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Volumn 6, Issue 3, 2015, Pages

Cathepsin W is required for escape of influenza A virus from late endosomes

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN W;

EID: 84936971212     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00297-15     Document Type: Article
Times cited : (34)

References (44)
  • 1
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Knipe DM, Howley (ed) Lippincott Williams & Wilkins, Philadelphia, PA
    • Palese P, Shaw ML. 2007. Orthomyxoviridae: the viruses and their replication, p 1647-1689. In Knipe DM, Howley (ed), Fields virology, vol 2, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology, vol 2, 5th ed , pp. 1647-1689
    • Palese, P.1    Shaw, M.L.2
  • 2
    • 0025620241 scopus 로고
    • Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity
    • Baum LG, Paulson JC. 1990. Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem Suppl 40:35-38.
    • (1990) Acta Histochem Suppl , vol.40 , pp. 35-38
    • Baum, L.G.1    Paulson, J.C.2
  • 3
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin KS, Reggio H, Helenius A, Simons K. 1981. Infectious entry pathway of influenza virus in a canine kidney cell line. J Cell Biol 91: 601-613. http://dx.doi.org/10.1083/jcb.91.3.601.
    • (1981) J Cell Biol , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 5
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski SB, Whittaker GR. 2002. Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J Virol 76: 10455-10464. http://dx.doi.org/10.1128/JVI.76.20.10455-10464.2002.
    • (2002) J Virol , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 6
    • 0041422345 scopus 로고    scopus 로고
    • Visualizing infection of individual influenza viruses
    • Lakadamyali M, Rust MJ, Babcock HP, Zhuang X. 2003. Visualizing infection of individual influenza viruses. Proc Natl Acad Sci U S A 100: 9280-9285. http://dx.doi.org/10.1073/pnas.0832269100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9280-9285
    • Lakadamyali, M.1    Rust, M.J.2    Babcock, H.P.3    Zhuang, X.4
  • 7
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. 1996. Endocytosis and molecular sorting. Annu Rev Cell Dev Biol 12:575-625. http://dx.doi.org/10.1146/annurev.cellbio.12.1.575.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 575-625
    • Mellman, I.1
  • 8
    • 0019203091 scopus 로고
    • Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes
    • Maeda T, Ohnishi S. 1980. Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes. FEBS Lett 122:283-287. http:// dx.doi.org/10.1016/0014-5793(80)80457-1.
    • (1980) FEBS Lett , vol.122 , pp. 283-287
    • Maeda, T.1    Ohnishi, S.2
  • 9
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, WileyDC. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69:531-569. http:// dx.doi.org/10.1146/annurev.biochem.69.1.531.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 10
    • 0142091712 scopus 로고    scopus 로고
    • Trafficking of viral genomic RNA into and out of the nucleus: Influenza, Thogoto and Borna disease viruses
    • Cros JF, Palese P. 2003. Trafficking of viral genomic RNA into and out of the nucleus: influenza, Thogoto and Borna disease viruses. Virus Res 95: 3-12. http://dx.doi.org/10.1016/S0168-1702(03)00159-X.
    • (2003) Virus Res , vol.95 , pp. 3-12
    • Cros, J.F.1    Palese, P.2
  • 11
    • 0026070664 scopus 로고
    • Transport of incoming influenza virus nucleocapsids into the nucleus
    • Martin K, Helenius A. 1991. Transport of incoming influenza virus nucleocapsids into the nucleus. J Virol 65:232-244. http://dx.doi.org/ 10.1016/0962-8924(92)90130-F.
    • (1991) J Virol , vol.65 , pp. 232-244
    • Martin, K.1    Helenius, A.2
  • 12
    • 84892608409 scopus 로고    scopus 로고
    • Entry of influenza A virus: Host factors and antiviral targets
    • Edinger TO, Pohl MO, Stertz S. 2014. Entry of influenza A virus: host factors and antiviral targets. J Gen Virol 95:263-277. http://dx.doi.org/ 10.1099/vir.0.059477-0.
    • (2014) J Gen Virol , vol.95 , pp. 263-277
    • Edinger, T.O.1    Pohl, M.O.2    Stertz, S.3
  • 13
    • 67249156976 scopus 로고    scopus 로고
    • Targeting cell signalling pathways to fight the flu: Towards a paradigm change in anti-influenza therapy
    • Ludwig S. 2009. Targeting cell signalling pathways to fight the flu: towards a paradigm change in anti-influenza therapy. J Antimicrob Chemother 64:1-4. http://dx.doi.org/10.1093/jac/dkp161.
    • (2009) J Antimicrob Chemother , vol.64 , pp. 1-4
    • Ludwig, S.1
  • 14
    • 84886389616 scopus 로고    scopus 로고
    • Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry
    • Su WC, Chen YC, Tseng CH, Hsu PW, Tung KF, Jeng KS, Lai MM. 2013. Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry. Proc Natl Acad Sci U S A 110:17516-17521. http://dx.doi.org/10.1073/ pnas.1312374110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 17516-17521
    • Su, W.C.1    Chen, Y.C.2    Tseng, C.H.3    Hsu, P.W.4    Tung, K.F.5    Jeng, K.S.6    Lai, M.M.7
  • 19
    • 55949117482 scopus 로고    scopus 로고
    • Cathepsins: Key modulators of cell death and inflammatory responses
    • Conus S, Simon HU. 2008. Cathepsins: key modulators of cell death and inflammatory responses. Biochem Pharmacol 76:1374-1382. http:// dx.doi.org/10.1016/j.bcp.2008.07.041.
    • (2008) Biochem Pharmacol , vol.76 , pp. 1374-1382
    • Conus, S.1    Simon, H.U.2
  • 20
    • 0033532532 scopus 로고    scopus 로고
    • Human cathepsins F and W: A new subgroup of cathepsins
    • Wex T, Levy B, Wex H, Brömme D. 1999. Human cathepsins F and W: a new subgroup of cathepsins. Biochem Biophys Res Commun 259: 401-407. http://dx.doi.org/10.1006/bbrc.1999.0700.
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 401-407
    • Wex, T.1    Levy, B.2    Wex, H.3    Brömme, D.4
  • 21
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM. 2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643-1645. http://dx.doi.org/10.1126/ science.1110656.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 22
  • 23
    • 84864018547 scopus 로고    scopus 로고
    • Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry
    • Kawase M, Shirato K, van der Hoek L, Taguchi F, Matsuyama S. 2012. Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry. J Virol 86:6537-6545. http://dx.doi.org/ 10.1128/JVI.00094-12.
    • (2012) J Virol , vol.86 , pp. 6537-6545
    • Kawase, M.1    Shirato, K.2    van der Hoek, L.3    Taguchi, F.4    Matsuyama, S.5
  • 24
    • 84861309290 scopus 로고    scopus 로고
    • Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment
    • Diederich S, Sauerhering L, Weis M, Altmeppen H, Schaschke N, Reinheckel T, Erbar S, Maisner A. 2012. Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment. J Virol 86:3736-3745. http:// dx.doi.org/10.1128/JVI.06628-11.
    • (2012) J Virol , vol.86 , pp. 3736-3745
    • Diederich, S.1    Sauerhering, L.2    Weis, M.3    Altmeppen, H.4    Schaschke, N.5    Reinheckel, T.6    Erbar, S.7    Maisner, A.8
  • 25
    • 0035881830 scopus 로고    scopus 로고
    • Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum
    • Wex T, Bühling F, Wex H, Günther D, Malfertheiner P, Weber E, Brömme D. 2001. Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum. J Immunol 167:2172-2178. http://dx.doi.org/10.4049/ jimmunol.167.4.2172.
    • (2001) J Immunol , vol.167 , pp. 2172-2178
    • Wex, T.1    Bühling, F.2    Wex, H.3    Günther, D.4    Malfertheiner, P.5    Weber, E.6    Brömme, D.7
  • 26
    • 3042595457 scopus 로고    scopus 로고
    • Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity
    • Ondr JK, Pham CT. 2004. Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity. J Biol Chem 279:27525-27533. http://dx.doi.org/10.1074/jbc.M400304200.
    • (2004) J Biol Chem , vol.279 , pp. 27525-27533
    • Ondr, J.K.1    Pham, C.T.2
  • 27
    • 84874738791 scopus 로고    scopus 로고
    • Dissecting the role of COPI complexes in influenza virus infection
    • Sun E, He J, Zhuang X. 2013. Dissecting the role of COPI complexes in influenza virus infection. J Virol 87:2673-2685. http://dx.doi.org/ 10.1128/JVI.02277-12.
    • (2013) J Virol , vol.87 , pp. 2673-2685
    • Sun, E.1    He, J.2    Zhuang, X.3
  • 28
    • 0032551750 scopus 로고    scopus 로고
    • Genomic structure, chromosomal localization, and expression of human cathepsin W
    • Wex T, Levy B, Smeekens SP, Ansorge S, Desnick RJ, Bromme D. 1998. Genomic structure, chromosomal localization, and expression of human cathepsin W. Biochem Biophys Res Commun 248:255-261. http:// dx.doi.org/10.1006/bbrc.1998.8954.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 255-261
    • Wex, T.1    Levy, B.2    Smeekens, S.P.3    Ansorge, S.4    Desnick, R.J.5    Bromme, D.6
  • 29
    • 0035881830 scopus 로고    scopus 로고
    • Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum
    • Wex T, Bühling F, Wex H, Günther D, Malfertheiner P, Weber E, Brömme D. 2001. Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum. J Immunol 167:2172-2178. http://dx.doi.org/10.4049/ jimmunol.167.4.2172.
    • (2001) J Immunol , vol.167 , pp. 2172-2178
    • Wex, T.1    Bühling, F.2    Wex, H.3    Günther, D.4    Malfertheiner, P.5    Weber, E.6    Brömme, D.7
  • 30
    • 84874761652 scopus 로고    scopus 로고
    • Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: Implications for host range and adaptation
    • Galloway SE, Reed ML, Russell CJ, Steinhauer DA. 2013. Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation. PLoS Pathog 9:e1003151. http://dx.doi.org/10.1371/journal.ppat.1003151.
    • (2013) PLoS Pathog , vol.9
    • Galloway, S.E.1    Reed, M.L.2    Russell, C.J.3    Steinhauer, D.A.4
  • 31
    • 40749124935 scopus 로고    scopus 로고
    • Cell entry by human pathogenic arenaviruses
    • Rojek JM, Kunz S. 2008. Cell entry by human pathogenic arenaviruses. Cell Microbiol 10:828-835. http://dx.doi.org/10.1111/j.1462-5822.2007.01113.x.
    • (2008) Cell Microbiol , vol.10 , pp. 828-835
    • Rojek, J.M.1    Kunz, S.2
  • 32
    • 33644822934 scopus 로고    scopus 로고
    • A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
    • Pager CT, Craft WW, Jr, Patch J, Dutch RE. 2006. A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346:251-257. http://dx.doi.org/10.1016/ j.virol.2006.01.007.
    • (2006) Virology , vol.346 , pp. 251-257
    • Pager, C.T.1    Craft, W.W.2    Patch, J.3    Dutch, R.E.4
  • 33
    • 26444552119 scopus 로고    scopus 로고
    • Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein
    • Pager CT, Dutch RE. 2005. Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J Virol 79:12714-12720. http:// dx.doi.org/10.1128/JVI.79.20.12714-12720.2005.
    • (2005) J Virol , vol.79 , pp. 12714-12720
    • Pager, C.T.1    Dutch, R.E.2
  • 34
    • 79953288103 scopus 로고    scopus 로고
    • Uncovering the global host cell requirements for influenza virus replication via RNAi screening
    • Stertz S, Shaw ML. 2011. Uncovering the global host cell requirements for influenza virus replication via RNAi screening. Microbes Infect 13: 516-525. http://dx.doi.org/10.1016/j.micinf.2011.01.012.
    • (2011) Microbes Infect , vol.13 , pp. 516-525
    • Stertz, S.1    Shaw, M.L.2
  • 36
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White JM, Wilson IA. 1987. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J Cell Biol 105:2887-2896. http://dx.doi.org/10.1083/ jcb.105.6.2887.
    • (1987) J Cell Biol , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 37
    • 84887312278 scopus 로고    scopus 로고
    • Dual function of CD81 in influenza virus uncoating and budding
    • He J, Sun E, Bujny MV, Kim D, Davidson MW, Zhuang X. 2013. Dual function of CD81 in influenza virus uncoating and budding. PLoS Pathog 9:e1003701. http://dx.doi.org/10.1371/journal.ppat.1003701.
    • (2013) PLoS Pathog , vol.9
    • He, J.1    Sun, E.2    Bujny, M.V.3    Kim, D.4    Davidson, M.W.5    Zhuang, X.6
  • 38
    • 84896381325 scopus 로고    scopus 로고
    • A review of reagents for fluorescence microscopy of cellular compartments and structures, part I: BacMam labeling and reagents for vesicular structures
    • Unit 12.30
    • Dolman NJ, Kilgore JA, Davidson MW. 2013. A review of reagents for fluorescence microscopy of cellular compartments and structures, part I: BacMam labeling and reagents for vesicular structures. Curr Protoc Cytom Chapter 12:Unit 12.30. http://dx.doi.org/10.1002/ 0471142956.cy1230s65.
    • (2013) Curr Protoc Cytom Chapter , vol.12
    • Dolman, N.J.1    Kilgore, J.A.2    Davidson, M.W.3
  • 39
    • 84924272105 scopus 로고    scopus 로고
    • Cathepsins: Fundamental effectors of endolysosomal proteolysis
    • Guha S, Padh H. 2008. Cathepsins: fundamental effectors of endolysosomal proteolysis. Indian J Biochem Biophys 45:-75-90.
    • (2008) Indian J Biochem Biophys , vol.45 , pp. -75-90
    • Guha, S.1    Padh, H.2
  • 40
    • 0036566039 scopus 로고    scopus 로고
    • Endolysosomal proteolysis and its regulation
    • Pillay CS, Elliott E, Dennison C. 2002. Endolysosomal proteolysis and its regulation. Biochem J 363:417-429. http://dx.doi.org/10.1042/0264-6021:3630417.
    • (2002) Biochem J , vol.363 , pp. 417-429
    • Pillay, C.S.1    Elliott, E.2    Dennison, C.3
  • 41
    • 0021875433 scopus 로고
    • Characterization of host cell binding variants of influenza virus by monoclonal antibodies
    • Nohinek B, Gerhard W, Schulze IT. 1985. Characterization of host cell binding variants of influenza virus by monoclonal antibodies. Virology 143:651-656. http://dx.doi.org/10.1016/0042-6822(85)90407-6.
    • (1985) Virology , vol.143 , pp. 651-656
    • Nohinek, B.1    Gerhard, W.2    Schulze, I.T.3
  • 42
    • 84906979425 scopus 로고    scopus 로고
    • Prolidase is required for early trafficking events during influenza A virus entry
    • Pohl MO, Edinger TO, Stertz S. 2014. Prolidase is required for early trafficking events during influenza A virus entry. J Virol 88:11271-11283. http://dx.doi.org/10.1128/JVI.00800-14.
    • (2014) J Virol , vol.88 , pp. 11271-11283
    • Pohl, M.O.1    Edinger, T.O.2    Stertz, S.3
  • 43
    • 32444439017 scopus 로고    scopus 로고
    • Dual wavelength imaging allows analysis of membrane fusion of influenza virus inside cells
    • Sakai T, Ohuchi M, Imai M, Mizuno T, Kawasaki K, Kuroda K, Yamashina S. 2006. Dual wavelength imaging allows analysis of membrane fusion of influenza virus inside cells. J Virol 80:2013-2018. http:// dx.doi.org/10.1128/JVI.80.4.2013-2018.2006.
    • (2006) J Virol , vol.80 , pp. 2013-2018
    • Sakai, T.1    Ohuchi, M.2    Imai, M.3    Mizuno, T.4    Kawasaki, K.5    Kuroda, K.6    Yamashina, S.7
  • 44
    • 84880076973 scopus 로고    scopus 로고
    • High-content analysis of sequential events during the early phase of influenza A virus infection
    • Banerjee I, Yamauchi Y, Helenius A, Horvath P. 2013. High-content analysis of sequential events during the early phase of influenza A virus infection. PLoS One 8:e68450. http://dx.doi.org/10.1371/ journal.pone.0068450.
    • (2013) PLoS One , vol.8
    • Banerjee, I.1    Yamauchi, Y.2    Helenius, A.3    Horvath, P.4


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