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Volumn 90, Issue 22, 2016, Pages 10329-10338

Role of LAMP1 binding and pH sensing by the spike complex of Lassa virus

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; VIRUS SPIKE PROTEIN; DYSTROGLYCAN; PROTEIN BINDING; VIRUS ENVELOPE PROTEIN; VIRUS RECEPTOR;

EID: 84995480446     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01624-16     Document Type: Article
Times cited : (62)

References (30)
  • 1
    • 0036371866 scopus 로고    scopus 로고
    • Arenaviruses. I. The epidemiology molecular and cell biology of arenaviruses. Introduction
    • Oldstone MB. 2002. Arenaviruses. I. The epidemiology molecular and cell biology of arenaviruses. Introduction. Curr Top Microbiol Immunol 262: V-XII.
    • (2002) Curr Top Microbiol Immunol , vol.262 , pp. V-XII
    • Oldstone, M.B.1
  • 2
    • 0036188676 scopus 로고    scopus 로고
    • Arenaviruses. II. The molecular pathogenesis of arenavirus infections. Introduction
    • Oldstone MB. 2002. Arenaviruses. II. The molecular pathogenesis of arenavirus infections. Introduction. Curr Top Microbiol Immunol 263:V-XII.
    • (2002) Curr Top Microbiol Immunol , vol.263 , pp. V-XII
    • Oldstone, M.B.1
  • 4
    • 18144366555 scopus 로고    scopus 로고
    • Characterization of the interaction of Lassa fever virus with its cellular receptor alpha-dystroglycan
    • Kunz S, Rojek JM, Perez M, Spiropoulou CF, Oldstone MB. 2005. Characterization of the interaction of Lassa fever virus with its cellular receptor alpha-dystroglycan. J Virol 79:5979-5987. http://dx.doi.org/10.1128/JVI.79.10.5979-5987.2005.
    • (2005) J Virol , vol.79 , pp. 5979-5987
    • Kunz, S.1    Rojek, J.M.2    Perez, M.3    Spiropoulou, C.F.4    Oldstone, M.B.5
  • 5
    • 33744935523 scopus 로고    scopus 로고
    • Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins
    • Eschli B, Quirin K, Wepf A, Weber J, Zinkernagel R, Hengartner H. 2006. Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral 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.5    Hengartner, H.6
  • 7
    • 84977597990 scopus 로고    scopus 로고
    • Lassa virus cell entry via dystroglycan involves an unusual pathway of macropinocytosis
    • Oppliger J, Torriani G, Herrador A, Kunz S. 2016. Lassa virus cell entry via dystroglycan involves an unusual pathway of macropinocytosis. J Virol 90:6412-6429. http://dx.doi.org/10.1128/JVI.00257-16.
    • (2016) J Virol , vol.90 , pp. 6412-6429
    • Oppliger, J.1    Torriani, G.2    Herrador, A.3    Kunz, S.4
  • 8
    • 80053437934 scopus 로고    scopus 로고
    • Old World arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport
    • Pasqual G, Rojek JM, Masin M, Chatton JY, Kunz S. 2011. Old World arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport. PLoS Pathog 7:e1002232. http://dx.doi.org/10.1371/journal.ppat.1002232.
    • (2011) PLoS Pathog , vol.7
    • Pasqual, G.1    Rojek, J.M.2    Masin, M.3    Chatton, J.Y.4    Kunz, S.5
  • 9
    • 79960950908 scopus 로고    scopus 로고
    • Arenavirus envelope glycoproteins mimic autoprocessing sites of the cellular proprotein convertase subtilisin kexin isozyme-1/site-1 protease
    • Pasquato A, Burri DJ, Traba EG, Hanna-El-Daher L, Seidah NG, Kunz S. 2011. Arenavirus envelope glycoproteins mimic autoprocessing sites of the cellular proprotein convertase subtilisin kexin isozyme-1/site-1 protease. Virology 417:18-26. http://dx.doi.org/10.1016/j.virol.2011.04.021.
    • (2011) Virology , vol.417 , pp. 18-26
    • Pasquato, A.1    Burri, D.J.2    Traba, E.G.3    Hanna-El-Daher, L.4    Seidah, N.G.5    Kunz, S.6
  • 10
    • 84868116190 scopus 로고    scopus 로고
    • Envelope glycoprotein of arenaviruses
    • Burri DJ, da Palma JR, Kunz S, Pasquato A. 2012. Envelope glycoprotein of arenaviruses. Viruses 4:2162-2181. http://dx.doi.org/10.3390/v4102162.
    • (2012) Viruses , vol.4 , pp. 2162-2181
    • Burri, D.J.1    da Palma, J.R.2    Kunz, S.3    Pasquato, A.4
  • 12
    • 0034912179 scopus 로고    scopus 로고
    • Lysosomal membrane proteins
    • Winchester BG. 2001. Lysosomal membrane proteins. Eur J Paediatr Neurol 5(Suppl A):11-19. http://dx.doi.org/10.1053/ejpn.2000.0428.
    • (2001) Eur J Paediatr Neurol , vol.5 , pp. 11-19
    • Winchester, B.G.1
  • 13
    • 33749041268 scopus 로고    scopus 로고
    • Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy
    • Eskelinen EL. 2006. Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy. Mol Aspects Med 27:495-502. http://dx.doi.org/10.1016/j.mam.2006.08.005.
    • (2006) Mol Aspects Med , vol.27 , pp. 495-502
    • Eskelinen, E.L.1
  • 14
    • 0025165397 scopus 로고
    • Modulation of lysosomal-associated membrane glycoproteins during retinoic acid-induced embryonal carcinoma cell differentiation
    • Amos B, Lotan R. 1990. Modulation of lysosomal-associated membrane glycoproteins during retinoic acid-induced embryonal carcinoma cell differentiation. J Biol Chem 265:19192-19198.
    • (1990) J Biol Chem , vol.265 , pp. 19192-19198
    • Amos, B.1    Lotan, R.2
  • 15
    • 0023644927 scopus 로고
    • Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: kinetic and morphological analysis
    • Lippincott-Schwartz J, Fambrough DM. 1987. Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: kinetic and morphological analysis. Cell 49:669-677. http://dx.doi.org/10.1016/0092-8674(87)90543-5.
    • (1987) Cell , vol.49 , pp. 669-677
    • Lippincott-Schwartz, J.1    Fambrough, D.M.2
  • 16
    • 84937717339 scopus 로고    scopus 로고
    • Molecular mechanism for LAMP1 recognition by Lassa virus
    • Cohen-Dvashi H, Cohen N, Israeli H, Diskin R. 2015. Molecular mechanism for LAMP1 recognition by Lassa virus. J Virol 89:7584-7592. http://dx.doi.org/10.1128/JVI.00651-15.
    • (2015) J Virol , vol.89 , pp. 7584-7592
    • Cohen-Dvashi, H.1    Cohen, N.2    Israeli, H.3    Diskin, R.4
  • 17
    • 29244449301 scopus 로고    scopus 로고
    • Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3
    • Falcon-Perez JM, Nazarian R, Sabatti C, Dell'Angelica EC. 2005. Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3. J Cell Sci 118:5243-5255. http://dx.doi.org/10.1242/jcs.02633.
    • (2005) J Cell Sci , vol.118 , pp. 5243-5255
    • Falcon-Perez, J.M.1    Nazarian, R.2    Sabatti, C.3    Dell'Angelica, E.C.4
  • 18
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider CA, Rasband WS, Eliceiri KW. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9:671-675. http://dx.doi.org/10.1038/nmeth.2089.
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 19
    • 84857782898 scopus 로고    scopus 로고
    • Polyubiquitin-sensor proteins reveal localization and linkagetype dependence of cellular ubiquitin signaling
    • Sims JJ, Scavone F, Cooper EM, Kane LA, Youle RJ, Boeke JD, Cohen RE. 2012. Polyubiquitin-sensor proteins reveal localization and linkagetype dependence of cellular ubiquitin signaling. Nat Methods 9:303-309. http://dx.doi.org/10.1038/nmeth.1888.
    • (2012) Nat Methods , vol.9 , pp. 303-309
    • Sims, J.J.1    Scavone, F.2    Cooper, E.M.3    Kane, L.A.4    Youle, R.J.5    Boeke, J.D.6    Cohen, R.E.7
  • 20
    • 0031954296 scopus 로고    scopus 로고
    • Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines
    • Wool-Lewis RJ, Bates P. 1998. Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines. J Virol 72:3155-3160.
    • (1998) J Virol , vol.72 , pp. 3155-3160
    • Wool-Lewis, R.J.1    Bates, P.2
  • 21
    • 35848955673 scopus 로고    scopus 로고
    • Old World arenavirus infection interferes with the expression of functional alphadystroglycan in the host cell
    • Rojek JM, Campbell KP, Oldstone MB, Kunz S. 2007. Old World arenavirus infection interferes with the expression of functional alphadystroglycan in the host cell. Mol Biol Cell 18:4493-4507. http://dx.doi.org/10.1091/mbc.E07-04-0374.
    • (2007) Mol Biol Cell , vol.18 , pp. 4493-4507
    • Rojek, J.M.1    Campbell, K.P.2    Oldstone, M.B.3    Kunz, S.4
  • 22
    • 84857081598 scopus 로고    scopus 로고
    • Identification of cell surface molecules involved in dystroglycanindependent Lassa virus cell entry
    • Shimojima M, Stroher U, Ebihara H, Feldmann H, Kawaoka Y. 2012. Identification of cell surface molecules involved in dystroglycanindependent Lassa virus cell entry. J Virol 86:2067-2078. http://dx.doi.org/10.1128/JVI.06451-11.
    • (2012) J Virol , vol.86 , pp. 2067-2078
    • Shimojima, M.1    Stroher, U.2    Ebihara, H.3    Feldmann, H.4    Kawaoka, Y.5
  • 23
    • 34547585371 scopus 로고    scopus 로고
    • Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-2 are critical for pH-dependent membrane fusion and infectivity
    • Klewitz C, Klenk HD, ter Meulen J. 2007. Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-2 are critical for pH-dependent membrane fusion and infectivity. J Gen Virol 88:2320-2328. http://dx.doi.org/10.1099/vir.0.82950-0.
    • (2007) J Gen Virol , vol.88 , pp. 2320-2328
    • Klewitz, C.1    Klenk, H.D.2    ter Meulen, J.3
  • 25
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer J, Schweizer A, Russell D, Kornfeld S. 1996. The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J Cell Biol 132:565-576. http://dx.doi.org/10.1083/jcb.132.4.565.
    • (1996) J Cell Biol , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 27
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman I, Fuchs R, Helenius A. 1986. Acidification of the endocytic and exocytic pathways. Annu Rev Biochem 55:663-700. http://dx.doi.org/10.1146/annurev.bi.55.070186.003311.
    • (1986) Annu Rev Biochem , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 28
    • 67649405075 scopus 로고    scopus 로고
    • Protein ionizable groups: pK values and their contribution to protein stability and solubility
    • Pace CN, Grimsley GR, Scholtz JM. 2009. Protein ionizable groups: pK values and their contribution to protein stability and solubility. J Biol Chem 284:13285-13289. http://dx.doi.org/10.1074/jbc.R800080200.
    • (2009) J Biol Chem , vol.284 , pp. 13285-13289
    • Pace, C.N.1    Grimsley, G.R.2    Scholtz, J.M.3
  • 29
    • 66149085621 scopus 로고    scopus 로고
    • Intersubunit interactions modulate pHinduced activation of membrane fusion by the Junin virus envelope glycoprotein GPC
    • York J, Nunberg JH. 2009. Intersubunit interactions modulate pHinduced 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
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison SC. 2008. Viral membrane fusion. Nat Struct Mol Biol 15:690-698. http://dx.doi.org/10.1038/nsmb.1456.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 690-698
    • Harrison, S.C.1


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