biol. Chem. 268:25764-25768.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25764-25768
    • Vogel, S.S.1    Leikina, E.A.2    Chernomordik, L.V.3
  • 43
    • 79251528593 scopus 로고    scopus 로고
    • Targeting cell entry of enveloped viruses as an antiviral strategy
    • Teissier E, Penin F, Pecheur EI. 2011. Targeting cell entry of enveloped viruses as an antiviral strategy. Molecules 16:221-250.
    • (2011) Molecules , vol.16 , pp. 221-250
    • Teissier, E.1    Penin, F.2    Pecheur, E.I.3
  • 45
    • 77953993735 scopus 로고    scopus 로고
    • Membranotropic effects of arbidol, a broad anti-viral molecule, on phospholipid model membranes
    • Villalain J. 2010. Membranotropic effects of arbidol, a broad anti-viral molecule, on phospholipid model membranes. J. Phys. Chem. B 114: 8544-8554.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8544-8554
    • Villalain, J.1
  • 46
    • 58249083139 scopus 로고    scopus 로고
    • Characteristics of arbidol-resistant mutants of influenza virus: implications for the mechanism of anti-influenza action of arbidol
    • Leneva IA, Russell RJ, Boriskin YS, Hay AJ. 2009. Characteristics of arbidol-resistant mutants of influenza virus: implications for the mechanism of anti-influenza action of arbidol. Antiviral Res. 81:132-140.
    • (2009) Antiviral Res. , vol.81 , pp. 132-140
    • Leneva, I.A.1    Russell, R.J.2    Boriskin, Y.S.3    Hay, A.J.4
  • 48
  • 52
    • 77951294418 scopus 로고    scopus 로고
    • A peptide derived from hepatitis C virus E2 envelope protein inhibits a postbinding step in HCV entry
    • Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. 2010. A peptide derived from hepatitis C virus E2 envelope protein inhibits a postbinding step in HCV entry. Antiviral Res. 86:172-179.
    • (2010) Antiviral Res. , vol.86 , pp. 172-179
    • Liu, R.1    Tewari, M.2    Kong, R.3    Zhang, R.4    Ingravallo, P.5    Ralston, R.6
  • 53
    • 77954995414 scopus 로고    scopus 로고
    • Respiratory syncytial virus-neutralizing monoclonal antibodies motavizumab and palivizumab inhibit fusion
    • Huang K, Incognito L, Cheng X, Ulbrandt ND, Wu H. 2010. Respiratory syncytial virus-neutralizing monoclonal antibodies motavizumab and palivizumab inhibit fusion. J. Virol. 84:8132-8140.
    • (2010) J. Virol. , vol.84 , pp. 8132-8140
    • Huang, K.1    Incognito, L.2    Cheng, X.3    Ulbrandt, N.D.4    Wu, H.5
  • 55
    • 33846574670 scopus 로고    scopus 로고
    • Isolation and characterization of human immunodeficiency virus type 1 resistant to the small-molecule CCR5 antagonist TAK-652
    • Baba M, Miyake H, Wang X, Okamoto M, Takashima K. 2007. Isolation and characterization of human immunodeficiency virus type 1 resistant to the small-molecule CCR5 antagonist TAK-652. Antimicrob. Agents Chemother. 51:707-715.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 707-715
    • Baba, M.1    Miyake, H.2    Wang, X.3    Okamoto, M.4    Takashima, K.5
  • 58
    • 0026100907 scopus 로고
    • Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway
    • Wittels M, Spear PG. 1991. Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway. Virus Res. 18: 271-290.
    • (1991) Virus Res. , vol.18 , pp. 271-290
    • Wittels, M.1    Spear, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.