메뉴 건너뛰기




Volumn 92, Issue 19, 2018, Pages

The S2 subunit of infectious bronchitis virus beaudette is a determinant of cellular tropism

Author keywords

Coronavirus; Infectious bronchitis virus; Reverse genetic analysis; S2= Cellular tropism

Indexed keywords

CORONAVIRUS SPIKE GLYCOPROTEIN;

EID: 85053405096     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01044-18     Document Type: Article
Times cited : (48)

References (98)
  • 1
    • 74849086825 scopus 로고    scopus 로고
    • Ratification vote on taxonomic proposals to the International Committee on Taxonomy of Viruses (2009)
    • Carstens EB. 2010. Ratification vote on taxonomic proposals to the International Committee on Taxonomy of Viruses (2009). Arch Virol 155:133–146. https://doi.org/10.1007/s00705-009-0547-x.
    • (2010) Arch Virol , vol.155 , pp. 133-146
    • Carstens, E.B.1
  • 2
    • 28944450194 scopus 로고    scopus 로고
    • Coronaviruses in poultry and other birds
    • Cavanagh D. 2005. Coronaviruses in poultry and other birds. Avian Pathol 34:439–448. https://doi.org/10.1080/03079450500367682.
    • (2005) Avian Pathol , vol.34 , pp. 439-448
    • Cavanagh, D.1
  • 3
    • 68249122816 scopus 로고    scopus 로고
    • Infectious bronchitis
    • Saif YM (ed), Blackwell Publishing, Ames, IA
    • Cavanagh D, Gelb J, Jr. 2008. Infectious bronchitis, p 117–135. In Saif YM (ed), Diseases of poultry, 12th ed. Blackwell Publishing, Ames, IA.
    • (2008) Diseases of Poultry, 12th Ed , pp. 117-135
    • Cavanagh, D.1    Gelb, J.2
  • 4
    • 77949335590 scopus 로고    scopus 로고
    • Viral respiratory diseases (ILT, aMPV infections, IB): Are they ever under control?
    • Jones RC. 2010. Viral respiratory diseases (ILT, aMPV infections, IB): are they ever under control? Br Poult Sci 51:1–11. https://doi.org/10.1080/00071660903541378.
    • (2010) Br Poult Sci , vol.51 , pp. 1-11
    • Jones, R.C.1
  • 5
    • 79959526711 scopus 로고    scopus 로고
    • Infectious bronchitis virus variants: A review of the history, current situation and control measures
    • de Wit JJ, Cook JKA, van der Heijden HMJF. 2011. Infectious bronchitis virus variants: a review of the history, current situation and control measures. Avian Pathol 40:223–235. https://doi.org/10.1080/03079457.2011.566260.
    • (2011) Avian Pathol , vol.40 , pp. 223-235
    • De Wit, J.J.1    Cook, J.K.A.2    Van Der Heijden, H.M.J.F.3
  • 6
    • 0002567367 scopus 로고    scopus 로고
    • Infectious bronchitis
    • Saif YM, Barnes HJ, Glisson JR, Fadly AM, McDougald LR, Swayne DE (ed.), 11th ed. Iowa State University Press, Ames, IA
    • Cavanagh D, Naqi S. 2003. Infectious bronchitis, p 101–119. In Saif YM, Barnes HJ, Glisson JR, Fadly AM, McDougald LR, Swayne DE (ed), Diseases of poultry, 11th ed. Iowa State University Press, Ames, IA.
    • (2003) Diseases of Poultry , pp. 101-119
    • Cavanagh, D.1    Naqi, S.2
  • 7
    • 70350528828 scopus 로고    scopus 로고
    • Avian coronavirus diseases and infectious bronchitis vaccine development
    • Thiel (ed), Caister Academic Press, Norfolk, United Kingdom
    • Britton P, Cavanagh D. 2007. Avian coronavirus diseases and infectious bronchitis vaccine development, p 161–181. In Thiel V (ed), Coronaviruses: molecular and cellular biology. Caister Academic Press, Norfolk, United Kingdom.
    • (2007) Coronaviruses: Molecular and Cellular Biology , pp. 161-181
    • Britton, P.1    Cavanagh, D.2
  • 8
    • 10044280770 scopus 로고    scopus 로고
    • Recombinant infectious bronchitis coronavirus Beaudette with the spike protein gene of the pathogenic M41 strain remains attenuated but induces protective immunity
    • Hodgson T, Casais R, Dove B, Britton P, Cavanagh D. 2004. Recombinant infectious bronchitis coronavirus Beaudette with the spike protein gene of the pathogenic M41 strain remains attenuated but induces protective immunity. J Virol 78:13804–13811. https://doi.org/10.1128/JVI.78.24.13804-13811.2004.
    • (2004) J Virol , vol.78 , pp. 13804-13811
    • Hodgson, T.1    Casais, R.2    Dove, B.3    Britton, P.4    Cavanagh, D.5
  • 9
    • 0025502073 scopus 로고
    • Early pathogenesis in chicks of infection with an enterotropic strain of infectious bronchitis virus
    • Ambali AG, Jones RC. 1990. Early pathogenesis in chicks of infection with an enterotropic strain of infectious bronchitis virus. Avian Dis 34: 809 – 817. https://doi.org/10.2307/1591367.
    • (1990) Avian Dis , vol.34 , pp. 809-817
    • Ambali, A.G.1    Jones, R.C.2
  • 10
    • 34147160583 scopus 로고    scopus 로고
    • Coronavirus avian infectious bronchitis virus
    • Cavanagh D. 2007. Coronavirus avian infectious bronchitis virus. Vet Res 38:281–297. https://doi.org/10.1051/vetres:2006055.
    • (2007) Vet Res , vol.38 , pp. 281-297
    • Cavanagh, D.1
  • 11
    • 0000673637 scopus 로고
    • Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus
    • Lambrechts C, Pensaert M, Ducatelle R. 1993. Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus. Avian Pathol 22:577–590. https://doi.org/10.1080/03079459308418945.
    • (1993) Avian Pathol , vol.22 , pp. 577-590
    • Lambrechts, C.1    Pensaert, M.2    Ducatelle, R.3
  • 13
    • 61449250832 scopus 로고    scopus 로고
    • Nidovirus genome organization and expression mechanisms
    • Perlman S, Gallagher T, Snijder EJ (ed.), ASM Press, Washington, DC
    • Britton P, Cavanagh D. 2008. Nidovirus genome organization and expression mechanisms, p 29 – 46. In Perlman S, Gallagher T, Snijder EJ (ed), Nidoviruses. ASM Press, Washington, DC.
    • (2008) Nidoviruses , pp. 29-46
    • Britton, P.1    Cavanagh, D.2
  • 14
    • 0030861788 scopus 로고    scopus 로고
    • The genome organisation of the Nidovirales: Similarities and differences between arteri-, toro- And coronaviruses
    • de Vries AAF, Horzinek MC, Rottier PJM, de Groot RJ. 1997. The genome organisation of the Nidovirales: similarities and differences between arteri-, toro- and coronaviruses. Semin Virol 8:33–47. https://doi.org/10.1006/smvy.1997.0104.
    • (1997) Semin Virol , vol.8 , pp. 33-47
    • De Vries, A.A.F.1    Horzinek, M.C.2    Rottier, P.J.M.3    De Groot, R.J.4
  • 15
    • 0030633479 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Lai MM, Cavanagh D. 1997. The molecular biology of coronaviruses. Adv Virus Res 48:1–100.
    • (1997) Adv Virus Res , vol.48 , pp. 1-100
    • Lai, M.M.1    Cavanagh, D.2
  • 16
    • 0025103827 scopus 로고
    • Assembly of coronavirus spike protein into trimers and its role in epitope expression
    • Delmas B, Laude H. 1990. Assembly of coronavirus spike protein into trimers and its role in epitope expression. J Virol 64:5367–5375.
    • (1990) J Virol , vol.64 , pp. 5367-5375
    • Delmas, B.1    Laude, H.2
  • 18
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex
    • Bosch BJ, van der Zee R, de Haan CA, Rottier PJ. 2003. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J Virol 77:8801–8811. https://doi.org/10.1128/JVI.77.16.8801-8811.2003.
    • (2003) J Virol , vol.77 , pp. 8801-8811
    • Bosch, B.J.1    Van Der Zee, R.2    De Haan, C.A.3    Rottier, P.J.4
  • 21
    • 85046421949 scopus 로고    scopus 로고
    • Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins
    • Shang J, Zheng Y, Yang Y, Liu C, Geng Q, Luo C, Zhang W, Li F. 2018. Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins. PLoS Pathog 14:e1007009. https://doi.org/10.1371/journal.ppat.1007009.
    • (2018) PLoS Pathog , vol.14
    • Shang, J.1    Zheng, Y.2    Yang, Y.3    Liu, C.4    Geng, Q.5    Luo, C.6    Zhang, W.7    Li, F.8
  • 22
    • 0035864294 scopus 로고    scopus 로고
    • Coronavirus spike proteins in viral entry and pathogenesis
    • Gallagher TM, Buchmeier MJ. 2001. Coronavirus spike proteins in viral entry and pathogenesis. Virology 279:371–374. https://doi.org/10.1006/viro.2000.0757.
    • (2001) Virology , vol.279 , pp. 371-374
    • Gallagher, T.M.1    Buchmeier, M.J.2
  • 23
    • 2442680275 scopus 로고    scopus 로고
    • Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion
    • De Haan CA, Stadler K, Godeke GJ, Bosch BJ, Rottier PJ. 2004. Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion. J Virol 78:6048 – 6054. https://doi.org/10.1128/JVI.78.11.6048-6054.2004.
    • (2004) J Virol , vol.78 , pp. 6048-6054
    • De Haan, C.A.1    Stadler, K.2    Godeke, G.J.3    Bosch, B.J.4    Rottier, P.J.5
  • 24
    • 0022397327 scopus 로고
    • Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments
    • Sturman LS, Ricard CS, Holmes KV. 1985. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments. J Virol 56:904–911.
    • (1985) J Virol , vol.56 , pp. 904-911
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 25
    • 0024226792 scopus 로고
    • Coronaviruses: Structure and genome expression
    • Spaan W, Cavanagh D, Horzinek MC. 1988. Coronaviruses: structure and genome expression. J Gen Virol 69:2939–2952. https://doi.org/10.1099/0022-1317-69-12-2939.
    • (1988) J Gen Virol , vol.69 , pp. 2939-2952
    • Spaan, W.1    Cavanagh, D.2    Horzinek, M.C.3
  • 26
    • 0025073955 scopus 로고
    • Antigenic domains of the peplomer protein of avian infectious bronchitis virus: Correlation with biological function
    • Koch G, Hartog L, Kant A, van Roozelaar DJ. 1990. Antigenic domains of the peplomer protein of avian infectious bronchitis virus: correlation with biological function. J Gen Virol 71:1929–1935. https://doi.org/10.1099/0022-1317-71-9-1929.
    • (1990) J Gen Virol , vol.71 , pp. 1929-1935
    • Koch, G.1    Hartog, L.2    Kant, A.3    Van Roozelaar, D.J.4
  • 27
    • 0026685054 scopus 로고
    • Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acid-containing receptors on erythrocytes
    • Schultze B, Cavanagh D, Herrler G. 1992. Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acid-containing receptors on erythrocytes. Virology 189:792–794. https://doi.org/10.1016/0042-6822(92)90608-R.
    • (1992) Virology , vol.189 , pp. 792-794
    • Schultze, B.1    Cavanagh, D.2    Herrler, G.3
  • 28
    • 0037223630 scopus 로고    scopus 로고
    • 8
    • Zelus BD, Schickli JH, Blau DM, Weiss SR, Holmes KV. 2003. Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8. J Virol 77:830–840. https://doi.org/10.1128/JVI.77.2.830-840.2003.
    • (2003) J Virol , vol.77 , pp. 830-840
    • Zelus, B.D.1    Schickli, J.H.2    Blau, D.M.3    Weiss, S.R.4    Holmes, K.V.5
  • 29
    • 70350322417 scopus 로고    scopus 로고
    • Two-step conformational changes in a coronavirus envelope glycoprotein mediated by receptor binding and pro-teolysis
    • Matsuyama S, Taguchi F. 2009. Two-step conformational changes in a coronavirus envelope glycoprotein mediated by receptor binding and pro-teolysis. J Virol 83:11133–11141. https://doi.org/10.1128/JVI.00959-09.
    • (2009) J Virol , vol.83 , pp. 11133-11141
    • Matsuyama, S.1    Taguchi, F.2
  • 30
    • 85031329007 scopus 로고    scopus 로고
    • Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
    • Walls AC, Tortorici MA, Snijder J, Xiong X, Bosch BJ, Rey FA, Veesler D. 2017. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc Natl Acad Sci U S A 114: 11157–11162. https://doi.org/10.1073/pnas.1708727114.
    • (2017) Proc Natl Acad Sci U S A , vol.114 , pp. 11157-11162
    • Walls, A.C.1    Tortorici, M.A.2    Snijder, J.3    Xiong, X.4    Bosch, B.J.5    Rey, F.A.6    Veesler, D.7
  • 31
    • 0029979024 scopus 로고    scopus 로고
    • The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins
    • Risco C, Anton IM, Enjuanes L, Carrascosa JL. 1996. The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins. J Virol 70:4773–4777.
    • (1996) J Virol , vol.70 , pp. 4773-4777
    • Risco, C.1    Anton, I.M.2    Enjuanes, L.3    Carrascosa, J.L.4
  • 32
    • 0032503238 scopus 로고    scopus 로고
    • Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein
    • Luo ZL, Weiss SR. 1998. Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein. Virology 244:483–494. https://doi.org/10.1006/viro.1998.9121.
    • (1998) Virology , vol.244 , pp. 483-494
    • Luo, Z.L.1    Weiss, S.R.2
  • 33
    • 10344234242 scopus 로고    scopus 로고
    • Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core
    • Xu Y, Lou Z, Liu Y, Pang H, Tien P, Gao GF, Rao Z. 2004. Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core. J Biol Chem 279:49414–49419. https://doi.org/10.1074/jbc.M408782200.
    • (2004) J Biol Chem , vol.279 , pp. 49414-49419
    • Xu, Y.1    Lou, Z.2    Liu, Y.3    Pang, H.4    Tien, P.5    Gao, G.F.6    Rao, Z.7
  • 35
    • 33845961570 scopus 로고    scopus 로고
    • Core structure of S2 from the human coronavirus NL63 spike glycoprotein
    • Zheng Q, Deng Y, Liu J, Van der Hoek L, Berkhout B, Lu M. 2006. Core structure of S2 from the human coronavirus NL63 spike glycoprotein. Biochemistry 45:15205–15215. https://doi.org/10.1021/bi061686w.
    • (2006) Biochemistry , vol.45 , pp. 15205-15215
    • Zheng, Q.1    Deng, Y.2    Liu, J.3    Van der Hoek, L.4    Berkhout, B.5    Lu, M.6
  • 36
    • 3142663245 scopus 로고    scopus 로고
    • Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core
    • Xu Y, Liu Y, Lou Z, Qin L, Li X, Bai Z, Pang H, Tien P, Gao GF, Rao Z. 2004. Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core. J Biol Chem 279:30514–30522.
    • (2004) J Biol Chem , vol.279 , pp. 30514-30522
    • Xu, Y.1    Liu, Y.2    Lou, Z.3    Qin, L.4    Li, X.5    Bai, Z.6    Pang, H.7    Tien, P.8    Gao, G.F.9    Rao, Z.10
  • 37
    • 17444401009 scopus 로고    scopus 로고
    • Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein
    • Duquerroy S, Vigouroux A, Rottier PJ, Rey FA, Jan Bosch B. 2005. Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein. Virology 335:276–285. https://doi.org/10.1016/j.virol.2005.02.022.
    • (2005) Virology , vol.335 , pp. 276-285
    • Duquerroy, S.1    Vigouroux, A.2    Rottier, P.J.3    Rey, F.A.4    Jan Bosch, B.5
  • 38
    • 84888052193 scopus 로고    scopus 로고
    • Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus
    • Gao J, Lu G, Qi J, Li Y, Wu Y, Deng Y, Geng H, Li H, Wang Q, Xiao H, Tan W, Yan J, Gao GF. 2013. Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus. J Virol 87:13134–13140. https://doi.org/10.1128/JVI.02433-13.
    • (2013) J Virol , vol.87 , pp. 13134-13140
    • Gao, J.1    Lu, G.2    Qi, J.3    Li, Y.4    Wu, Y.5    Deng, Y.6    Geng, H.7    Li, H.8    Wang, Q.9    Xiao, H.10    Tan, W.11    Yan, J.12    Gao, G.F.13
  • 39
    • 11144237311 scopus 로고    scopus 로고
    • Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
    • Supekar VM, Bruckmann C, Ingallinella P, Bianchi E, Pessi A, Carfi A. 2004. Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein. Proc Natl Acad Sci U S A 101:17958 –17963. https://doi.org/10.1073/pnas.0406128102.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17958-17963
    • Supekar, V.M.1    Bruckmann, C.2    Ingallinella, P.3    Bianchi, E.4    Pessi, A.5    Carfi, A.6
  • 41
    • 2442698802 scopus 로고    scopus 로고
    • Structural characterization of the SARS-coronavirus spike S fusion protein core
    • Tripet B, Howard MW, Jobling M, Holmes RK, Holmes KV, Hodges RS. 2004. Structural characterization of the SARS-coronavirus spike S fusion protein core. J Biol Chem 279:20836–20849. https://doi.org/10.1074/jbc.M400759200.
    • (2004) J Biol Chem , vol.279 , pp. 20836-20849
    • Tripet, B.1    Howard, M.W.2    Jobling, M.3    Holmes, R.K.4    Holmes, K.V.5    Hodges, R.S.6
  • 43
    • 70450231625 scopus 로고    scopus 로고
    • Role of spike protein endodomains in regulating coronavirus entry
    • Shulla A, Gallagher T. 2009. Role of spike protein endodomains in regulating coronavirus entry. J Biol Chem 284:32725–32734. https://doi.org/10.1074/jbc.M109.043547.
    • (2009) J Biol Chem , vol.284 , pp. 32725-32734
    • Shulla, A.1    Gallagher, T.2
  • 45
    • 0032874344 scopus 로고    scopus 로고
    • Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein
    • de Haan CA, Smeets M, Vernooij F, Vennema H, Rottier PJ. 1999. Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein. J Virol 73:7441–7452.
    • (1999) J Virol , vol.73 , pp. 7441-7452
    • De Haan, C.A.1    Smeets, M.2    Vernooij, F.3    Vennema, H.4    Rottier, P.J.5
  • 46
    • 0028018126 scopus 로고
    • Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein
    • Kubo H, Yamada YK, Taguchi F. 1994. Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein. J Virol 68: 5403–5410.
    • (1994) J Virol , vol.68 , pp. 5403-5410
    • Kubo, H.1    Yamada, Y.K.2    Taguchi, F.3
  • 47
    • 0037321751 scopus 로고    scopus 로고
    • Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E
    • Bonavia A, Zelus BD, Wentworth DE, Talbot PJ, Holmes KV. 2003. Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E. J Virol 77:2530–2538. https://doi.org/10.1128/JVI.77.4.2530-2538.2003.
    • (2003) J Virol , vol.77 , pp. 2530-2538
    • Bonavia, A.1    Zelus, B.D.2    Wentworth, D.E.3    Talbot, P.J.4    Holmes, K.V.5
  • 48
    • 2942592665 scopus 로고    scopus 로고
    • Amino acids 270 to 510 of the severe acute respiratory syndrome coronavirus spike protein are required for interaction with receptor
    • Babcock GJ, Esshaki DJ, Thomas WD, Jr, Ambrosino DM. 2004. Amino acids 270 to 510 of the severe acute respiratory syndrome coronavirus spike protein are required for interaction with receptor. J Virol 78: 4552–4560. https://doi.org/10.1128/JVI.78.9.4552-4560.2004.
    • (2004) J Virol , vol.78 , pp. 4552-4560
    • Babcock, G.J.1    Esshaki, D.J.2    Thomas, W.D.3    Ambrosino, D.M.4
  • 49
    • 84885762928 scopus 로고    scopus 로고
    • Mapping of the receptor-binding domain and amino acids critical for attachment in the spike protein of avian coronavirus infectious bronchitis virus
    • Promkuntod N, van Eijndhoven RE, de Vrieze G, Grone A, Verheije MH. 2014. Mapping of the receptor-binding domain and amino acids critical for attachment in the spike protein of avian coronavirus infectious bronchitis virus. Virology 448:26–32. https://doi.org/10.1016/j.virol.2013.09.018.
    • (2014) Virology , vol.448 , pp. 26-32
    • Promkuntod, N.1    Van Eijndhoven, R.E.2    De Vrieze, G.3    Grone, A.4    Verheije, M.H.5
  • 50
    • 0026729302 scopus 로고
    • Aminopeptidase N is a major receptor for the enteropatho-genic coronavirus TGEV
    • Delmas B, Gelfi J, L’Haridon R, Vogel LK, Sjöström H, Norén O, Laude H. 1992. Aminopeptidase N is a major receptor for the enteropatho-genic coronavirus TGEV. Nature 357:417–420. https://doi.org/10.1038/357417a0.
    • (1992) Nature , vol.357 , pp. 417-420
    • Delmas, B.1    Gelfi, J.2    L’Haridon, R.3    Vogel, L.K.4    Sjöström, H.5    Norén, O.6    Laude, H.7
  • 52
    • 0029861760 scopus 로고    scopus 로고
    • Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I
    • Tresnan DB, Levis R, Holmes KV. 1996. Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I. J Virol 70:8669 – 8674.
    • (1996) J Virol , vol.70 , pp. 8669-8674
    • Tresnan, D.B.1    Levis, R.2    Holmes, K.V.3
  • 53
    • 0026095354 scopus 로고
    • Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins
    • Williams RK, Jiang G-S, Holmes KV. 1991. Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins. Proc Natl Acad Sci U S A 88:5533–5536.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5533-5536
    • Williams, R.K.1    Jiang, G.-S.2    Holmes, K.V.3
  • 54
    • 77956622340 scopus 로고    scopus 로고
    • Attachment of mouse hepatitis virus to O-acetylated sialic acid is mediated by hemagglutinin-esterase and not by the spike protein
    • Langereis MA, van Vliet AL, Boot W, de Groot RJ. 2010. Attachment of mouse hepatitis virus to O-acetylated sialic acid is mediated by hemagglutinin-esterase and not by the spike protein. J Virol 84: 8970–8974. https://doi.org/10.1128/JVI.00566-10.
    • (2010) J Virol , vol.84 , pp. 8970-8974
    • Langereis, M.A.1    Van Vliet, A.L.2    Boot, W.3    De Groot, R.J.4
  • 57
    • 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. https://doi.org/10.1128/JVI.00315-07.
    • (2007) J Virol , vol.81 , pp. 12029-12039
    • Han, D.P.1    Lohani, M.2    Cho, M.W.3
  • 59
    • 33646155945 scopus 로고    scopus 로고
    • Sialic acid is a receptor determinant for infection of cells by avian infectious bronchitis virus
    • Winter C, Schwegmann-Wessels C, Cavanagh D, Neumann U, Herrler G. 2006. Sialic acid is a receptor determinant for infection of cells by avian infectious bronchitis virus. J Gen Virol 87:1209–1216. https://doi.org/10.1099/vir.0.81651-0.
    • (2006) J Gen Virol , vol.87 , pp. 1209-1216
    • Winter, C.1    Schwegmann-Wessels, C.2    Cavanagh, D.3    Neumann, U.4    Herrler, G.5
  • 60
    • 80052297532 scopus 로고    scopus 로고
    • Binding of avian coronavirus spike proteins to host factors reflects virus tropism and pathogenicity
    • Wickramasinghe IN, de Vries RP, Grone A, de Haan CA, Verheije MH. 2011. Binding of avian coronavirus spike proteins to host factors reflects virus tropism and pathogenicity. J Virol 85:8903–8912. https://doi.org/10.1128/JVI.05112-11.
    • (2011) J Virol , vol.85 , pp. 8903-8912
    • Wickramasinghe, I.N.1    De Vries, R.P.2    Grone, A.3    De Haan, C.A.4    Verheije, M.H.5
  • 61
    • 42649093768 scopus 로고    scopus 로고
    • Infection of the tracheal epithelium by infectious bronchitis virus is sialic acid dependent
    • Winter C, Herrler G, Neumann U. 2008. Infection of the tracheal epithelium by infectious bronchitis virus is sialic acid dependent. Microbes Infect 10:367–373. https://doi.org/10.1016/j.micinf.2007.12.009.
    • (2008) Microbes Infect , vol.10 , pp. 367-373
    • Winter, C.1    Herrler, G.2    Neumann, U.3
  • 62
    • 60549097922 scopus 로고    scopus 로고
    • Comparative analysis of the sialic acid binding activity and the tropism for the respiratory epithelium of four different strains of avian infectious bronchitis virus
    • Abd El Rahman S, El-Kenawy AA, Neumann U, Herrler G, Winter C. 2009. Comparative analysis of the sialic acid binding activity and the tropism for the respiratory epithelium of four different strains of avian infectious bronchitis virus. Avian Pathol 38:41– 45. https://doi.org/10.1080/03079450802632049.
    • (2009) Avian Pathol , vol.38 , pp. 41-45
    • Abd El Rahman, S.1    El-Kenawy, A.A.2    Neumann, U.3    Herrler, G.4    Winter, C.5
  • 63
    • 33947611188 scopus 로고    scopus 로고
    • Heparan sulfate is a selective attachment factor for the avian coronavirus infectious bronchitis virus Beaudette
    • Madu IG, Chu VC, Lee H, Regan AD, Bauman BE, Whittaker GR. 2007. Heparan sulfate is a selective attachment factor for the avian coronavirus infectious bronchitis virus Beaudette. Avian Dis 51:45–51. https://doi.org/10.1637/0005-2086(2007)051[0045:HSIASA]2.0.CO;2.
    • (2007) Avian Dis , vol.51 , pp. 45-51
    • Madu, I.G.1    Chu, V.C.2    Lee, H.3    Regan, A.D.4    Bauman, B.E.5    Whittaker, G.R.6
  • 64
    • 69249215352 scopus 로고    scopus 로고
    • Proteolytic activation of the spike protein at a novel RRRR/S motif is implicated in furin-dependent entry, syncytium formation, and infectivity of coronavirus infectious bronchitis virus in cultured cells
    • Yamada Y, Liu DX. 2009. Proteolytic activation of the spike protein at a novel RRRR/S motif is implicated in furin-dependent entry, syncytium formation, and infectivity of coronavirus infectious bronchitis virus in cultured cells. J Virol 83:8744 – 8758. https://doi.org/10.1128/JVI.00613-09.
    • (2009) J Virol , vol.83 , pp. 8744-8758
    • Yamada, Y.1    Liu, D.X.2
  • 65
    • 84867215031 scopus 로고    scopus 로고
    • Characterization of cellular furin content as a potential factor determining the susceptibility of cultured human and animal cells to coronavirus infectious bronchitis virus infection
    • Tay F, Huang M, Wang L, Yamada Y, Liu DX. 2012. Characterization of cellular furin content as a potential factor determining the susceptibility of cultured human and animal cells to coronavirus infectious bronchitis virus infection. Virology 433:421–430. https://doi.org/10.1016/j.virol.2012.08.037.
    • (2012) Virology , vol.433 , pp. 421-430
    • Tay, F.1    Huang, M.2    Wang, L.3    Yamada, Y.4    Liu, D.X.5
  • 66
    • 65249097210 scopus 로고    scopus 로고
    • Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites
    • Belouzard S, Chu VC, Whittaker GR. 2009. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc Natl Acad Sci U S A 106:5871–5876. https://doi.org/10.1073/pnas.0809524106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5871-5876
    • Belouzard, S.1    Chu, V.C.2    Whittaker, G.R.3
  • 67
    • 84908065761 scopus 로고    scopus 로고
    • Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein
    • Millet JK, Whittaker GR. 2014. Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein. Proc Natl Acad Sci U S A 111:15214–15219. https://doi.org/10.1073/pnas.1407087111.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 15214-15219
    • Millet, J.K.1    Whittaker, G.R.2
  • 68
    • 85012005505 scopus 로고    scopus 로고
    • A camel-derived MERS-CoV with a variant spike protein cleavage site and distinct fusion activation properties
    • Millet JK, Goldstein M, Labitt RN, Hsu H, Daniel S, Whittaker GR. 2016. A camel-derived MERS-CoV with a variant spike protein cleavage site and distinct fusion activation properties. Emerg Microbes Infect 5:e126. https://doi.org/10.1038/emi.2016.125.
    • (2016) Emerg Microbes Infect , vol.5 , pp. e126
    • Millet, J.K.1    Goldstein, M.2    Labitt, R.N.3    Hsu, H.4    Daniel, S.5    Whittaker, G.R.6
  • 69
    • 85049847621 scopus 로고    scopus 로고
    • HCoV-229E spike protein fusion activation by trypsin-like serine pro-teases is mediated by proteolytic processing in the S2= region
    • Bonnin A, Danneels A, Dubuisson J, Goffard A, Belouzard S. 2018. HCoV-229E spike protein fusion activation by trypsin-like serine pro-teases is mediated by proteolytic processing in the S2= region. J Gen Virol 99:908–912. https://doi.org/10.1099/jgv.0.001074.
    • (2018) J Gen Virol , vol.99 , pp. 908-912
    • Bonnin, A.1    Danneels, A.2    Dubuisson, J.3    Goffard, A.4    Belouzard, S.5
  • 70
    • 0344069787 scopus 로고    scopus 로고
    • Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence
    • Sanchez CM, Izeta A, Sanchez-Morgado JM, Alonso S, Sola I, Balasch M, Plana-Duran J, Enjuanes L. 1999. Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence. J Virol 73:7607–7618.
    • (1999) J Virol , vol.73 , pp. 7607-7618
    • Sanchez, C.M.1    Izeta, A.2    Sanchez-Morgado, J.M.3    Alonso, S.4    Sola, I.5    Balasch, M.6    Plana-Duran, J.7    Enjuanes, L.8
  • 71
    • 73949093289 scopus 로고    scopus 로고
    • Chimeric feline coronaviruses that encode type II spike protein on type I genetic background display accelerated viral growth and altered receptor usage
    • Tekes G, Hofmann-Lehmann R, Bank-Wolf B, Maier R, Thiel HJ, Thiel V. 2010. Chimeric feline coronaviruses that encode type II spike protein on type I genetic background display accelerated viral growth and altered receptor usage. J Virol 84:1326–1333. https://doi.org/10.1128/JVI.01568-09.
    • (2010) J Virol , vol.84 , pp. 1326-1333
    • Tekes, G.1    Hofmann-Lehmann, R.2    Bank-Wolf, B.3    Maier, R.4    Thiel, H.J.5    Thiel, V.6
  • 72
    • 0015399142 scopus 로고
    • Replication of avian infectious bronchitis virus in African green monkey kidney cell line VERO
    • Cunningham CH, Spring MP, Nazerian K. 1972. Replication of avian infectious bronchitis virus in African green monkey kidney cell line VERO. J Gen Virol 16:423– 427. https://doi.org/10.1099/0022-1317-16-3-423.
    • (1972) J Gen Virol , vol.16 , pp. 423-427
    • Cunningham, C.H.1    Spring, M.P.2    Nazerian, K.3
  • 73
    • 0018428180 scopus 로고
    • Studies on avian infectious bronchitis virus (IBV). II. Propagation of IBV in several cultured cells
    • Otsuki K, Noro K, Yamamoto H, Tsubokura M. 1979. Studies on avian infectious bronchitis virus (IBV). II. Propagation of IBV in several cultured cells. Arch Virol 60:115–122.
    • (1979) Arch Virol , vol.60 , pp. 115-122
    • Otsuki, K.1    Noro, K.2    Yamamoto, H.3    Tsubokura, M.4
  • 74
    • 0042208051 scopus 로고    scopus 로고
    • Recombinant avian infectious bronchitis virus expressing a heterologous spike gene demonstrates that the spike protein is a determinant of cell tropism
    • Casais R, Dove B, Cavanagh D, Britton P. 2003. Recombinant avian infectious bronchitis virus expressing a heterologous spike gene demonstrates that the spike protein is a determinant of cell tropism. J Virol 77:9084–9089. https://doi.org/10.1128/JVI.77.16.9084-9089.2003.
    • (2003) J Virol , vol.77 , pp. 9084-9089
    • Casais, R.1    Dove, B.2    Cavanagh, D.3    Britton, P.4
  • 75
    • 0035194291 scopus 로고    scopus 로고
    • Reverse genetics system for the avian coronavirus infectious bronchitis virus
    • Casais R, Thiel V, Siddell SG, Cavanagh D, Britton P. 2001. Reverse genetics system for the avian coronavirus infectious bronchitis virus. J Virol 75:12359–12369. https://doi.org/10.1128/JVI.75.24.12359-12369.2001.
    • (2001) J Virol , vol.75 , pp. 12359-12369
    • Casais, R.1    Thiel, V.2    Siddell, S.G.3    Cavanagh, D.4    Britton, P.5
  • 76
    • 11144306448 scopus 로고    scopus 로고
    • Generation of a recombinant avian coronavirus infectious bronchitis virus using transient dominant selection
    • Britton P, Evans S, Dove B, Davies M, Casais R, Cavanagh D. 2005. Generation of a recombinant avian coronavirus infectious bronchitis virus using transient dominant selection. J Virol Methods 123:203–211. https://doi.org/10.1016/j.jviromet.2004.09.017.
    • (2005) J Virol Methods , vol.123 , pp. 203-211
    • Britton, P.1    Evans, S.2    Dove, B.3    Davies, M.4    Casais, R.5    Cavanagh, D.6
  • 77
    • 84934439755 scopus 로고    scopus 로고
    • Transient dominant selection for the modification and generation of recombinant infectious bronchitis coronaviruses
    • Armesto M, Casais R, Cavanagh D, Britton P. 2008. Transient dominant selection for the modification and generation of recombinant infectious bronchitis coronaviruses. Methods Mol Biol 454:255–273. https://doi.org/10.1007/978-1-59745-181-9_19.
    • (2008) Methods Mol Biol , vol.454 , pp. 255-273
    • Armesto, M.1    Casais, R.2    Cavanagh, D.3    Britton, P.4
  • 78
    • 80052304197 scopus 로고    scopus 로고
    • A recombinant avian infectious bronchitis virus expressing a heterologous spike gene belonging to the 4/91 serotype
    • Armesto M, Evans S, Cavanagh D, Abu-Median AB, Keep S, Britton P. 2011. A recombinant avian infectious bronchitis virus expressing a heterologous spike gene belonging to the 4/91 serotype. PLoS One 6:e24352. https://doi.org/10.1371/journal.pone.0024352.
    • (2011) PLoS One , vol.6
    • Armesto, M.1    Evans, S.2    Cavanagh, D.3    Abu-Median, A.B.4    Keep, S.5    Britton, P.6
  • 80
    • 0019182613 scopus 로고
    • The large-scale cultivation of VERO cells in micro-carrier culture for virus vaccine production. Preliminary results for killed poliovirus vaccine
    • Montagnon BJ, Fanget B, Nicolas AJ. 1981. The large-scale cultivation of VERO cells in micro-carrier culture for virus vaccine production. Preliminary results for killed poliovirus vaccine. Dev Biol Stand 47: 55–64.
    • (1981) Dev Biol Stand , vol.47 , pp. 55-64
    • Montagnon, B.J.1    Fanget, B.2    Nicolas, A.J.3
  • 81
    • 0029945540 scopus 로고    scopus 로고
    • African green monkey kidney (Vero) cells provide an alternative host cell system for influenza A and B viruses
    • Govorkova EA, Murti G, Meignier B, De Taisne C, Webster RG. 1996. African green monkey kidney (Vero) cells provide an alternative host cell system for influenza A and B viruses. J Virol 70:5519–5524.
    • (1996) J Virol , vol.70 , pp. 5519-5524
    • Govorkova, E.A.1    Murti, G.2    Meignier, B.3    De Taisne, C.4    Webster, R.G.5
  • 82
    • 0032078697 scopus 로고    scopus 로고
    • Development of a mammalian cell (Vero) derived candidate influenza virus vaccine
    • Kistner O, Barrett PN, Mundt W, Reiter M, Schober-Bendixen S, Dorner F. 1998. Development of a mammalian cell (Vero) derived candidate influenza virus vaccine. Vaccine 16:960–968. https://doi.org/10.1016/S0264-410X(97)00301-0.
    • (1998) Vaccine , vol.16 , pp. 960-968
    • Kistner, O.1    Barrett, P.N.2    Mundt, W.3    Reiter, M.4    Schober-Bendixen, S.5    Dorner, F.6
  • 83
    • 34250444348 scopus 로고
    • The pathogenesis of virulent and avirulent avian infectious bronchitis virus
    • Geilhausen HE, Ligon FB, Lukert PD. 1973. The pathogenesis of virulent and avirulent avian infectious bronchitis virus. Arch Gesamte Virusforsch 40:285–290.
    • (1973) Arch Gesamte Virusforsch , vol.40 , pp. 285-290
    • Geilhausen, H.E.1    Ligon, F.B.2    Lukert, P.D.3
  • 85
    • 0017259047 scopus 로고
    • The use of chicken tracheal organ cultures for the isolation and assay of avian infectious bronchitis virus
    • Cook JKA, Darbyshire JH, Peters RW. 1976. The use of chicken tracheal organ cultures for the isolation and assay of avian infectious bronchitis virus. Arch Virol 50:109–118. https://doi.org/10.1007/BF01318005.
    • (1976) Arch Virol , vol.50 , pp. 109-118
    • Cook, J.K.A.1    Darbyshire, J.H.2    Peters, R.W.3
  • 86
    • 0018647549 scopus 로고
    • Taxonomic studies on strains of avian infectious bronchitis virus using neutralisation tests in tracheal organ cultures
    • Darbyshire JH, Rowell JG, Cook JKA, Peters RW. 1979. Taxonomic studies on strains of avian infectious bronchitis virus using neutralisation tests in tracheal organ cultures. Arch Virol 61:227–238. https://doi.org/10.1007/BF01318057.
    • (1979) Arch Virol , vol.61 , pp. 227-238
    • Darbyshire, J.H.1    Rowell, J.G.2    Cook, J.K.A.3    Peters, R.W.4
  • 87
    • 0141629027 scopus 로고
    • Cultivation of the virus of infectious bronchitis
    • Beaudette FR, Hudson CB. 1937. Cultivation of the virus of infectious bronchitis. J Am Vet Med Assoc 90:51–60.
    • (1937) J Am Vet Med Assoc , vol.90 , pp. 51-60
    • Beaudette, F.R.1    Hudson, C.B.2
  • 88
    • 0022626625 scopus 로고
    • Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41
    • Cavanagh D, Davis PJ, Pappin DJC, Binns MM, Boursnell MEG, Brown TDK. 1986. Coronavirus IBV: partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41. Virus Res 4:133–143. https://doi.org/10.1016/0168-1702(86)90037-7.
    • (1986) Virus Res , vol.4 , pp. 133-143
    • Cavanagh, D.1    Davis, P.J.2    Pappin, D.J.C.3    Binns, M.M.4    Boursnell, M.E.G.5    Brown, T.D.K.6
  • 89
    • 0027930161 scopus 로고
    • Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus
    • Pénzes Z, Tibbles K, Shaw K, Britton P, Brown TDK, Cavanagh D. 1994. Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus. Virology 203:286 –293. https://doi.org/10.1006/viro.1994.1486.
    • (1994) Virology , vol.203 , pp. 286-293
    • Pénzes, Z.1    Tibbles, K.2    Shaw, K.3    Britton, P.4    Brown, T.D.K.5    Cavanagh, D.6
  • 90
    • 0029864544 scopus 로고    scopus 로고
    • Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame
    • Pénzes Z, Wroe C, Brown TD, Britton P, Cavanagh D. 1996. Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame. J Virol 70:8660–8668.
    • (1996) J Virol , vol.70 , pp. 8660-8668
    • Pénzes, Z.1    Wroe, C.2    Brown, T.D.3    Britton, P.4    Cavanagh, D.5
  • 91
    • 0033956460 scopus 로고    scopus 로고
    • Leader switching occurs during the rescue of defective RNAs by heterologous strains of the coronavirus infectious bronchitis virus
    • Stirrups K, Shaw K, Evans S, Dalton K, Cavanagh D, Britton P. 2000. Leader switching occurs during the rescue of defective RNAs by heterologous strains of the coronavirus infectious bronchitis virus. J Gen Virol 81:791–801. https://doi.org/10.1099/0022-1317-81-3-791.
    • (2000) J Gen Virol , vol.81 , pp. 791-801
    • Stirrups, K.1    Shaw, K.2    Evans, S.3    Dalton, K.4    Cavanagh, D.5    Britton, P.6
  • 93
    • 0014914261 scopus 로고
    • Avian infectious bronchitis
    • Cunningham CH. 1970. Avian infectious bronchitis. Adv Vet Sci 14: 106–148.
    • (1970) Adv Vet Sci , vol.14 , pp. 106-148
    • Cunningham, C.H.1
  • 94
    • 0016418375 scopus 로고
    • Immunity to avian infectious bronchitis
    • Perkins FT, Regamey RH (ed.), Karger, London, United Kingdom
    • Cunningham CH. 1975. Immunity to avian infectious bronchitis, p 546–562. In Perkins FT, Regamey RH (ed), Immunity to infections of the respiratory system in man and animals, vol 28. Karger, London, United Kingdom.
    • (1975) Immunity to Infections of The Respiratory System in Man and Animals , vol.28 , pp. 546-562
    • Cunningham, C.H.1
  • 95
    • 85054082319 scopus 로고    scopus 로고
    • Bickerton E. 2011. PhD thesis. University of Warwick, United Kingdom
    • Bickerton E. 2011. PhD thesis. University of Warwick, United Kingdom.
  • 97
    • 0023264833 scopus 로고
    • Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus
    • Boursnell MEG, Brown TDK, Foulds IJ, Green PF, Tomley FM, Binns MM. 1987. Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus. J Gen Virol 68:57–77. https://doi.org/10.1099/0022-1317-68-1-57.
    • (1987) J Gen Virol , vol.68 , pp. 57-77
    • Boursnell, M.E.G.1    Brown, T.D.K.2    Foulds, I.J.3    Green, P.F.4    Tomley, F.M.5    Binns, M.M.6
  • 98
    • 0029592773 scopus 로고
    • A new DNA sequence assembly program
    • Bonfield JK, Smith KF, Staden R. 1995. A new DNA sequence assembly program. Nucleic Acids Res 23:4992–4999. https://doi.org/10.1093/nar/23.24.4992.
    • (1995) Nucleic Acids Res , vol.23 , pp. 4992-4999
    • Bonfield, J.K.1    Smith, K.F.2    Staden, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.