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Volumn 88, Issue 15, 2014, Pages 8556-8564

Inhibition of arenavirus infection by a glycoprotein-derived peptide with a novel mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; AVP P; GLYCOPROTEIN; HYBRID PROTEIN; UNCLASSIFIED DRUG;

EID: 84903885404     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01133-14     Document Type: Article
Times cited : (15)

References (31)
  • 1
    • 84903887427 scopus 로고    scopus 로고
    • NIAID. NIAID biodefense research agenda for CDC category A agents. NIH publication no. 03-5308. NIH, Bethesda, MD.
    • NIAID. 2002. NIAID biodefense research agenda for CDC category A agents. NIH publication no. 03-5308. NIH, Bethesda, MD.
    • (2002)
  • 4
    • 0029093727 scopus 로고
    • Review of cases of nosocomial Lassa fever in Nigeria: the high price of poor medical practice
    • Fisher-Hoch SP, Tomori O, Nasidi A, Perez-Oronoz GI, Fakile Y, Hutwagner L, McCormick JB. 1995. Review of cases of nosocomial Lassa fever in Nigeria: the high price of poor medical practice. BMJ 311:857-859. http://dx.doi.org/10.1136/bmj.311.7009.857.
    • (1995) BMJ , vol.311 , pp. 857-859
    • Fisher-Hoch, S.P.1    Tomori, O.2    Nasidi, A.3    Perez-Oronoz, G.I.4    Fakile, Y.5    Hutwagner, L.6    McCormick, J.B.7
  • 5
    • 0036189297 scopus 로고    scopus 로고
    • Human infection with arenaviruses in the Americas
    • Peters CJ. 2002. Human infection with arenaviruses in the Americas. Curr. Top. Microbiol. Immunol. 262:65-74.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.262 , pp. 65-74
    • Peters, C.J.1
  • 7
    • 33750571888 scopus 로고    scopus 로고
    • Ribavirin-induced anemia: mechanisms, risk factors and related targets for future research
    • Russmann S, Grattagliano I, Portincasa P, Palmieri VO, Palasciano G. 2006. Ribavirin-induced anemia: mechanisms, risk factors and related targets for future research. Curr. Med. Chem. 13:3351-3357. http://dx.doi.org/10.2174/092986706778773059.
    • (2006) Curr. Med. Chem. , vol.13 , pp. 3351-3357
    • Russmann, S.1    Grattagliano, I.2    Portincasa, P.3    Palmieri, V.O.4    Palasciano, G.5
  • 8
    • 33744935523 scopus 로고    scopus 로고
    • Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I fusion proteins
    • Eschli B, Quirin K, Wepf A, Weber J, Zinkernagel RM, Hengartner H. 2006. Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I fusion proteins. J. Virol. 80:5897-5907. http://dx.doi.org/10.1128/JVI.00008-06.
    • (2006) J. Virol. , vol.80 , pp. 5897-5907
    • Eschli, B.1    Quirin, K.2    Wepf, A.3    Weber, J.4    Zinkernagel, R.M.5    Hengartner, H.6
  • 10
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Muñoz-Barroso I, Durell S, Sakaguchi K, Appella E, Blumenthal R. 1998. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell Biol. 140:315-323. http://dx.doi.org/10.1083/jcb.140.2.315.
    • (1998) J. Cell Biol. , vol.140 , pp. 315-323
    • Muñoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 11
    • 33745400398 scopus 로고    scopus 로고
    • Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
    • Sainz B, Jr, Mossel EC, Gallaher WR, Peters CJ, Wilson RB, Garry RF. 2006. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. Virus Res. 120:146-155. http://dx.doi.org/10.1016/j.virusres.2006.03.001.
    • (2006) Virus Res. , vol.120 , pp. 146-155
    • Sainz Jr., B.1    Mossel, E.C.2    Gallaher, W.R.3    Peters, C.J.4    Wilson, R.B.5    Garry, R.F.6
  • 12
    • 82755163036 scopus 로고    scopus 로고
    • Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus
    • Lee KK, Pessi A, Gui L, Santoprete A, Talekar A, Moscona A, Porotto M. 2011. Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus. J. Biol. Chem. 286:42141-42149. http://dx.doi.org/10.1074/jbc.M111.254243.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42141-42149
    • Lee, K.K.1    Pessi, A.2    Gui, L.3    Santoprete, A.4    Talekar, A.5    Moscona, A.6    Porotto, M.7
  • 13
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai viruscell fusion: an emerging similarity with functional domains of other viruses
    • Rapaport D, Ovadia M, Shai Y. 1995. A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai viruscell fusion: an emerging similarity with functional domains of other viruses. EMBO J. 14:5524-5531.
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 14
    • 0033771310 scopus 로고    scopus 로고
    • Functional importance of the coiled-coil of the Ebola virus glycoprotein
    • Watanabe S, Takada A, Watanabe T, Ito H, Kida H, Kawaoka Y. 2000. Functional importance of the coiled-coil of the Ebola virus glycoprotein. J. Virol. 74:10194-10201. http://dx.doi.org/10.1128/JVI.74.21.10194-10201.2000.
    • (2000) J. Virol. , vol.74 , pp. 10194-10201
    • Watanabe, S.1    Takada, A.2    Watanabe, T.3    Ito, H.4    Kida, H.5    Kawaoka, Y.6
  • 15
    • 84934434650 scopus 로고    scopus 로고
    • Purification and electron microscopy of coronavirus particles
    • Neuman BW, Adair BD, Yeager M, Buchmeier MJ. 2008. Purification and electron microscopy of coronavirus particles. Methods Mol. Biol. 454: 129-136. http://dx.doi.org/10.1007/978-1-59745-181-9_12.
    • (2008) Methods Mol. Biol. , vol.454 , pp. 129-136
    • Neuman, B.W.1    Adair, B.D.2    Yeager, M.3    Buchmeier, M.J.4
  • 16
    • 0021673527 scopus 로고
    • Fluorescence method for measuring the kinetics of fusion between biological membranes
    • Hoekstra D, de Boer T, Klappe K, Wilschut J. 1984. Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 23:5675-5681. http://dx.doi.org/10.1021/bi00319a002.
    • (1984) Biochemistry , vol.23 , pp. 5675-5681
    • Hoekstra, D.1    de Boer, T.2    Klappe, K.3    Wilschut, J.4
  • 17
    • 0028241840 scopus 로고
    • Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike
    • Di Simone C, Zandonatti MA, Buchmeier MJ. 1994. Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike. Virology 198:455-465. http://dx.doi.org/10.1006/viro.1994.1057.
    • (1994) Virology , vol.198 , pp. 455-465
    • Di Simone, C.1    Zandonatti, M.A.2    Buchmeier, M.J.3
  • 18
    • 14744278960 scopus 로고    scopus 로고
    • Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis
    • Neuman BW, Adair BD, Burns JW, Milligan RA, Buchmeier MJ, Yeager M. 2005. Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis. J. Virol. 79:3822-3830. http://dx.doi.org/10.1128/JVI.79.6.3822-3830.2005.
    • (2005) J. Virol. , vol.79 , pp. 3822-3830
    • Neuman, B.W.1    Adair, B.D.2    Burns, J.W.3    Milligan, R.A.4    Buchmeier, M.J.5    Yeager, M.6
  • 19
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobic-ity scale for proteins at membrane interfaces
    • Wimley WC, White SH. 1996. Experimentally determined hydrophobic-ity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848. http://dx.doi.org/10.1038/nsb1096-842.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 20
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile Virus infectivity
    • Hrobowski YM, Garry RF, Michael SF. 2005. Peptide inhibitors of dengue virus and West Nile Virus infectivity. Virol. J. 2:49. http://dx.doi.org/10.1186/1743-422X-2-49.
    • (2005) Virol. J. , vol.2 , pp. 49
    • Hrobowski, Y.M.1    Garry, R.F.2    Michael, S.F.3
  • 21
    • 79951794466 scopus 로고    scopus 로고
    • Peptide inhibition of human cytomegalovirus infection
    • Melnik LI, Garry RF, Morris CA. 2011. Peptide inhibition of human cytomegalovirus infection. Virol. J. 8:76. http://dx.doi.org/10.1186/1743-422X-8-76.
    • (2011) Virol. J. , vol.8 , pp. 76
    • Melnik, L.I.1    Garry, R.F.2    Morris, C.A.3
  • 22
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion
    • Blumenthal R, Sarkar DP, Durell S, Howard DE, Morris SJ. 1996. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion. J. Cell Biol. 135:63-71. http://dx.doi.org/10.1083/jcb.135.1.63.
    • (1996) J. Cell Biol. , vol.135 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 23
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli T, Pelletier SL, Henis YI, White JM. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559-569. http://dx.doi.org/10.1083/jcb.133.3.559.
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 24
    • 0036309399 scopus 로고    scopus 로고
    • Characterization of the equilibrium between the native and fusion-inactive conformation of the rabies virus glycoprotein indicates that the fusion complex is made of several trimers
    • Roche S, Gaudin Y. 2002. Characterization of the equilibrium between the native and fusion-inactive conformation of the rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology 297:128-135. http://dx.doi.org/10.1006/viro.2002.1429.
    • (2002) Virology , vol.297 , pp. 128-135
    • Roche, S.1    Gaudin, Y.2
  • 25
    • 2942702017 scopus 로고    scopus 로고
    • Influenza hemagglutinins outside of the contact zone are necessary for fusion pore expansion
    • Leikina E, Mittal A, Cho MS, Melikov K, Kozlov MM, Chernomordik LV. 2004. Influenza hemagglutinins outside of the contact zone are necessary for fusion pore expansion. J. Biol. Chem. 279:26526-26532. http://dx.doi.org/10.1074/jbc.M401883200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26526-26532
    • Leikina, E.1    Mittal, A.2    Cho, M.S.3    Melikov, K.4    Kozlov, M.M.5    Chernomordik, L.V.6
  • 26
    • 34247118403 scopus 로고    scopus 로고
    • Bitopic membrane topology of the stable signal peptide in the tripartite Junin virus GP-C envelope glycoprotein complex
    • Agnihothram SS, York J, Trahey M, Nunberg JH. 2007. Bitopic membrane topology of the stable signal peptide in the tripartite Junin virus GP-C envelope glycoprotein complex. J. Virol. 81:4331-4337. http://dx.doi.org/10.1128/JVI.02779-06.
    • (2007) J. Virol. , vol.81 , pp. 4331-4337
    • Agnihothram, S.S.1    York, J.2    Trahey, M.3    Nunberg, J.H.4
  • 27
    • 84863583991 scopus 로고    scopus 로고
    • Dissection of the role of the stable signal peptide of the arenavirus envelope glycoprotein in membrane fusion
    • Messina EL, York J, Nunberg JH. 2012. Dissection of the role of the stable signal peptide of the arenavirus envelope glycoprotein in membrane fusion. J. Virol. 86:6138-6145. http://dx.doi.org/10.1128/JVI.07241-11.
    • (2012) J. Virol. , vol.86 , pp. 6138-6145
    • Messina, E.L.1    York, J.2    Nunberg, J.H.3
  • 28
    • 33746377920 scopus 로고    scopus 로고
    • Role of the stable signal peptide of the Junin arenavirus envelope glycoprotein in pH-dependent membrane fusion
    • York J, Nunberg JH. 2006. Role of the stable signal peptide of the Junin arenavirus envelope glycoprotein in pH-dependent membrane fusion. J. Virol. 80:7775-7780. http://dx.doi.org/10.1128/JVI.00642-06.
    • (2006) J. Virol. , vol.80 , pp. 7775-7780
    • York, J.1    Nunberg, J.H.2
  • 29
    • 66149085621 scopus 로고    scopus 로고
    • Intersubunit interactions modulate the pH-induced activation of membrane fusion by the Junin virus envelope glycoprotein GPC
    • York J, Nunberg JH. 2009. Intersubunit interactions modulate the pH-induced activation of membrane fusion by the Junin virus envelope glycoprotein GPC. J. Virol. 83:4121-4126. http://dx.doi.org/10.1128/JVI.02410-08.
    • (2009) J. Virol. , vol.83 , pp. 4121-4126
    • York, J.1    Nunberg, J.H.2
  • 30
    • 79952295448 scopus 로고    scopus 로고
    • Synthetic protocells interact with viral nanomachinery and inactivate pathogenic human virus
    • e16874
    • Porotto M, Yi F, Moscona A, LaVan DA. 2011. Synthetic protocells interact with viral nanomachinery and inactivate pathogenic human virus. PLoS One 6:e16874. http://dx.doi.org/10.1371/journal.pone.0016874.
    • (2011) PLoS One , vol.6
    • Porotto, M.1    Yi, F.2    Moscona, A.3    LaVan, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.