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Volumn 86, Issue 21, 2012, Pages 11745-11753

Monitoring of s protein maturation in the endoplasmic reticulum by calnexin is important for the infectivity of severe acute respiratory syndrome coronavirus

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; SMALL INTERFERING RNA; VITRONECTIN;

EID: 84869050218     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01250-12     Document Type: Article
Times cited : (71)

References (49)
  • 1
    • 0032573391 scopus 로고    scopus 로고
    • Enhanced secretion of hydrophobic peptide fused lysozyme by the introduction of N-glycosylation signal and the disruption of calnexin gene in Saccharomyces cerevisiae
    • Arima H, Kinoshita T, Ibrahim HR, Azakami H, Kato A. 1998. Enhanced secretion of hydrophobic peptide fused lysozyme by the introduction of N-glycosylation signal and the disruption of calnexin gene in Saccharomyces cerevisiae. FEBS Lett. 440:89-92
    • (1998) FEBS Lett , vol.440 , pp. 89-92
    • Arima, H.1    Kinoshita, T.2    Ibrahim, H.R.3    Azakami, H.4    Kato, A.5
  • 2
    • 23944438373 scopus 로고    scopus 로고
    • Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57
    • Bedard K, Szabo E, Michalak M, Opas M. 2005. Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int.Rev. Cytol. 245:91-121
    • (2005) Int.Rev. Cytol , vol.245 , pp. 91-121
    • Bedard, K.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 3
    • 10444237158 scopus 로고    scopus 로고
    • Implication of proprotein convertases in the processing and spread of severe acute respiratory syndrome coronavirus
    • Bergeron E, et al. 2005. Implication of proprotein convertases in the processing and spread of severe acute respiratory syndrome coronavirus.Biochem. Biophys. Res. Commun. 326:554-563
    • (2005) Biochem. Biophys. Res. Commun , vol.326 , pp. 554-563
    • Bergeron, E.1
  • 4
    • 2942741241 scopus 로고    scopus 로고
    • Influence of N-linked glycans on intracellular transport of hepatitis C virus E1 chimeric glycoprotein and its role in pseudotype virus infectivity
    • Beyene A, Basu A, Meyer K, Ray R. 2004. Influence of N-linked glycans on intracellular transport of hepatitis C virus E1 chimeric glycoprotein and its role in pseudotype virus infectivity. Virology 324:273-285
    • (2004) Virology , vol.324 , pp. 273-285
    • Beyene, A.1    Basu, A.2    Meyer, K.3    Ray, R.4
  • 6
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo JJ, Parodi AJ. 2008. Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 283:10221-10225
    • (2008) J. Biol. Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 7
    • 33645550893 scopus 로고    scopus 로고
    • Antiviral effect of alpha-glucosidase inhibitors on viral morphogenesis and binding properties of hepatitis C virus-like particles
    • Chapel C, et al. 2006. Antiviral effect of alpha-glucosidase inhibitors on viral morphogenesis and binding properties of hepatitis C virus-like particles.J. Gen. Virol. 87:861- 871
    • (2006) J. Gen. Virol , vol.87 , pp. 861-871
    • Chapel, C.1
  • 8
    • 34247842741 scopus 로고    scopus 로고
    • The immunobiology of SARS
    • Chen J, Subbarao K. 2007. The immunobiology of SARS. Annu. Rev.Immunol. 25:443-472
    • (2007) Annu. Rev.Immunol , vol.25 , pp. 443-472
    • Chen, J.1    Subbarao, K.2
  • 9
    • 11144239774 scopus 로고    scopus 로고
    • Influenza virus entry and infection require host cell N-linked glycoprotein
    • Chu VC, Whittaker GR. 2004. Influenza virus entry and infection require host cell N-linked glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 101:18153-18158
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 18153-18158
    • Chu, V.C.1    Whittaker, G.R.2
  • 10
    • 0036838084 scopus 로고    scopus 로고
    • Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression
    • Denzel A, et al. 2002. Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression. Mol. Cell. Biol. 22:7398-7404
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7398-7404
    • Denzel, A.1
  • 11
    • 0038523806 scopus 로고    scopus 로고
    • Identification of a novel coronavirus in patients with severe acute respiratory syndrome
    • Drosten C, et al. 2003. Identification of a novel coronavirus in patients with severe acute respiratory syndrome. N. Engl. J. Med. 348:1967-1976
    • (2003) N. Engl. J. Med , vol.348 , pp. 1967-1976
    • Drosten, C.1
  • 13
    • 0344080741 scopus 로고    scopus 로고
    • Phylogeny of the SARS coronavirus
    • Eickmann M, et al. 2003. Phylogeny of the SARS coronavirus. Science 302:1504-1505
    • (2003) Science , vol.302 , pp. 1504-1505
    • Eickmann, M.1
  • 14
    • 33745282653 scopus 로고    scopus 로고
    • Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry
    • Follis KE, York J, Nunberg JH. 2006. Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry. Virology 350:358-369
    • (2006) Virology , vol.350 , pp. 358-369
    • Follis, K.E.1    York, J.2    Nunberg, J.H.3
  • 15
    • 45549097784 scopus 로고    scopus 로고
    • Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry
    • Haga S, et al. 2008. Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry. Proc. Natl. Acad. Sci. U.S.A. 105:7809-7814
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7809-7814
    • Haga, S.1
  • 16
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway:retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond C, Helenius A. 1994. Quality control in the secretory pathway:retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126:41-52
    • (1994) J. Cell Biol , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 17
    • 35448944884 scopus 로고    scopus 로고
    • Specific asparagine-linked glycosylation sites are critical for DC-SIGN-and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry
    • Han DP, Lohani M, Cho MW. 2007. Specific asparagine-linked glycosylation sites are critical for DC-SIGN-and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry. J. Virol. 81:12029-12039
    • (2007) J. Virol , vol.81 , pp. 12029-12039
    • Han, D.P.1    Lohani, M.2    Cho, M.W.3
  • 18
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding,quality control, degradation, and related human diseases
    • Hebert DN, Molinari M. 2007. In and out of the ER: protein folding,quality control, degradation, and related human diseases. Physiol. Rev.87:1377-1408
    • (2007) Physiol. Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 19
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5:253-265
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 20
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M. 2004. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73:1019-1049
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 21
    • 0036241369 scopus 로고    scopus 로고
    • Production of human monoclonal and polyclonal antibodies in TransChromo animals
    • Ishida I, et al. 2002. Production of human monoclonal and polyclonal antibodies in TransChromo animals. Cloning Stem Cells 4:91-102
    • (2002) Cloning Stem Cells , vol.4 , pp. 91-102
    • Ishida, I.1
  • 22
    • 8144221600 scopus 로고    scopus 로고
    • CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus
    • Jeffers SA, et al. 2004. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. Proc. Natl. Acad. Sci. U.S.A. 101:15748-15753
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15748-15753
    • Jeffers, S.A.1
  • 23
    • 0038076030 scopus 로고    scopus 로고
    • A novel coronavirus associated with severe acute respiratory syndrome
    • Ksiazek TG, et al. 2003. A novel coronavirus associated with severe acute respiratory syndrome. N. Engl. J. Med. 348:1953-1966
    • (2003) N. Engl. J. Med , vol.348 , pp. 1953-1966
    • Ksiazek, T.G.1
  • 24
    • 23844463115 scopus 로고    scopus 로고
    • A crucial role of angiotensin converting enzyme 2(ACE2) in SARS coronavirus-induced lung injury
    • Kuba K, et al. 2005. A crucial role of angiotensin converting enzyme 2(ACE2) in SARS coronavirus-induced lung injury. Nat. Med. 11:875-879
    • (2005) Nat. Med , vol.11 , pp. 875-879
    • Kuba, K.1
  • 25
    • 84859434125 scopus 로고    scopus 로고
    • Palmitoylated calnexin is a key component of the ribosome-translocon complex
    • Lakkaraju AK, et al. 2012. Palmitoylated calnexin is a key component of the ribosome-translocon complex. EMBO J. 31:1823-1835
    • (2012) EMBO J. , vol.31 , pp. 1823-1835
    • Lakkaraju, A.K.1
  • 26
    • 24944498409 scopus 로고    scopus 로고
    • Structure of SARS coronavirus spike receptor-binding domain complexed with receptor
    • Li F, Li W, Farzan M, Harrison SC. 2005. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 309:1864-1868
    • (2005) Science , vol.309 , pp. 1864-1868
    • Li, F.1    Li, W.2    Farzan, M.3    Harrison, S.C.4
  • 27
    • 0344395657 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
    • Li W, et al. 2003. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426:450-454
    • (2003) Nature , vol.426 , pp. 450-454
    • Li, W.1
  • 28
    • 12144287276 scopus 로고    scopus 로고
    • Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors
    • Liu S, et al. 2004. Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. Lancet 363:938-947
    • (2004) Lancet , vol.363 , pp. 938-947
    • Liu, S.1
  • 29
    • 77956856952 scopus 로고    scopus 로고
    • Role of N-linked glycosylation of the 5-HT2A receptor in JC virus infection
    • Maginnis MS, Haley SA, Gee GV, Atwood WJ. 2010. Role of N-linked glycosylation of the 5-HT2A receptor in JC virus infection. J. Virol. 84:9677-9684
    • (2010) J.Virol , vol.84 , pp. 9677-9684
    • Maginnis, M.S.1    Haley, S.A.2    Gee, G.V.3    Atwood, W.J.4
  • 30
    • 0038823524 scopus 로고    scopus 로고
    • The Genome sequence of the SARS-associated coronavirus
    • Marra MA, et al. 2003. The Genome sequence of the SARS-associated coronavirus. Science 300:1399-1404
    • (2003) Science , vol.300 , pp. 1399-1404
    • Marra, M.A.1
  • 31
    • 0032560488 scopus 로고    scopus 로고
    • Alphaglucosidase inhibitors as potential broad based anti-viral agents
    • Mehta A, Zitzmann N, Rudd PM, Block TM, Dwek RA. 1998. Alphaglucosidase inhibitors as potential broad based anti-viral agents. FEBS Lett. 430:17-22
    • (1998) FEBS Lett , vol.430 , pp. 17-22
    • Mehta, A.1    Zitzmann, N.2    Rudd, P.M.3    Block, T.M.4    Dwek, R.A.5
  • 32
    • 79956227227 scopus 로고    scopus 로고
    • Fully human monoclonal antibody directed to proteolytic cleavage site in severe acute respiratory syndrome (SARS) coronavirus S protein neutralizes the virus in a rhesus macaque SARS model
    • Miyoshi-Akiyama T, et al. 2011. Fully human monoclonal antibody directed to proteolytic cleavage site in severe acute respiratory syndrome (SARS) coronavirus S protein neutralizes the virus in a rhesus macaque SARS model. J. Infect. Dis. 203:1574-1581
    • (2011) J.Infect.Dis , vol.203 , pp. 1574-1581
    • Miyoshi-Akiyama, T.1
  • 33
    • 4544289289 scopus 로고    scopus 로고
    • Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2
    • Moore MJ, et al. 2004. Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2. J. Virol. 78:10628-10635
    • (2004) J. Virol , vol.78 , pp. 10628-10635
    • Moore, M.J.1
  • 34
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation:diversity, synthesis and function
    • Moremen KW, Tiemeyer M, Nairn AV. 2012. Vertebrate protein glycosylation:diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13:448-462
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 35
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y, Hosokawa N, Wada I, Nagata K. 2003. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299:1394-1397
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 36
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus
    • Parlati F, Dominguez M, Bergeron JJ, Thomas DY. 1995. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270:244-253
    • (1995) J. Biol. Chem , vol.270 , pp. 244-253
    • Parlati, F.1    Dominguez, M.2    Bergeron, J.J.3    Thomas, D.Y.4
  • 37
    • 0242717589 scopus 로고    scopus 로고
    • Coronavirus as a possible cause of severe acute respiratory syndrome
    • Peiris JS, et al. 2003. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 361:1319-1325
    • (2003) Lancet , vol.361 , pp. 1319-1325
    • Peiris, J.S.1
  • 38
  • 39
    • 77249162621 scopus 로고    scopus 로고
    • Identification of N-linked carbohydrates from severe acute respiratory syndrome (SARS) spike glycoprotein
    • 39. Ritchie G, et al. 2010. Identification of N-linked carbohydrates from severe acute respiratory syndrome (SARS) spike glycoprotein. Virology 399:257-269
    • (2010) Virology , vol.399 , pp. 257-269
    • Ritchie, G.1
  • 40
    • 0037561920 scopus 로고    scopus 로고
    • Characterization of a novel coronavirus associated with severe acute respiratory syndrome
    • Rota PA, et al. 2003. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science 300:1394-1399
    • (2003) Science , vol.300 , pp. 1394-1399
    • Rota, P.A.1
  • 41
    • 77954143268 scopus 로고    scopus 로고
    • Targeting a host process as an antiviral approach against dengue virus
    • Sayce AC, Miller JL, Zitzmann N. 2010. Targeting a host process as an antiviral approach against dengue virus. Trends Microbiol. 18:323-330
    • (2010) Trends Microbiol , vol.18 , pp. 323-330
    • Sayce, A.C.1    Miller, J.L.2    Zitzmann, N.3
  • 42
    • 8144221377 scopus 로고    scopus 로고
    • Assessment of synthetic peptides of severe acute respiratory syndrome coronavirus recognized by long-lasting immunity
    • 42. Shichijo S, et al. 2004. Assessment of synthetic peptides of severe acute respiratory syndrome coronavirus recognized by long-lasting immunity.Tissue Antigens 64:600-607
    • (2004) Tissue Antigens , vol.64 , pp. 600-607
    • Shichijo, S.1
  • 43
    • 1642488368 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoproteinmediated viral entry
    • Simmons G, et al. 2004. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoproteinmediated viral entry. Proc. Natl. Acad. Sci. U.S.A. 101:4240-4245
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 4240-4245
    • Simmons, G.1
  • 44
    • 0025937289 scopus 로고
    • SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
    • Wada I, et al. 1991. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem.266:19599-19610
    • (1991) J. Biol. Chem , vol.266 , pp. 19599-19610
    • Wada, I.1
  • 45
    • 0942298133 scopus 로고    scopus 로고
    • A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensinconverting enzyme 2
    • Wong SK, Li W, Moore MJ, Choe H, Farzan M. 2004. A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensinconverting enzyme 2. J. Biol. Chem. 279:3197-3201
    • (2004) J. Biol. Chem , vol.279 , pp. 3197-3201
    • Wong, S.K.1    Li, W.2    Moore, M.J.3    Choe, H.4    Farzan, M.5
  • 47
    • 2442691605 scopus 로고    scopus 로고
    • pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN
    • Yang ZY, et al. 2004. pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN. J. Virol. 78:5642-5650
    • (2004) J. Virol , vol.78 , pp. 5642-5650
    • Yang, Z.Y.1
  • 48
    • 77956625296 scopus 로고    scopus 로고
    • A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms
    • Zhou Y, et al. 2010. A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms.J. Virol. 84:8753-8764
    • (2010) J. Virol , vol.84 , pp. 8753-8764
    • Zhou, Y.1
  • 49
    • 0032694353 scopus 로고    scopus 로고
    • Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus:implications for the development of broad spectrum anti-hepatitis virus agents
    • Zitzmann N, et al. 1999. Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus:implications for the development of broad spectrum anti-hepatitis virus agents. Proc. Natl. Acad. Sci. U.S.A. 96:11878-11882
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11878-11882
    • Zitzmann, N.1


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