메뉴 건너뛰기




Volumn 9, Issue 12, 2013, Pages 1-10

Tmprss2 Is Essential for Influenza H1N1 Virus Pathogenesis in Mice

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; SERINE PROTEINASE; TMPRSS2 PROTEIN, MOUSE;

EID: 84892860172     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003774     Document Type: Article
Times cited : (148)

References (39)
  • 1
    • 84857190187 scopus 로고    scopus 로고
    • Antiviral resistance during the 2009 influenza A H1N1 pandemic: public health, laboratory, and clinical perspectives
    • Hurt AC, Chotpitayasunondh T, Cox NJ, Daniels R, Fry AM, et al. (2012) Antiviral resistance during the 2009 influenza A H1N1 pandemic: public health, laboratory, and clinical perspectives. Lancet Infect Dis 12: 240-248.
    • (2012) Lancet Infect Dis , vol.12 , pp. 240-248
    • Hurt, A.C.1    Chotpitayasunondh, T.2    Cox, N.J.3    Daniels, R.4    Fry, A.M.5
  • 2
    • 0016679968 scopus 로고
    • Activation of influenza A viruses by trypsin treatment
    • Klenk HD, Rott R, Orlich M, Blodorn J, (1975) Activation of influenza A viruses by trypsin treatment. Virology 68: 426-439.
    • (1975) Virology , vol.68 , pp. 426-439
    • Klenk, H.D.1    Rott, R.2    Orlich, M.3    Blodorn, J.4
  • 3
    • 0016590407 scopus 로고
    • Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide
    • Lazarowitz SG, Choppin PW, (1975) Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology 68: 440-454.
    • (1975) Virology , vol.68 , pp. 440-454
    • Lazarowitz, S.G.1    Choppin, P.W.2
  • 4
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Grober A, Vey M, Angliker H, Shaw E, Thomas G, et al. (1992) Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J 11: 2407-2414.
    • (1992) EMBO J , vol.11 , pp. 2407-2414
    • Stieneke-Grober, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5
  • 5
    • 0026689352 scopus 로고
    • Isolation and characterization of a novel trypsin-like protease found in rat bronchiolar epithelial Clara cells. A possible activator of the viral fusion glycoprotein
    • Kido H, Yokogoshi Y, Sakai K, Tashiro M, Kishino Y, et al. (1992) Isolation and characterization of a novel trypsin-like protease found in rat bronchiolar epithelial Clara cells. A possible activator of the viral fusion glycoprotein. J Biol Chem 267: 13573-13579.
    • (1992) J Biol Chem , vol.267 , pp. 13573-13579
    • Kido, H.1    Yokogoshi, Y.2    Sakai, K.3    Tashiro, M.4    Kishino, Y.5
  • 6
    • 0034830879 scopus 로고    scopus 로고
    • Mini-plasmin found in the epithelial cells of bronchioles triggers infection by broad-spectrum influenza A viruses and Sendai virus
    • Murakami M, Towatari T, Ohuchi M, Shiota M, Akao M, et al. (2001) Mini-plasmin found in the epithelial cells of bronchioles triggers infection by broad-spectrum influenza A viruses and Sendai virus. Eur J Biochem 268: 2847-2855.
    • (2001) Eur J Biochem , vol.268 , pp. 2847-2855
    • Murakami, M.1    Towatari, T.2    Ohuchi, M.3    Shiota, M.4    Akao, M.5
  • 7
    • 77956639165 scopus 로고    scopus 로고
    • Novel insights into proteolytic cleavage of influenza virus hemagglutinin
    • Bertram S, Glowacka I, Steffen I, Kuhl A, Pohlmann S, (2010) Novel insights into proteolytic cleavage of influenza virus hemagglutinin. Rev Med Virol 20: 298-310.
    • (2010) Rev Med Virol , vol.20 , pp. 298-310
    • Bertram, S.1    Glowacka, I.2    Steffen, I.3    Kuhl, A.4    Pohlmann, S.5
  • 8
    • 0036337409 scopus 로고    scopus 로고
    • Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases
    • Zhirnov OP, Ikizler MR, Wright PF, (2002) Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases. J Virol 76: 8682-8689.
    • (2002) J Virol , vol.76 , pp. 8682-8689
    • Zhirnov, O.P.1    Ikizler, M.R.2    Wright, P.F.3
  • 9
    • 78951481964 scopus 로고    scopus 로고
    • Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2
    • Böttcher-Friebertshauser E, Stein DA, Klenk HD, Garten W, (2011) Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2. J Virol 85: 1554-1562.
    • (2011) J Virol , vol.85 , pp. 1554-1562
    • Böttcher-Friebertshauser, E.1    Stein, D.A.2    Klenk, H.D.3    Garten, W.4
  • 10
    • 77956869264 scopus 로고    scopus 로고
    • TMPRSS2 and TMPRSS4 facilitate trypsin-independent spread of influenza virus in Caco-2 cells
    • Bertram S, Glowacka I, Blazejewska P, Soilleux E, Allen P, et al. (2010) TMPRSS2 and TMPRSS4 facilitate trypsin-independent spread of influenza virus in Caco-2 cells. J Virol 84: 10016-10025.
    • (2010) J Virol , vol.84 , pp. 10016-10025
    • Bertram, S.1    Glowacka, I.2    Blazejewska, P.3    Soilleux, E.4    Allen, P.5
  • 11
    • 33748950305 scopus 로고    scopus 로고
    • Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
    • Böttcher E, Matrosovich T, Beyerle M, Klenk HD, Garten W, et al. (2006) Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J Virol 80: 9896-9898.
    • (2006) J Virol , vol.80 , pp. 9896-9898
    • Böttcher, E.1    Matrosovich, T.2    Beyerle, M.3    Klenk, H.D.4    Garten, W.5
  • 12
    • 77951023285 scopus 로고    scopus 로고
    • Characterization of lentiviral pseudotypes with influenza H5N1 hemagglutinin and their performance in neutralization assays
    • Wang W, Xie H, Ye Z, Vassell R, Weiss CD, (2010) Characterization of lentiviral pseudotypes with influenza H5N1 hemagglutinin and their performance in neutralization assays. J Virol Methods 165: 305-310.
    • (2010) J Virol Methods , vol.165 , pp. 305-310
    • Wang, W.1    Xie, H.2    Ye, Z.3    Vassell, R.4    Weiss, C.D.5
  • 13
    • 84860485820 scopus 로고    scopus 로고
    • Influenza and SARS-Coronavirus Activating Proteases TMPRSS2 and HAT Are Expressed at Multiple Sites in Human Respiratory and Gastrointestinal Tracts
    • Bertram S, Heurich A, Lavender H, Gierer S, Danisch S, et al. (2012) Influenza and SARS-Coronavirus Activating Proteases TMPRSS2 and HAT Are Expressed at Multiple Sites in Human Respiratory and Gastrointestinal Tracts. PLoS ONE 7: e35876.
    • (2012) PLoS ONE , vol.7
    • Bertram, S.1    Heurich, A.2    Lavender, H.3    Gierer, S.4    Danisch, S.5
  • 14
    • 31344447481 scopus 로고    scopus 로고
    • Phenotypic analysis of mice lacking the Tmprss2-encoded protease
    • Kim TS, Heinlein C, Hackman RC, Nelson PS, (2006) Phenotypic analysis of mice lacking the Tmprss2-encoded protease. Mol Cell Biol 26: 965-975.
    • (2006) Mol Cell Biol , vol.26 , pp. 965-975
    • Kim, T.S.1    Heinlein, C.2    Hackman, R.C.3    Nelson, P.S.4
  • 15
    • 79952537278 scopus 로고    scopus 로고
    • Pathogenicity of different PR8 influenza A virus variants in mice is determined by both viral and host factors
    • Blazejewska P, Koscinski L, Viegas N, Anhlan D, Ludwig S, et al. (2011) Pathogenicity of different PR8 influenza A virus variants in mice is determined by both viral and host factors. Virology 412: 36-45.
    • (2011) Virology , vol.412 , pp. 36-45
    • Blazejewska, P.1    Koscinski, L.2    Viegas, N.3    Anhlan, D.4    Ludwig, S.5
  • 16
    • 0018744652 scopus 로고
    • Natural, genetically determined resistance toward influenza virus in hemopoietic mouse chimeras. Role of mononuclear phagocytes
    • Haller O, Arnheiter H, Lindenmann J, (1979) Natural, genetically determined resistance toward influenza virus in hemopoietic mouse chimeras. Role of mononuclear phagocytes. J Exp Med 150: 117-126.
    • (1979) J Exp Med , vol.150 , pp. 117-126
    • Haller, O.1    Arnheiter, H.2    Lindenmann, J.3
  • 17
    • 63149086109 scopus 로고    scopus 로고
    • Proteolytic activation of the 1918 influenza virus hemagglutinin
    • Chaipan C, Kobasa D, Bertram S, Glowacka I, Steffen I, et al. (2009) Proteolytic activation of the 1918 influenza virus hemagglutinin. J Virol 83: 3200-3211.
    • (2009) J Virol , vol.83 , pp. 3200-3211
    • Chaipan, C.1    Kobasa, D.2    Bertram, S.3    Glowacka, I.4    Steffen, I.5
  • 18
    • 33947611615 scopus 로고    scopus 로고
    • Proteases essential for human influenza virus entry into cells and their inhibitors as potential therapeutic agents
    • Kido H, Okumura Y, Yamada H, Le TQ, Yano M, (2007) Proteases essential for human influenza virus entry into cells and their inhibitors as potential therapeutic agents. Curr Pharm Des 13: 405-414.
    • (2007) Curr Pharm Des , vol.13 , pp. 405-414
    • Kido, H.1    Okumura, Y.2    Yamada, H.3    Le, T.Q.4    Yano, M.5
  • 19
    • 0025151601 scopus 로고
    • An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo
    • Gotoh B, Ogasawara T, Toyoda T, Inocencio NM, Hamaguchi M, et al. (1990) An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo. EMBO J 9: 4189-4195.
    • (1990) EMBO J , vol.9 , pp. 4189-4195
    • Gotoh, B.1    Ogasawara, T.2    Toyoda, T.3    Inocencio, N.M.4    Hamaguchi, M.5
  • 20
    • 0026565988 scopus 로고
    • Isolation of factor Xa from chick embryo as the amniotic endoprotease responsible for paramyxovirus activation
    • Gotoh B, Yamauchi F, Ogasawara T, Nagai Y, (1992) Isolation of factor Xa from chick embryo as the amniotic endoprotease responsible for paramyxovirus activation. FEBS Lett 296: 274-278.
    • (1992) FEBS Lett , vol.296 , pp. 274-278
    • Gotoh, B.1    Yamauchi, F.2    Ogasawara, T.3    Nagai, Y.4
  • 21
    • 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.
    • (2013) PLoS Pathog , vol.9
    • Galloway, S.E.1    Reed, M.L.2    Russell, C.J.3    Steinhauer, D.A.4
  • 22
    • 84868094018 scopus 로고    scopus 로고
    • Cleavage Activation of the Human-Adapted Influenza Virus Subtypes by Matriptase Reveals Both Subtype- and Strain-Specificity
    • Hamilton BS, Gludish DW, Whittaker GR, (2012) Cleavage Activation of the Human-Adapted Influenza Virus Subtypes by Matriptase Reveals Both Subtype- and Strain-Specificity. J Virol 86: 10579-86.
    • (2012) J Virol , vol.86 , pp. 10579-10586
    • Hamilton, B.S.1    Gludish, D.W.2    Whittaker, G.R.3
  • 23
    • 84879065012 scopus 로고    scopus 로고
    • Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12
    • Hamilton BS, Whittaker GR, (2013) Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12. J Biol Chem 288: 17399-17407.
    • (2013) J Biol Chem , vol.288 , pp. 17399-17407
    • Hamilton, B.S.1    Whittaker, G.R.2
  • 24
    • 80052847571 scopus 로고    scopus 로고
    • Aprotinin and similar protease inhibitors as drugs against influenza
    • Zhirnov OP, Klenk HD, Wright PF, (2011) Aprotinin and similar protease inhibitors as drugs against influenza. Antiviral Res 92: 27-36.
    • (2011) Antiviral Res , vol.92 , pp. 27-36
    • Zhirnov, O.P.1    Klenk, H.D.2    Wright, P.F.3
  • 25
    • 78651583374 scopus 로고    scopus 로고
    • Inhibition of lung serine proteases in mice: a potentially new approach to control influenza infection
    • Bahgat MM, Blazejewska P, Schughart K, (2011) Inhibition of lung serine proteases in mice: a potentially new approach to control influenza infection. Virol J 8: 27.
    • (2011) Virol J , vol.8 , pp. 27
    • Bahgat, M.M.1    Blazejewska, P.2    Schughart, K.3
  • 26
    • 0021336866 scopus 로고
    • Suppression of influenza virus replication in infected mice by protease inhibitors
    • Zhirnov OP, Ovcharenko AV, Bukrinskaya AG, (1984) Suppression of influenza virus replication in infected mice by protease inhibitors. J Gen Virol 65 (Pt 1):: 191-196.
    • (1984) J Gen Virol , vol.65 , Issue.Pt 1 , pp. 191-196
    • Zhirnov, O.P.1    Ovcharenko, A.V.2    Bukrinskaya, A.G.3
  • 27
    • 0023106232 scopus 로고
    • High protection of animals lethally infected with influenza virus by aprotinin-rimantadine combination
    • Zhirnov OP, (1987) High protection of animals lethally infected with influenza virus by aprotinin-rimantadine combination. J Med Virol 21: 161-167.
    • (1987) J Med Virol , vol.21 , pp. 161-167
    • Zhirnov, O.P.1
  • 28
    • 0027979897 scopus 로고
    • Aprotinin aerosol treatment of influenza and paramyxovirus bronchopneumonia of mice
    • Ovcharenko AV, Zhirnov OP, (1994) Aprotinin aerosol treatment of influenza and paramyxovirus bronchopneumonia of mice. Antiviral Res 23: 107-118.
    • (1994) Antiviral Res , vol.23 , pp. 107-118
    • Ovcharenko, A.V.1    Zhirnov, O.P.2
  • 29
    • 50149096147 scopus 로고    scopus 로고
    • Efficient multiplication of human metapneumovirus in Vero cells expressing the transmembrane serine protease TMPRSS2
    • Shirogane Y, Takeda M, Iwasaki M, Ishiguro N, Takeuchi H, et al. (2008) Efficient multiplication of human metapneumovirus in Vero cells expressing the transmembrane serine protease TMPRSS2. J Virol 82: 8942-8946.
    • (2008) J Virol , vol.82 , pp. 8942-8946
    • Shirogane, Y.1    Takeda, M.2    Iwasaki, M.3    Ishiguro, N.4    Takeuchi, H.5
  • 30
    • 84877339392 scopus 로고    scopus 로고
    • The spike protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, can be activated by TMPRSS2, and is targeted by neutralizing antibodies
    • Gierer S, Bertram S, Kaup F, Wrensch F, Heurich A, et al. (2013) The spike protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, can be activated by TMPRSS2, and is targeted by neutralizing antibodies. J Virol 87: 5502-5511.
    • (2013) J Virol , vol.87 , pp. 5502-5511
    • Gierer, S.1    Bertram, S.2    Kaup, F.3    Wrensch, F.4    Heurich, A.5
  • 31
    • 84887169848 scopus 로고    scopus 로고
    • Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Infection Mediated by the Transmembrane Serine Protease TMPRSS2
    • doi:10.1128/JVI.01890-13
    • Shirato K, Kawase M, Matsuyama S, (2013) Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Infection Mediated by the Transmembrane Serine Protease TMPRSS2. J Virol doi: 10.1128/JVI.01890-13.
    • (2013) J Virol
    • Shirato, K.1    Kawase, M.2    Matsuyama, S.3
  • 32
    • 79954628266 scopus 로고    scopus 로고
    • Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response
    • Glowacka I, Bertram S, Muller MA, Allen P, Soilleux E, et al. (2011) Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J Virol 85: 4122-4134.
    • (2011) J Virol , vol.85 , pp. 4122-4134
    • Glowacka, I.1    Bertram, S.2    Muller, M.A.3    Allen, P.4    Soilleux, E.5
  • 33
    • 78650652994 scopus 로고    scopus 로고
    • A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry
    • Shulla A, Heald-Sargent T, Subramanya G, Zhao J, Perlman S, et al. (2011) A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry. J Virol 85: 873-882.
    • (2011) J Virol , vol.85 , pp. 873-882
    • Shulla, A.1    Heald-Sargent, T.2    Subramanya, G.3    Zhao, J.4    Perlman, S.5
  • 34
    • 78649407547 scopus 로고    scopus 로고
    • Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2
    • Matsuyama S, Nagata N, Shirato K, Kawase M, Takeda M, et al. (2010) Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J Virol 84: 12658-12664.
    • (2010) J Virol , vol.84 , pp. 12658-12664
    • Matsuyama, S.1    Nagata, N.2    Shirato, K.3    Kawase, M.4    Takeda, M.5
  • 35
    • 29444438899 scopus 로고    scopus 로고
    • The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host
    • Gabriel G, Dauber B, Wolff T, Planz O, Klenk HD, et al. (2005) The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host. Proc Natl Acad Sci U S A 102: 18590-18595.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18590-18595
    • Gabriel, G.1    Dauber, B.2    Wolff, T.3    Planz, O.4    Klenk, H.D.5
  • 36
    • 0033945532 scopus 로고    scopus 로고
    • Characterization of the Influenza a Virus Gene Pool in Avian Species in Southern China: Was H6N1 a Derivative or a Precursor of H5N1?
    • Hoffmann E, Stech J, Leneva I, Krauss S, Scholtissek C, et al. (2000) Characterization of the Influenza a Virus Gene Pool in Avian Species in Southern China: Was H6N1 a Derivative or a Precursor of H5N1? Journal of Virology 74: 6309-6315.
    • (2000) Journal of Virology , vol.74 , pp. 6309-6315
    • Hoffmann, E.1    Stech, J.2    Leneva, I.3    Krauss, S.4    Scholtissek, C.5
  • 37
    • 84869487923 scopus 로고    scopus 로고
    • The mouse as model system to study host-pathogen interactions in influenza A infections
    • Wilk E, Schughart K, (2012) The mouse as model system to study host-pathogen interactions in influenza A infections. Curr Protoc Mouse Biol 2: 177-205.
    • (2012) Curr Protoc Mouse Biol , vol.2 , pp. 177-205
    • Wilk, E.1    Schughart, K.2
  • 38
    • 34249857885 scopus 로고    scopus 로고
    • Replication fitness determines high virulence of influenza A virus in mice carrying functional Mx1 resistance gene
    • Grimm D, Staeheli P, Hufbauer M, Koerner I, Martínez-Sobrido L, et al. (2007) Replication fitness determines high virulence of influenza A virus in mice carrying functional Mx1 resistance gene. PNAS 104: 6806-6811.
    • (2007) PNAS , vol.104 , pp. 6806-6811
    • Grimm, D.1    Staeheli, P.2    Hufbauer, M.3    Koerner, I.4    Martínez-Sobrido, L.5
  • 39
    • 84870244269 scopus 로고    scopus 로고
    • Characterization of the neuraminidase of the H1N1/09 pandemic influenza virus
    • Gerlach T, Kuhling L, Uhlendorff J, Laukemper V, Matrosovich T, et al. (2012) Characterization of the neuraminidase of the H1N1/09 pandemic influenza virus. Vaccine 30: 7348-52.
    • (2012) Vaccine , vol.30 , pp. 7348-7352
    • Gerlach, T.1    Kuhling, L.2    Uhlendorff, J.3    Laukemper, V.4    Matrosovich, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.