메뉴 건너뛰기




Volumn 80, Issue 7, 2006, Pages 3180-3188

The avian coronavirus infectious bronchitis virus undergoes direct low-pH-dependent fusion activation during entry into host cells

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE INHIBITOR; VIRUS PROTEIN;

EID: 33645229326     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.80.7.3180-3188.2006     Document Type: Article
Times cited : (74)

References (57)
  • 1
    • 0141629027 scopus 로고
    • Cultivation of the virus of infectious bronchitis
    • Beaudette, F. R., and C. R. Hudson. 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.R.2
  • 3
    • 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, B. J., R. van der Zee, C. A. de Haan, and P. J. Rottier. 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.
    • (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
  • 4
    • 0023403269 scopus 로고
    • The influenza hemagglutinin precursor as an acid-sensitive probe of the biosynthetic pathway
    • Boulay, F., R. W. Doms, I. Wilson, and A. Helenius. 1987. The influenza hemagglutinin precursor as an acid-sensitive probe of the biosynthetic pathway. EMBO J. 6:2643-2650.
    • (1987) EMBO J. , vol.6 , pp. 2643-2650
    • Boulay, F.1    Doms, R.W.2    Wilson, I.3    Helenius, A.4
  • 5
    • 28944439705 scopus 로고    scopus 로고
    • Coronaviridae: A review of coronaviruses and toroviruses
    • A. Schmidt, M. H. Wolff, and O. Weber (ed.). Birkhauser Verlag, Basel, Switzerland
    • Cavanagh, D. 2005. Coronaviridae: a review of coronaviruses and toroviruses, p. 1-54. In A. Schmidt, M. H. Wolff, and O. Weber (ed.), Coronaviruses with special emphasis on first insights concerning SARS. Birkhauser Verlag, Basel, Switzerland.
    • (2005) Coronaviruses with Special Emphasis on First Insights Concerning SARS , pp. 1-54
    • Cavanagh, D.1
  • 6
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • S. G. Siddell (ed.). Plenum Press, New York, N.Y.
    • Cavanagh, D. 1995. The coronavirus surface glycoprotein, p. 73-113. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 73-113
    • Cavanagh, D.1
  • 7
    • 0022743435 scopus 로고
    • Coronavirus IBV: Removal of spike glycopolypeptide S1 by urea abolishes infectivity and haemagglutination but not attachment to cells
    • Cavanagh, D., and P. J. Davis. 1986. Coronavirus IBV: removal of spike glycopolypeptide S1 by urea abolishes infectivity and haemagglutination but not attachment to cells. J. Gen. Virol. 67:1443-1448.
    • (1986) J. Gen. Virol. , vol.67 , pp. 1443-1448
    • Cavanagh, D.1    Davis, P.J.2
  • 8
    • 0002567367 scopus 로고    scopus 로고
    • Infectious bronchitis
    • S. M. Saif (ed.). Iowa State Press, Ames, Iowa
    • Cavanagh, D., and S. A. Naqi. 2003. Infectious bronchitis, p. 101-119. In S. M. Saif (ed.), Diseases of poultry. Iowa State Press, Ames, Iowa.
    • (2003) Diseases of Poultry , pp. 101-119
    • Cavanagh, D.1    Naqi, S.A.2
  • 9
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., C. R. Pringle, and A. J. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 10
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 11
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P. M., and M. C. Lawrence. 2003. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell. Biol. 4:309-319.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 12
    • 0037370724 scopus 로고    scopus 로고
    • The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH
    • Earp, L. J., S. E. Delos, R. C. Netter, P. Bates, and J. M. White. 2003. The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH. J. Virol. 77:3058-3066.
    • (2003) J. Virol. , vol.77 , pp. 3058-3066
    • Earp, L.J.1    Delos, S.E.2    Netter, R.C.3    Bates, P.4    White, J.M.5
  • 14
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 15
    • 26444468666 scopus 로고
    • Studies on the diagnosis of Newcastle disease and infectious bronchitis. IV. The use of the serum neutralization test in the diagnosis of infectious bronchitis
    • Fabricant, J. 1951. Studies on the diagnosis of Newcastle disease and infectious bronchitis. IV. The use of the serum neutralization test in the diagnosis of infectious bronchitis. Cornell Vet. 61:68-80.
    • (1951) Cornell Vet. , vol.61 , pp. 68-80
    • Fabricant, J.1
  • 16
    • 0035864294 scopus 로고    scopus 로고
    • Coronavirus spike proteins in viral entry and pathogenesis
    • Gallagher, T. M., and M. J. Buchmeier. 2001. Coronavirus spike proteins in viral entry and pathogenesis. Virology 279:371-374.
    • (2001) Virology , vol.279 , pp. 371-374
    • Gallagher, T.M.1    Buchmeier, M.J.2
  • 17
    • 0033656456 scopus 로고    scopus 로고
    • Reversibility in fusion protein conformational changes. The intriguing case of rhabdovirus-induced membrane fusion
    • Gaudin, Y. 2000. Reversibility in fusion protein conformational changes. The intriguing case of rhabdovirus-induced membrane fusion. Subcell. Biochem. 34:379-408.
    • (2000) Subcell. Biochem. , vol.34 , pp. 379-408
    • Gaudin, Y.1
  • 18
    • 0025093305 scopus 로고
    • Fusion of Rous sarcoma virus with host cells does not require exposure to low pH
    • Gilbert, J. M., D. Mason, and J. M. White. 1990. Fusion of Rous sarcoma virus with host cells does not require exposure to low pH. J. Virol. 64:5106-5113.
    • (1990) J. Virol. , vol.64 , pp. 5106-5113
    • Gilbert, J.M.1    Mason, D.2    White, J.M.3
  • 19
    • 0031964681 scopus 로고    scopus 로고
    • The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment
    • Hansen, G. H., B. Delmas, L. Besnardeau, L. K. Vogel, H. Laude, H. Sjostrom, and O. Noren. 1998. The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment. J. Virol. 72:527-534.
    • (1998) J. Virol. , vol.72 , pp. 527-534
    • Hansen, G.H.1    Delmas, B.2    Besnardeau, L.3    Vogel, L.K.4    Laude, H.5    Sjostrom, H.6    Noren, O.7
  • 20
    • 0027250564 scopus 로고
    • Fluorescence assays to monitor fusion of enveloped viruses
    • Hoekstra, D., and K. Klappe. 1993. Fluorescence assays to monitor fusion of enveloped viruses. Methods Enzymol. 220:261-276.
    • (1993) Methods Enzymol. , vol.220 , pp. 261-276
    • Hoekstra, D.1    Klappe, K.2
  • 21
    • 4644323974 scopus 로고    scopus 로고
    • Cellular entry of the SARS coronavirus
    • Hofmann, H., and S. Pohlmann. 2004. Cellular entry of the SARS coronavirus. Trends Microbiol. 12:466-472.
    • (2004) Trends Microbiol. , vol.12 , pp. 466-472
    • Hofmann, H.1    Pohlmann, S.2
  • 22
    • 0038326554 scopus 로고    scopus 로고
    • SARS-associated Coronavirus
    • Holmes, K. V. 2003. SARS-associated Coronavirus. N. Engl. J. Med. 348:1948-1951.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1948-1951
    • Holmes, K.V.1
  • 23
    • 0344051755 scopus 로고
    • Coronavirus receptors
    • S. G. Siddell (ed.). Plenum Press, New York, N.Y.
    • Holmes, K. V., and S. R. Compton. 1995. Coronavirus receptors, p. 55-71. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 55-71
    • Holmes, K.V.1    Compton, S.R.2
  • 25
    • 0026936301 scopus 로고
    • Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes
    • Karaca, K., S. Naqi, and J. Gelb, Jr. 1992. Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes. Avian Dis. 36:903-915.
    • (1992) Avian Dis. , vol.36 , pp. 903-915
    • Karaca, K.1    Naqi, S.2    Gelb Jr., J.3
  • 26
    • 3042845376 scopus 로고    scopus 로고
    • Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy
    • Kliger, Y., and E. Y. Levanon. 2003. Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy. BMC Microbiol. 3:20.
    • (2003) BMC Microbiol. , vol.3 , pp. 20
    • Kliger, Y.1    Levanon, E.Y.2
  • 27
    • 0028170284 scopus 로고
    • pH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational change of hemagglutinin
    • Korte, T., and A. Herrmann. 1994. pH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational change of hemagglutinin. Eur. Biophys. J. 23:105-113.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 105-113
    • Korte, T.1    Herrmann, A.2
  • 28
    • 0003208239 scopus 로고    scopus 로고
    • Coronaviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howely (ed.). Lippincott Wilkins and Williams, Philadelphia, Pa.
    • Lai, M. M. C., and K. V. Holmes. 2001. Coronaviridae: the viruses and their replication. In D. M. Knipe and P. M. Howely (ed.), Fields virology. Lippincott Wilkins and Williams, Philadelphia, Pa.
    • (2001) Fields Virology
    • Lai, M.M.C.1    Holmes, K.V.2
  • 29
    • 0037205452 scopus 로고    scopus 로고
    • Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors
    • Lewicki, D. N., and T. M. Gallagher. 2002. Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors. J. Biol. Chem. 277:19727-19734.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19727-19734
    • Lewicki, D.N.1    Gallagher, T.M.2
  • 30
    • 0026442011 scopus 로고
    • Coronavirus IBV-induced membrane fusion occurs at near-neutral pH
    • Li, D., and D. Cavanagh. 1992. Coronavirus IBV-induced membrane fusion occurs at near-neutral pH. Arch. Virol. 122:307-316.
    • (1992) Arch. Virol. , vol.122 , pp. 307-316
    • Li, D.1    Cavanagh, D.2
  • 31
    • 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., G. Xiao, Y. Chen, Y. He, J. Niu, C. R. Escalante, H. Xiong, J. Farmar, A. K. Debnath, P. Tien, and S. Jiang. 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    Xiao, G.2    Chen, Y.3    He, Y.4    Niu, J.5    Escalante, C.R.6    Xiong, H.7    Farmar, J.8    Debnath, A.K.9    Tien, P.10    Jiang, S.11
  • 32
    • 2442647673 scopus 로고    scopus 로고
    • Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site
    • Lontok, E., E. Corse, and C. E. Machamer. 2004. Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site. J. Virol. 78:5913-5922.
    • (2004) J. Virol. , vol.78 , pp. 5913-5922
    • Lontok, E.1    Corse, E.2    Machamer, C.E.3
  • 33
    • 0031026138 scopus 로고    scopus 로고
    • SFV infection in CHO cells: Cell-type specific restrictions to productive virus entry at the cell surface
    • Marsh, M., and R. Bron. 1997. SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface. J. Cell Sci. 110:95-103.
    • (1997) J. Cell Sci. , vol.110 , pp. 95-103
    • Marsh, M.1    Bron, R.2
  • 34
    • 0036889416 scopus 로고    scopus 로고
    • Receptor-induced conformational changes of murine coronavirus spike protein
    • Matsuyama, S., and F. Taguchi. 2002. Receptor-induced conformational changes of murine coronavirus spike protein. J. Virol. 76:11819-11826.
    • (2002) J. Virol. , vol.76 , pp. 11819-11826
    • Matsuyama, S.1    Taguchi, F.2
  • 35
    • 24644441711 scopus 로고    scopus 로고
    • Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection
    • Matsuyama, S., M. Ujike, S. Morikawa, M. Tashiro, and F. Taguchi. 2005. Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection. Proc. Natl. Acad. Sci. USA 102:12543-12547.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12543-12547
    • Matsuyama, S.1    Ujike, M.2    Morikawa, S.3    Tashiro, M.4    Taguchi, F.5
  • 36
    • 0000514665 scopus 로고
    • Infectious bronchitis
    • J. B. McFerran and M. S. McNulty (ed.). Elsevier, Amsterdam, The Netherlands
    • McMartin, D. 1993. Infectious bronchitis. In J. B. McFerran and M. S. McNulty (ed.), Virus infections of birds. Elsevier, Amsterdam, The Netherlands.
    • (1993) Virus Infections of Birds
    • McMartin, D.1
  • 38
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes, W., A. L. Boerger, S. Narayan, J. M. Cunningham, and J. A. T. Young. 2000. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 103:679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.T.5
  • 39
    • 0032546590 scopus 로고    scopus 로고
    • Probe transfer with and without membrane fusion in a fluorescence fusion assay
    • Ohki, S., T. D. Flanagan, and D. Hoekstra. 1998. Probe transfer with and without membrane fusion in a fluorescence fusion assay. Biochemistry 37:7496-7503.
    • (1998) Biochemistry , vol.37 , pp. 7496-7503
    • Ohki, S.1    Flanagan, T.D.2    Hoekstra, D.3
  • 40
    • 0018428180 scopus 로고
    • Studies on avian infectious bronchitis virus (IBV). II. Propagation of IBV in several cultured cells
    • Otsuki, K., K. Noro, H. Yamamoto, and M. Tsubokura. 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
  • 41
    • 0024273129 scopus 로고
    • Analysis of cell fusion induced by bovine coronavirus infection
    • Payne, H. R., and J. Storz. 1988. Analysis of cell fusion induced by bovine coronavirus infection. Arch. Virol. 103:27-33.
    • (1988) Arch. Virol. , vol.103 , pp. 27-33
    • Payne, H.R.1    Storz, J.2
  • 42
    • 0026611884 scopus 로고
    • Kinetic modeling of Sendai virus fusion with PC-12 cells. Effect of pH and temperature on fusion and viral inactivation
    • Pedroso de Lima, M. C., J. Ramalho-Santos, M. F. Martins, A. Pato de Carvalho, V. Bairos, and S. Nir. 1992. Kinetic modeling of Sendai virus fusion with PC-12 cells. Effect of pH and temperature on fusion and viral inactivation. Eur. J. Biochem. 205:181-186.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 181-186
    • Pedroso De Lima, M.C.1    Ramalho-Santos, J.2    Martins, M.F.3    Pato De Carvalho, A.4    Bairos, V.5    Nir, S.6
  • 43
    • 10944238037 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome
    • Peiris, J. S., Y. Guan, and K. Y. Yuen. 2004. Severe acute respiratory syndrome. Nat. Med. 10:S88-S97.
    • (2004) Nat. Med. , vol.10
    • Peiris, J.S.1    Guan, Y.2    Yuen, K.Y.3
  • 45
    • 0032750933 scopus 로고    scopus 로고
    • Vesicular stomatitis virus G protein acquires pH-independent fusion activity during transport in a polarized endometrial cell line
    • Roberts, P. C., T. Kipperman, and R. W. Compans. 1999. Vesicular stomatitis virus G protein acquires pH-independent fusion activity during transport in a polarized endometrial cell line. J. Virol. 73:10447-10457.
    • (1999) J. Virol. , vol.73 , pp. 10447-10457
    • Roberts, P.C.1    Kipperman, T.2    Compans, R.W.3
  • 46
    • 0014589353 scopus 로고
    • Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties
    • Rosen, C. G., and G. Weber. 1969. Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties. Biochemistry 8:3915-3920.
    • (1969) Biochemistry , vol.8 , pp. 3915-3920
    • Rosen, C.G.1    Weber, G.2
  • 47
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski, S. B., and G. R. Whittaker. 2002. Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J. Virol. 76:10455-10464.
    • (2002) J. Virol. , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 49
    • 1642488368 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry
    • Simmons, G., J. D. Reeves, A. J. Rennekamp, S. M. Amberg, A. J. Piefer, and P. Bates. 2004. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc. Natl. Acad. Sci. USA 101:4240-4245.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4240-4245
    • Simmons, G.1    Reeves, J.D.2    Rennekamp, A.J.3    Amberg, S.M.4    Piefer, A.J.5    Bates, P.6
  • 50
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 51
    • 0025354474 scopus 로고
    • Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion
    • Sturman, L. S., C. S. Ricard, and K. V. Holmes. 1990. Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion. J. Virol. 64:3042-3050.
    • (1990) J. Virol. , vol.64 , pp. 3042-3050
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 52
    • 29044440663 scopus 로고    scopus 로고
    • Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions
    • Veiga, S., Y. Yuan, X. Li, N. C. Santos, G. Liu, and M. A. Castanho. 2005. Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions. Biochim. Biophys. Acta 1760:55-61.
    • (2005) Biochim. Biophys. Acta , vol.1760 , pp. 55-61
    • Veiga, S.1    Yuan, Y.2    Li, X.3    Santos, N.C.4    Liu, G.5    Castanho, M.A.6
  • 53
    • 0025169833 scopus 로고
    • Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly
    • Vennema, H., L. Heijnen, A. Zijderveld, M. C. Horzinek, and W. J. Spaan. 1990. Intracellular transport of recombinant coronavirus spike proteins: implications for virus assembly. J. Virol. 64:339-346.
    • (1990) J. Virol. , vol.64 , pp. 339-346
    • Vennema, H.1    Heijnen, L.2    Zijderveld, A.3    Horzinek, M.C.4    Spaan, W.J.5
  • 54
    • 0025375789 scopus 로고
    • Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions
    • Weismiller, D. G., L. S. Sturman, M. J. Buchmeier, J. O. Fleming, and K. V. Holmes. 1990. Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions. J. Virol. 64:3051-3055.
    • (1990) J. Virol. , vol.64 , pp. 3051-3055
    • Weismiller, D.G.1    Sturman, L.S.2    Buchmeier, M.J.3    Fleming, J.O.4    Holmes, K.V.5
  • 55
    • 29144451985 scopus 로고    scopus 로고
    • Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus
    • Weiss, S. R., and S. Navas-Martin. 2005. Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus. Microbiol. Mol. Biol. Rev. 69:635-664.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 635-664
    • Weiss, S.R.1    Navas-Martin, S.2
  • 57
    • 0037223630 scopus 로고    scopus 로고
    • Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAM1 receptors or by pH 8
    • Zelus, B. D., J. H. Schickli, D. M. Blau, S. R. Weiss, and K. V. Holmes. 2003. Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAM1 receptors or by pH 8. J. Virol. 77:830-840.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.