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Volumn 88, Issue 7, 2007, Pages 1859-1865

Proteolytic cleavage of glycoprotein B is dispensable for in vitro replication, but required for syncytium formation of pseudorabies virus

Author keywords

[No Author keywords available]

Indexed keywords

FURIN; GLYCOPROTEIN B; VIRUS PROTEIN;

EID: 34347329338     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.82610-0     Document Type: Article
Times cited : (20)

References (39)
  • 1
    • 0034732314 scopus 로고    scopus 로고
    • Glycoprotein B of human herpesvirus 8 is a component of the virion in a cleaved form composed of amino- and carboxyl-terminal fragments
    • Baghian, A., Luftig, M., Black, J. B., Meng, Y. X., Pau, C. P., Voss, T., Pellett, P. E. & Kousoulas, K. G. (2000). Glycoprotein B of human herpesvirus 8 is a component of the virion in a cleaved form composed of amino- and carboxyl-terminal fragments. Virology 269, 18-25.
    • (2000) Virology , vol.269 , pp. 18-25
    • Baghian, A.1    Luftig, M.2    Black, J.B.3    Meng, Y.X.4    Pau, C.P.5    Voss, T.6    Pellett, P.E.7    Kousoulas, K.G.8
  • 2
    • 0001049622 scopus 로고
    • Molecular biology of pseudorabies virus
    • Edited by B. Roizman. New York, NY: Plenum Publishing Corp
    • Ben-Porat, T. & Kaplan, A. S. (1985). Molecular biology of pseudorabies virus. In The Herpesviruses, pp. 105-173. Edited by B. Roizman. New York, NY: Plenum Publishing Corp.
    • (1985) The Herpesviruses , pp. 105-173
    • Ben-Porat, T.1    Kaplan, A.S.2
  • 3
    • 0024585227 scopus 로고
    • Processing of the gp55/116 envelope glycoprotein complex (gB) of human cytomegalovirus
    • Britt, W. J. & Vugler, L. G. (1989). Processing of the gp55/116 envelope glycoprotein complex (gB) of human cytomegalovirus. J Virol 63, 403-410.
    • (1989) J Virol , vol.63 , pp. 403-410
    • Britt, W.J.1    Vugler, L.G.2
  • 4
    • 0021165912 scopus 로고
    • Nucleotide sequence of a region of the herpes simplex virus type 1 gB glycoprotein gene: Mutations affecting rate of virus entry and cell fusion
    • Bzik, D. J., Fox, B. A., DeLuca, N. A. & Person, S. (1984). Nucleotide sequence of a region of the herpes simplex virus type 1 gB glycoprotein gene: mutations affecting rate of virus entry and cell fusion. Virology 137, 185-190.
    • (1984) Virology , vol.137 , pp. 185-190
    • Bzik, D.J.1    Fox, B.A.2    DeLuca, N.A.3    Person, S.4
  • 5
    • 0023037932 scopus 로고
    • Oligomerization of herpes simplex virus glycoprotein B
    • Claesson-Welsh, L. & Spear, P. G. (1986). Oligomerization of herpes simplex virus glycoprotein B. J Virol 60, 803-806.
    • (1986) J Virol , vol.60 , pp. 803-806
    • Claesson-Welsh, L.1    Spear, P.G.2
  • 6
    • 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, C. A., Stadler, K., Godeke, G. J., Bosch, B. J. & Rottier, P. J. (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.
    • (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
  • 7
    • 0023115697 scopus 로고
    • Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB
    • Gong, M., Ooka, T., Matsuo, T. & Kieff, E. (1987). Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J Virol 61, 499-508.
    • (1987) J Virol , vol.61 , pp. 499-508
    • Gong, M.1    Ooka, T.2    Matsuo, T.3    Kieff, E.4
  • 8
  • 9
    • 0002547043 scopus 로고
    • Immunoaffinity purification
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Harlow, E. & Lane, D. (1988). Immunoaffinity purification. In Antibodies: a Laboratory Manual, pp. 511-552. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1988) Antibodies: A Laboratory Manual , pp. 511-552
    • Harlow, E.1    Lane, D.2
  • 12
    • 0016679968 scopus 로고
    • Activation of influenza A viruses by trypsin treatment
    • Klenk, H. D., Rott, R., Orlich, M. & Blodorn, J. (1975). Activation of influenza A viruses by trypsin treatment. Virology 68, 426-443.
    • (1975) Virology , vol.68 , pp. 426-443
    • Klenk, H.D.1    Rott, R.2    Orlich, M.3    Blodorn, J.4
  • 13
    • 0026549162 scopus 로고
    • Identification and characterization of pseudorabies virus glycoprotein H
    • Klupp, B. G., Visser, N. & Mettenleiter, T. C. (1992). Identification and characterization of pseudorabies virus glycoprotein H. J Virol 66, 3048-3055.
    • (1992) J Virol , vol.66 , pp. 3048-3055
    • Klupp, B.G.1    Visser, N.2    Mettenleiter, T.C.3
  • 14
    • 0033928392 scopus 로고    scopus 로고
    • Pseudorabies virus glycoprotein M inhibits membrane fusion
    • Klupp, B. G., Nixdorf, R. & Mettenleiter, T. C. (2000). Pseudorabies virus glycoprotein M inhibits membrane fusion. J Virol 74, 6760-6768.
    • (2000) J Virol , vol.74 , pp. 6760-6768
    • Klupp, B.G.1    Nixdorf, R.2    Mettenleiter, T.C.3
  • 15
    • 0028118515 scopus 로고
    • Proteolytic cleavage of bovine herpesvirus 1 (BHV-1) glycoprotein gB is not necessary for its function in BHV-1 or pseudorabies virus
    • Kopp, A., Blewett, E., Misra, V. & Mettenleiter, T. C. (1994). Proteolytic cleavage of bovine herpesvirus 1 (BHV-1) glycoprotein gB is not necessary for its function in BHV-1 or pseudorabies virus. J Virol 68, 1667-1674.
    • (1994) J Virol , vol.68 , pp. 1667-1674
    • Kopp, A.1    Blewett, E.2    Misra, V.3    Mettenleiter, T.C.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0024599232 scopus 로고
    • Identification of the gB homologues of equine herpesvirus types 1 and 4 as disulphide-linked heterodimers and their characterization using monoclonal antibodies
    • Meredith, D. M., Stocks, J. M., Whittaker, G. R., Halliburton, I. W., Snowden, B. W. & Killington, R. A. (1989). Identification of the gB homologues of equine herpesvirus types 1 and 4 as disulphide-linked heterodimers and their characterization using monoclonal antibodies. J Gen Virol 70, 1161-1172.
    • (1989) J Gen Virol , vol.70 , pp. 1161-1172
    • Meredith, D.M.1    Stocks, J.M.2    Whittaker, G.R.3    Halliburton, I.W.4    Snowden, B.W.5    Killington, R.A.6
  • 18
    • 0028156738 scopus 로고
    • Glycoprotein gB (gII) of pseudorabies virus can functionally substitute for glycoprotein gB in herpes simplex virus type 1
    • Mettenleiter, T. C. & Spear, P. G. (1994). Glycoprotein gB (gII) of pseudorabies virus can functionally substitute for glycoprotein gB in herpes simplex virus type 1. J Virol 68, 500-504.
    • (1994) J Virol , vol.68 , pp. 500-504
    • Mettenleiter, T.C.1    Spear, P.G.2
  • 19
    • 0017276239 scopus 로고
    • Studies on the assembly of the envelope of Newcastle disease virus
    • Nagai, Y., Ogura, H. & Klenk, H. (1976). Studies on the assembly of the envelope of Newcastle disease virus. Virology 69, 523-538.
    • (1976) Virology , vol.69 , pp. 523-538
    • Nagai, Y.1    Ogura, H.2    Klenk, H.3
  • 20
    • 4043156357 scopus 로고    scopus 로고
    • A synthetic peptide from a heptad repeat region of herpesvirus glycoprotein B inhibits virus replication
    • Okazaki, K. & Kida, H. (2004). A synthetic peptide from a heptad repeat region of herpesvirus glycoprotein B inhibits virus replication. J Gen Virol 85, 2131-2137.
    • (2004) J Gen Virol , vol.85 , pp. 2131-2137
    • Okazaki, K.1    Kida, H.2
  • 21
    • 0022641766 scopus 로고
    • Mechanisms of neutralization by monoclonal antibodies to different antigenic sites on the bovine herpesvirus type 1 glycoproteins
    • Okazaki, K., Honda, E., Minetoma, T. & Kumagai, T. (1986). Mechanisms of neutralization by monoclonal antibodies to different antigenic sites on the bovine herpesvirus type 1 glycoproteins. Virology 150, 260-264.
    • (1986) Virology , vol.150 , pp. 260-264
    • Okazaki, K.1    Honda, E.2    Minetoma, T.3    Kumagai, T.4
  • 22
    • 0023231163 scopus 로고
    • Intracellular localization and transport of three different bovine herpes-virus type 1 glycoproteins involved in neutralization
    • Okazaki, K., Honda, E., Minetoma, T. & Kumagai, T. (1987). Intracellular localization and transport of three different bovine herpes-virus type 1 glycoproteins involved in neutralization. Arch Viral 92, 17-26.
    • (1987) Arch Viral , vol.92 , pp. 17-26
    • Okazaki, K.1    Honda, E.2    Minetoma, T.3    Kumagai, T.4
  • 23
    • 0025503782 scopus 로고
    • The immunodominant glycoprotein complex of equid herpesvirus 1 (EHV-1) and the counterpart of EHV-4
    • Okazaki, K., Kumagai, T., Honda, E. & Okazaki, K. (1990). The immunodominant glycoprotein complex of equid herpesvirus 1 (EHV-1) and the counterpart of EHV-4. Nippon Juigaku Zasshi 52, 1127-1130.
    • (1990) Nippon Juigaku Zasshi , vol.52 , pp. 1127-1130
    • Okazaki, K.1    Kumagai, T.2    Honda, E.3    Okazaki, K.4
  • 24
    • 0025847026 scopus 로고
    • BHV-1 adsorption is mediated by the interaction of glycoprotein gIII with heparinlike moiety on the cell surface
    • Okazaki, K., Matsuzaki, T., Sugahara, Y., Okada, J., Hasebe, K., Iwamura, Y., Ohnishi, M., Kanno, T., Shimizu, M. & other authors (1991). BHV-1 adsorption is mediated by the interaction of glycoprotein gIII with heparinlike moiety on the cell surface. Virology 181, 666-670.
    • (1991) Virology , vol.181 , pp. 666-670
    • Okazaki, K.1    Matsuzaki, T.2    Sugahara, Y.3    Okada, J.4    Hasebe, K.5    Iwamura, Y.6    Ohnishi, M.7    Kanno, T.8    Shimizu, M.9
  • 25
    • 0027195006 scopus 로고
    • Hemadsorptive activity of transfected COS-7 cells expressing BHV-1 glycoprotein gIII
    • Okazaki, K., Kanno, T., Honda, E. & Kono, Y. (1993). Hemadsorptive activity of transfected COS-7 cells expressing BHV-1 glycoprotein gIII. Virology 193, 1024-1027.
    • (1993) Virology , vol.193 , pp. 1024-1027
    • Okazaki, K.1    Kanno, T.2    Honda, E.3    Kono, Y.4
  • 26
    • 0028196642 scopus 로고
    • Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2
    • Ortmann, D., Ohuchi, M., Angliker, H., Shaw, E., Garten, W. & Klenk, H. D. (1994). Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2. J Virol 68, 2772-2776.
    • (1994) J Virol , vol.68 , pp. 2772-2776
    • Ortmann, D.1    Ohuchi, M.2    Angliker, H.3    Shaw, E.4    Garten, W.5    Klenk, H.D.6
  • 27
    • 0026072796 scopus 로고
    • Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration
    • Rauh, I. & Mettenleiter, T. C. (1991). Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration. J Virol 65, 5348-5356.
    • (1991) J Virol , vol.65 , pp. 5348-5356
    • Rauh, I.1    Mettenleiter, T.C.2
  • 28
    • 31944439998 scopus 로고    scopus 로고
    • Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection
    • Richards, R. M., Douglas, L. R., Schiller, I. T. & Day, P. M. (2006). Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection. Proc Natl Acad Sci U S A 105, 1522-1527.
    • (2006) Proc Natl Acad Sci U S A , vol.105 , pp. 1522-1527
    • Richards, R.M.1    Douglas, L.R.2    Schiller, I.T.3    Day, P.M.4
  • 29
    • 0024375380 scopus 로고
    • Nucleotide sequence and characterization of the Marek's disease virus homologue of glycoprotein B of herpes simplex virus
    • Ross, L. J., Sanderson, M., Scott, S. D., Binns, M. M., Doel, T. & Milne, B. (1989). Nucleotide sequence and characterization of the Marek's disease virus homologue of glycoprotein B of herpes simplex virus. J Gen Virol 70, 1789-1804.
    • (1989) J Gen Virol , vol.70 , pp. 1789-1804
    • Ross, L.J.1    Sanderson, M.2    Scott, S.D.3    Binns, M.M.4    Doel, T.5    Milne, B.6
  • 30
    • 0036145340 scopus 로고    scopus 로고
    • Proteolytic processing of human cytomegalovirus glycoprotein B is dispensable for viral growth in culture
    • Strive, T., Borst, E., Messerle, M. & Radsak, K. (2002). Proteolytic processing of human cytomegalovirus glycoprotein B is dispensable for viral growth in culture. J Virol 76, 1252-1264.
    • (2002) J Virol , vol.76 , pp. 1252-1264
    • Strive, T.1    Borst, E.2    Messerle, M.3    Radsak, K.4
  • 32
    • 0031963977 scopus 로고    scopus 로고
    • Glycoproteins gB, gD, and gH/gL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system
    • Turner, A., Bruun, B., Minson, T. & Browne, H. (1998). Glycoproteins gB, gD, and gH/gL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system. J Virol 72, 873-875.
    • (1998) J Virol , vol.72 , pp. 873-875
    • Turner, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 33
    • 0022481619 scopus 로고    scopus 로고
    • van Drunen Littel-van den Hurk, S.& Babiuk, L. A. (1986). Synthesis and processing of bovine herpesvirus 1 glycoproteins. J Virol 59, 401-410.
    • van Drunen Littel-van den Hurk, S.& Babiuk, L. A. (1986). Synthesis and processing of bovine herpesvirus 1 glycoproteins. J Virol 59, 401-410.
  • 34
    • 0028801453 scopus 로고
    • Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin
    • Vey, M., Schafer, W., Reis, B., Ohuchi, R., Britt, W., Garten, W., Klenk, H. D. & Radsak, K. (1995). Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin. Virology 206, 746-749.
    • (1995) Virology , vol.206 , pp. 746-749
    • Vey, M.1    Schafer, W.2    Reis, B.3    Ohuchi, R.4    Britt, W.5    Garten, W.6    Klenk, H.D.7    Radsak, K.8
  • 35
    • 0032510732 scopus 로고    scopus 로고
    • Processing of the Ebola virus glycoprotein by the proprotein convertase furin
    • Volchkov, V. E., Feldmann, H., Volchkova, V. A. & Klenk, H. D. (1998). Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc Natl Acad Sci U S A 95, 5762-5767.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5762-5767
    • Volchkov, V.E.1    Feldmann, H.2    Volchkova, V.A.3    Klenk, H.D.4
  • 36
    • 0025269950 scopus 로고
    • The export pathway of the pseudorabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the Golgi apparatus
    • Whealy, M. E., Robbins, A. K. & Enquist, L. W. (1990). The export pathway of the pseudorabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the Golgi apparatus. J Virol 64, 1946-1955.
    • (1990) J Virol , vol.64 , pp. 1946-1955
    • Whealy, M.E.1    Robbins, A.K.2    Enquist, L.W.3
  • 37
    • 0026083301 scopus 로고
    • Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egresss
    • Whealy, M. E., Card, J. P., Meade, R. P., Robbins, A. K. & Enquist, L. W. (1991). Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egresss. J Virol 65, 1066-1081.
    • (1991) J Virol , vol.65 , pp. 1066-1081
    • Whealy, M.E.1    Card, J.P.2    Meade, R.P.3    Robbins, A.K.4    Enquist, L.W.5
  • 39
    • 0037369080 scopus 로고    scopus 로고
    • Furin processing and proteolytic activation of Semliki Forest virus
    • Zhang, X., Fugere, M., Day, R. & Kielian, M. (2003). Furin processing and proteolytic activation of Semliki Forest virus. J Virol 77, 2981-2989.
    • (2003) J Virol , vol.77 , pp. 2981-2989
    • Zhang, X.1    Fugere, M.2    Day, R.3    Kielian, M.4


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