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Volumn 80, Issue 1, 2006, Pages 514-525

Crimean-Congo hemorrhagic fever virus glycoprotein precursor is cleaved by furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; FURIN; GLYCOPROTEIN; GLYCOPROTEIN GC; GLYCOPROTEIN GN; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 38; GLYCOPROTEIN GP 85; MUCIN; PROPROTEIN CONVERTASE 1; PROTEIN PRECURSOR; PROTEINASE; SKI 1 PROTEASE; UNCLASSIFIED DRUG;

EID: 33645967164     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.80.1.514-525.2006     Document Type: Article
Times cited : (106)

References (43)
  • 1
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • Barr, P. J. 1991. Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell 66:1-3.
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 2
    • 0035253151 scopus 로고    scopus 로고
    • Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: A comparative analysis with fluorogenic peptides
    • Basak, A., M. Zhong, J. S. Munzer, M. Chrétien, and N. G. Seidah. 2001. Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: a comparative analysis with fluorogenic peptides. Biochem. J. 353:537-545.
    • (2001) Biochem. J. , vol.353 , pp. 537-545
    • Basak, A.1    Zhong, M.2    Munzer, J.S.3    Chrétien, M.4    Seidah, N.G.5
  • 4
    • 0037372280 scopus 로고    scopus 로고
    • Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/SIP
    • Beyer, W. R., D. Pöpplau, W. Garten, D. von Laer, and O. Lenz. 2003. Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/SIP. J. Virol. 77:2866-2872.
    • (2003) J. Virol. , vol.77 , pp. 2866-2872
    • Beyer, W.R.1    Pöpplau, D.2    Garten, W.3    Von Laer, D.4    Lenz, O.5
  • 5
    • 0001142645 scopus 로고    scopus 로고
    • Arenaviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Buchmeier, M. J., M. D. Bowen, and C. J. Peters. 2001. Arenaviridae: the viruses and their replication, p. 1635-1668. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 2nd ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 2nd Ed. , pp. 1635-1668
    • Buchmeier, M.J.1    Bowen, M.D.2    Peters, C.J.3
  • 6
    • 0002244194 scopus 로고
    • Glycoproteins of the arenaviruses
    • M. S. Salvato (ed.). Plenum Press, New York, N.Y.
    • Burns, J. W., and M. J. Buchmeier. 1993. Glycoproteins of the arenaviruses, p. 17-35. In M. S. Salvato (ed.), The arenaviridae. Plenum Press, New York, N.Y.
    • (1993) The Arenaviridae , pp. 17-35
    • Burns, J.W.1    Buchmeier, M.J.2
  • 7
    • 0000768105 scopus 로고    scopus 로고
    • Respiratory syncytial virus
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Collins, P. L., R. M. Chanock, and B. R. Murphy. 2001. Respiratory syncytial virus, p. 1443-1485. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 2nd ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 2nd Ed. , pp. 1443-1485
    • Collins, P.L.1    Chanock, R.M.2    Murphy, B.R.3
  • 8
    • 0034703095 scopus 로고    scopus 로고
    • O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate
    • Comer, F. I., and G. W. Hart. 2000. O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J. Biol. Chem. 275:29179-29182.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29179-29182
    • Comer, F.I.1    Hart, G.W.2
  • 10
    • 0017725296 scopus 로고
    • Physicochemical characteristics, morphology and morphogenesis of virions of the causative agent of Crimean hemorrhagic fever
    • Donets, M. A., M. P. Chumakov, M. B., Korolev, and S. G. Rubin. 1977. Physicochemical characteristics, morphology and morphogenesis of virions of the causative agent of Crimean hemorrhagic fever. Intervirology 8:294-308.
    • (1977) Intervirology , vol.8 , pp. 294-308
    • Donets, M.A.1    Chumakov, M.P.2    Korolev, M.B.3    Rubin, S.G.4
  • 11
    • 0028246971 scopus 로고
    • Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein
    • Feldmann, H., S. T. Nichol, H.-D. Klenk, C. J. Peters, and A. Sanchez. 1994. Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein. Virology 199:469-473.
    • (1994) Virology , vol.199 , pp. 469-473
    • Feldmann, H.1    Nichol, S.T.2    Klenk, H.-D.3    Peters, C.J.4    Sanchez, A.5
  • 12
    • 0023199650 scopus 로고
    • The role of envelope glycoprotein processing in murine leukemia virus infection
    • Freed, E. O., and R. Risser. 1987. The role of envelope glycoprotein processing in murine leukemia virus infection. J. Virol. 9:2852-2856.
    • (1987) J. Virol. , vol.9 , pp. 2852-2856
    • Freed, E.O.1    Risser, R.2
  • 13
    • 15444371889 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of bunyaviruses are class II viral fusion protein (beta-penetrenes)
    • Garry, C. E., and R. F. Garry. 2004. Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of bunyaviruses are class II viral fusion protein (beta-penetrenes). Theor. Biol. Med. Model. 1:10.
    • (2004) Theor. Biol. Med. Model. , vol.1 , pp. 10
    • Garry, C.E.1    Garry, R.F.2
  • 14
    • 21944446444 scopus 로고    scopus 로고
    • Intracellular localization of Crimean-Congo hemorrhagic fever (CCHF) virus glycoproteins
    • Haferkamp, S., L. Fernando, T. F. Schwarz, H. Feldmann, and R. Flick. 2005. Intracellular localization of Crimean-Congo hemorrhagic fever (CCHF) virus glycoproteins. Virol. J. 2:42.
    • (2005) Virol. J. , vol.2 , pp. 42
    • Haferkamp, S.1    Fernando, L.2    Schwarz, T.F.3    Feldmann, H.4    Flick, R.5
  • 15
    • 0036670360 scopus 로고    scopus 로고
    • The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein
    • Huang, Y., L. Xu, Y. Sun, and G. J. Nabel. 2002. The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein. Mol. Cell 10:307-316.
    • (2002) Mol. Cell , vol.10 , pp. 307-316
    • Huang, Y.1    Xu, L.2    Sun, Y.3    Nabel, G.J.4
  • 16
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk, H.-D., and W. Garten. 1994. Host cell proteases controlling virus pathogenicity. Trends Microbiol. 2:39-43.
    • (1994) Trends Microbiol. , vol.2 , pp. 39-43
    • Klenk, H.-D.1    Garten, W.2
  • 17
    • 0035940409 scopus 로고    scopus 로고
    • The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
    • Lenz, O., J. ter Meulen, H.-D. Klenk, N. G. Seidah, and W. Garten. 2001. The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. Proc. Natl. Acad. Sci. USA 98:12701-12705.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12701-12705
    • Lenz, O.1    Ter Meulen, J.2    Klenk, H.-D.3    Seidah, N.G.4    Garten, W.5
  • 18
    • 0026739576 scopus 로고
    • Dugbe Nairovirus M RNA: Nucleotide sequence and coding strategy
    • Marriott, A. C., A. A. El-Ghorr, and P. A. Nuttall. 1992. Dugbe Nairovirus M RNA: nucleotide sequence and coding strategy. Virology 190:606-615.
    • (1992) Virology , vol.190 , pp. 606-615
    • Marriott, A.C.1    El-Ghorr, A.A.2    Nuttall, P.A.3
  • 19
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune, J. M., L. B. Rabin, M. B. Feinburg, M. Lieberman, J. C. Kosek, G. R. Reyes, and I. L. Weissman. 1988. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 53:55-67.
    • (1988) Cell , vol.53 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinburg, M.B.3    Lieberman, M.4    Kosek, J.C.5    Reyes, G.R.6    Weissman, I.L.7
  • 20
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama, K. 1997. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327:625-635.
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 21
    • 0036133094 scopus 로고    scopus 로고
    • Reverse genetics demonstrates that proteolytic processing of the Ebola virus glycoprotein is not essential for replication in cell culture
    • Neumann, G., H. Feldmann, S. Watanabe, I. Lulashevich, and Y. Kawaoka. 2002. Reverse genetics demonstrates that proteolytic processing of the Ebola virus glycoprotein is not essential for replication in cell culture. J. Virol. 76:406-410.
    • (2002) J. Virol. , vol.76 , pp. 406-410
    • Neumann, G.1    Feldmann, H.2    Watanabe, S.3    Lulashevich, I.4    Kawaoka, Y.5
  • 22
    • 0000004674 scopus 로고    scopus 로고
    • Bunyaviruses
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Nichol, S. T. 2001. Bunyaviruses, p. 1603-1633. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 2nd ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 2nd Ed. , pp. 1603-1633
    • Nichol, S.T.1
  • 23
    • 0000647125 scopus 로고    scopus 로고
    • Synthesis, assembly, and intracellular transport of Bunyaviridae membrane proteins
    • R. M. Elliot (ed.). Plenum Press, New York, N.Y.
    • Pettersson, R. F., and L. Melin. 1996. Synthesis, assembly, and intracellular transport of Bunyaviridae membrane proteins, p 159-188. In R. M. Elliot (ed.), The Bunyaviridae. Plenum Press, New York, N.Y.
    • (1996) The Bunyaviridae , pp. 159-188
    • Pettersson, R.F.1    Melin, L.2
  • 24
    • 0036631642 scopus 로고    scopus 로고
    • Characterization of the glycoproteins of Crimean-Congo hemorrhagic fever virus
    • Sanchez, A. J., M. J. Vincent, and S. T. Nichol. 2002. Characterization of the glycoproteins of Crimean-Congo hemorrhagic fever virus. J. Virol. 76:7263-7275.
    • (2002) J. Virol. , vol.76 , pp. 7263-7275
    • Sanchez, A.J.1    Vincent, M.J.2    Nichol, S.T.3
  • 25
    • 0036060893 scopus 로고    scopus 로고
    • The Marburg virus surface protein GP is phosphorylated at its ectodomain
    • Sänger, C., E. Mühlberger, B. Lötfering, H. D. Klenk, and S. Becker. 2002. The Marburg virus surface protein GP is phosphorylated at its ectodomain. Virology 295:20-29.
    • (2002) Virology , vol.295 , pp. 20-29
    • Sänger, C.1    Mühlberger, E.2    Lötfering, B.3    Klenk, H.D.4    Becker, S.5
  • 26
    • 0001424127 scopus 로고    scopus 로고
    • Bunyaviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Schmaljohn, C. S., and J. W. Hooper. 2001. Bunyaviridae: the viruses and their replication, p. 1581-1602. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 2nd ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 2nd Ed. , pp. 1581-1602
    • Schmaljohn, C.S.1    Hooper, J.W.2
  • 28
    • 0038394566 scopus 로고    scopus 로고
    • Precursor convertases in the secretory pathway, cytosol and extracellular milieu
    • Seidah, N. G., and A. Prat. 2002. Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem. 38:79-94.
    • (2002) Essays Biochem. , vol.38 , pp. 79-94
    • Seidah, N.G.1    Prat, A.2
  • 29
    • 0036171135 scopus 로고    scopus 로고
    • Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence
    • Simmons, G., R. J. Wool-Lewis, F. Baribaud, R. C. Netter, and P. Bates. 2002. Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. J. Virol. 76:2518-2528.
    • (2002) J. Virol. , vol.76 , pp. 2518-2528
    • Simmons, G.1    Wool-Lewis, R.J.2    Baribaud, F.3    Netter, R.C.4    Bates, P.5
  • 30
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler, K., S. L. Allison, J. Schalich, and F. X. Heinz. 1997. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71:8475-8481.
    • (1997) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 31
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multi-basic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Grober, A., M. Vey, H. Angliker, E. Shaw, G. Thomas, C. Roberts, H.-D. Klenk, and W. Garten. 1992. Influenza virus hemagglutinin with multi-basic 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    Roberts, C.6    Klenk, H.-D.7    Garten, W.8
  • 32
    • 0030059770 scopus 로고    scopus 로고
    • Molecular cloning and expression of cDNA encoding human macrophage C-type lectin
    • Suzuki, N., K. Yamamoto, S. Toyoshima, T. Osawa, and T. Irimura. 1996. Molecular cloning and expression of cDNA encoding human macrophage C-type lectin. J. Immunol. 156:128-135.
    • (1996) J. Immunol. , vol.156 , pp. 128-135
    • Suzuki, N.1    Yamamoto, K.2    Toyoshima, S.3    Osawa, T.4    Irimura, T.5
  • 35
    • 0032510732 scopus 로고    scopus 로고
    • Processing of the Ebola virus glycoprotein by the proprotein convertase furin
    • Volchkov, V. E., H. Feldmann, V. A. Volchkova, and H. D. Klenk. 1998. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc. Natl. Acad. Sci. USA 95:5762-5767.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5762-5767
    • Volchkov, V.E.1    Feldmann, H.2    Volchkova, V.A.3    Klenk, H.D.4
  • 37
    • 0033527892 scopus 로고    scopus 로고
    • Delta-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus
    • Volchkova, V. A., H.-D. Klenk, and V. E. Volchkov. 1999. Delta-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus. Virology 265:164-171.
    • (1999) Virology , vol.265 , pp. 164-171
    • Volchkova, V.A.1    Klenk, H.-D.2    Volchkov, V.E.3
  • 38
    • 0029868289 scopus 로고    scopus 로고
    • Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases
    • Vollenweider, F., S. Benjannet, E. Decroly, D. Savaria, C. Lazure, G. Thomas, M. Chrétien, and N. G. Seidah. 1996. Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases. Biochem. J. 314:521-532.
    • (1996) Biochem. J. , vol.314 , pp. 521-532
    • Vollenweider, F.1    Benjannet, S.2    Decroly, E.3    Savaria, D.4    Lazure, C.5    Thomas, G.6    Chrétien, M.7    Seidah, N.G.8
  • 39
    • 0028960688 scopus 로고
    • Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe, M., A. Hirano, S. Stenglein, J. Nelson, G. Thomas, and T. C. Wong. 1995. Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J. Virol. 69:3206-3210.
    • (1995) J. Virol. , vol.69 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3    Nelson, J.4    Thomas, G.5    Wong, T.C.6
  • 40
    • 0024439334 scopus 로고
    • Structure and cell surface maturation of the attachment glycoprotein of human respiratory syncytial virus in a cell line deficient in O glycosylation
    • Wertz, G. W., M. Krieger, and L. A. Ball. 1989. Structure and cell surface maturation of the attachment glycoprotein of human respiratory syncytial virus in a cell line deficient in O glycosylation. J. Virol. 63:4767-4776.
    • (1989) J. Virol. , vol.63 , pp. 4767-4776
    • Wertz, G.W.1    Krieger, M.2    Ball, L.A.3
  • 41
    • 0032949982 scopus 로고    scopus 로고
    • Endoproteolytic processing of the Ebola virus envelope glycoprotein: Cleavage is not required for function
    • Wool-Lewis, R. J., and P. Bates. 1999. Endoproteolytic processing of the Ebola virus envelope glycoprotein: cleavage is not required for function. J. Virol. 73:1419-1426.
    • (1999) J. Virol. , vol.73 , pp. 1419-1426
    • Wool-Lewis, R.J.1    Bates, P.2
  • 42
    • 0032512668 scopus 로고    scopus 로고
    • Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins
    • Yang, Z.-Y., R. Delgado, L. Xu, R. F. Todd, E. G. Nabel, A. Sanchez, and G. J. Nabel. 1998. Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins. Science 279:1034-1037.
    • (1998) Science , vol.279 , pp. 1034-1037
    • Yang, Z.-Y.1    Delgado, R.2    Xu, L.3    Todd, R.F.4    Nabel, E.G.5    Sanchez, A.6    Nabel, G.J.7
  • 43
    • 0033831191 scopus 로고    scopus 로고
    • Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury
    • Yang, Z.-Y., H. J. Duckers, N. J. Sullivan, A. Sanchez, E. G. Nabel, and G. J. Nabel. 2000. Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Nature Med. 6:886-889.
    • (2000) Nature Med. , vol.6 , pp. 886-889
    • Yang, Z.-Y.1    Duckers, H.J.2    Sullivan, N.J.3    Sanchez, A.4    Nabel, E.G.5    Nabel, G.J.6


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