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Volumn 251, Issue 2, 1998, Pages 402-413

Human herpesvirus-8 glycoprotein B interacts with Epstein-Barr virus (EBV) glycoprotein 110 but fails to complement the infectivity of EBV mutants

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS GLYCOPROTEIN;

EID: 0032567118     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9412     Document Type: Article
Times cited : (20)

References (85)
  • 1
    • 0028016066 scopus 로고
    • Comparative studies of the structural proteins and glycoproteins of equine herpesviruses 2 and 5
    • Agius C. T., Crabb B. S., Telford E. A. R., Davison A. J., Studdert M. J. Comparative studies of the structural proteins and glycoproteins of equine herpesviruses 2 and 5. J. Gen. Virol. 75:1994;2707-2717.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2707-2717
    • Agius, C.T.1    Crabb, B.S.2    Telford, E.A.R.3    Davison, A.J.4    Studdert, M.J.5
  • 3
    • 0020484234 scopus 로고
    • Structural prediction of membrane bound proteins
    • Argos P., Rao J. K. N., Hargrave P. A. Structural prediction of membrane bound proteins. Eur. J. Biochem. 128:1982;565-575.
    • (1982) Eur. J. Biochem. , vol.128 , pp. 565-575
    • Argos, P.1    Rao, J.K.N.2    Hargrave, P.A.3
  • 5
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem. J. 209:1983;331-336.
    • (1983) Biochem. J. , vol.209 , pp. 331-336
    • Bause, E.1
  • 6
    • 0031910646 scopus 로고    scopus 로고
    • Receptor-binding properties of a soluble form of human cytomegalovirus glycoprotein B
    • Boyle K., Compton T. Receptor-binding properties of a soluble form of human cytomegalovirus glycoprotein B. J. Virol. 72:1998;1826-1833.
    • (1998) J. Virol. , vol.72 , pp. 1826-1833
    • Boyle, K.1    Compton, T.2
  • 7
    • 0021215460 scopus 로고
    • Neutralizing antibodies detect a disulfide-linked glycoprotein complex within the envelope of human cytomegalovirus
    • Britt W. J. Neutralizing antibodies detect a disulfide-linked glycoprotein complex within the envelope of human cytomegalovirus. Virology. 135:1984;369-378.
    • (1984) Virology , vol.135 , pp. 369-378
    • Britt, W.J.1
  • 8
    • 0024585227 scopus 로고
    • Processing of the gp55-116 envelope glycoprotein complex (gB) of human cytomegalovirus
    • Britt W. J., Vugler L. G. Processing of the gp55-116 envelope glycoprotein complex (gB) of human cytomegalovirus. J. Virol. 63:1989;403-410.
    • (1989) J. Virol. , vol.63 , pp. 403-410
    • Britt, W.J.1    Vugler, L.G.2
  • 9
    • 0025119284 scopus 로고
    • Inhibition of endoproteolytic cleavage of cytomegalovirus (HCMV) glycoprotein B by palmitoyl-peptidyl-chloromethyl ketone
    • Brücher K. H., Garten W., Klenk H. D., Shaw E., Radsak K. Inhibition of endoproteolytic cleavage of cytomegalovirus (HCMV) glycoprotein B by palmitoyl-peptidyl-chloromethyl ketone. Virology. 178:1990;617-620.
    • (1990) Virology , vol.178 , pp. 617-620
    • Brücher, K.H.1    Garten, W.2    Klenk, H.D.3    Shaw, E.4    Radsak, K.5
  • 10
    • 0021340187 scopus 로고
    • Nucleotide sequence specifying the glycoprotein gene, gB, of herpes simplex virus type 1
    • Bzik D. J., Fox B. A., DeLuca N. A., Person S. Nucleotide sequence specifying the glycoprotein gene, gB, of herpes simplex virus type 1. Virology. 133:1984;301-314.
    • (1984) Virology , vol.133 , pp. 301-314
    • Bzik, D.J.1    Fox, B.A.2    Deluca, N.A.3    Person, S.4
  • 11
    • 0023705653 scopus 로고
    • Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion
    • Cai W., Gu B., Person S. Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. J. Virol. 62:1988;2596-2604.
    • (1988) J. Virol. , vol.62 , pp. 2596-2604
    • Cai, W.1    Gu, B.2    Person, S.3
  • 12
    • 0023101293 scopus 로고
    • Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1
    • Cai W., Person S., Warner S. C., Zhou J., DeLuca N. A. Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1. J. Virol. 61:1987;714-721.
    • (1987) J. Virol. , vol.61 , pp. 714-721
    • Cai, W.1    Person, S.2    Warner, S.C.3    Zhou, J.4    Deluca, N.A.5
  • 13
    • 0023037932 scopus 로고
    • Oligomerization of herpes simplex virus glycoprotein B
    • Claesson-Welsh L., Spear P. G. Oligomerization of herpes simplex virus glycoprotein B. J. Virol. 60:1986;803-806.
    • (1986) J. Virol. , vol.60 , pp. 803-806
    • Claesson-Welsh, L.1    Spear, P.G.2
  • 14
    • 0027315907 scopus 로고
    • Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate
    • Compton T., Nowlin D. M., Cooper N. R. Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate. Virology. 193:1993;834-841.
    • (1993) Virology , vol.193 , pp. 834-841
    • Compton, T.1    Nowlin, D.M.2    Cooper, N.R.3
  • 15
    • 0002275937 scopus 로고
    • Early events in human herpesvirus infection of cells
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press. p. 365-388
    • Cooper N. R. Early events in human herpesvirus infection of cells. Cellular Receptors for Animal Viruses. 1994;Cold Spring Harbor Laboratory Press, Cold Spring Harbor. p. 365-388.
    • (1994) Cellular Receptors for Animal Viruses
    • Cooper, N.R.1
  • 16
    • 0023100479 scopus 로고
    • Identification of an Epstein-Barr virus glycoprotein which is antigenically homologous to the varicella-zoster virus glycoprotein II and the herpes simplex virus glycoprotein B
    • Emini E. A., Luka J., Armstrong M. E., Keller P. M., Ellis R. W., Pearson G. R. Identification of an Epstein-Barr virus glycoprotein which is antigenically homologous to the varicella-zoster virus glycoprotein II and the herpes simplex virus glycoprotein B. Virology. 157:1987;552-555.
    • (1987) Virology , vol.157 , pp. 552-555
    • Emini, E.A.1    Luka, J.2    Armstrong, M.E.3    Keller, P.M.4    Ellis, R.W.5    Pearson, G.R.6
  • 17
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel Y., von Heijne G. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng. 3:1990;433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 18
    • 0028063228 scopus 로고
    • Glycoprotein B of bovine herpesvirus 4: Its phylogenetic relationship to gB equivalents of the herpesviruses
    • Goltz M., Broll H., Mankertz A., Weigelt W., Ludwig H., Buhk H.-J., Borchers K. Glycoprotein B of bovine herpesvirus 4: Its phylogenetic relationship to gB equivalents of the herpesviruses. Virus Genes. 9:1994;53-59.
    • (1994) Virus Genes , vol.9 , pp. 53-59
    • Goltz, M.1    Broll, H.2    Mankertz, A.3    Weigelt, W.4    Ludwig, H.5    Buhk, H.-J.6    Borchers, K.7
  • 19
    • 0025218465 scopus 로고
    • Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110
    • Gong M., Kieff E. Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. J. Virol. 64:1990;1507-1516.
    • (1990) J. Virol. , vol.64 , pp. 1507-1516
    • Gong, M.1    Kieff, E.2
  • 20
    • 0023115697 scopus 로고
    • Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB
    • Gong M., Ooka T., Matsuo T., Kieff E. Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J. Virol. 61:1987;499-508.
    • (1987) J. Virol. , vol.61 , pp. 499-508
    • Gong, M.1    Ooka, T.2    Matsuo, T.3    Kieff, E.4
  • 21
    • 0023830099 scopus 로고
    • Identification and characterization of three distinct families of glycoprotein complexes in the envelopes of human cytomegalovirus
    • Gretch D. R., Kari B., Rasmussen L., Gehrz R. C., Stinski M. F. Identification and characterization of three distinct families of glycoprotein complexes in the envelopes of human cytomegalovirus. J. Virol. 62:1988;875-881.
    • (1988) J. Virol. , vol.62 , pp. 875-881
    • Gretch, D.R.1    Kari, B.2    Rasmussen, L.3    Gehrz, R.C.4    Stinski, M.F.5
  • 22
    • 0021337660 scopus 로고
    • Varicella-zoster virus-specific gp140: A highly immunogenic and disulfide-linked structural glycoprotein
    • Grose C., Edwards D. P., Weigle K. A., Friedrichs W. E., McGuire W. L. Varicella-zoster virus-specific gp140: A highly immunogenic and disulfide-linked structural glycoprotein. Virology. 132:1984;138-146.
    • (1984) Virology , vol.132 , pp. 138-146
    • Grose, C.1    Edwards, D.P.2    Weigle, K.A.3    Friedrichs, W.E.4    McGuire, W.L.5
  • 23
    • 0024417154 scopus 로고
    • Depletion of glycoprotein gp85 from virosomes made with Epstein-Barr virus proteins abolishes their ability to fuse with virus receptor-bearing cells
    • Haddad R. S., Hutt-Fletcher L. M. Depletion of glycoprotein gp85 from virosomes made with Epstein-Barr virus proteins abolishes their ability to fuse with virus receptor-bearing cells. J. Virol. 63:1989;4998-5005.
    • (1989) J. Virol. , vol.63 , pp. 4998-5005
    • Haddad, R.S.1    Hutt-Fletcher, L.M.2
  • 24
    • 0018858691 scopus 로고
    • Alterations in glycoprotein gB specified by mutants and their partial revertants in herpes simplex virus type 1 and relationship to other mutant phenotypes
    • Haffey M. L., Spear P. G. Alterations in glycoprotein gB specified by mutants and their partial revertants in herpes simplex virus type 1 and relationship to other mutant phenotypes. J. Virol. 35:1980;114-128.
    • (1980) J. Virol. , vol.35 , pp. 114-128
    • Haffey, M.L.1    Spear, P.G.2
  • 25
    • 0023834891 scopus 로고
    • Identification of the Epstein-Barr virus gp85 gene
    • Heineman T., Gong M., Sample J., Kieff E. Identification of the Epstein-Barr virus gp85 gene. J. Virol. 62:1988;1101-1107.
    • (1988) J. Virol. , vol.62 , pp. 1101-1107
    • Heineman, T.1    Gong, M.2    Sample, J.3    Kieff, E.4
  • 26
    • 0028236443 scopus 로고
    • Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B
    • Herold B. C., Visalli R. J., Susmarski N., Brandt C. R., Spear P. G. Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B. J. Gen. Virol. 75:1994;1211-1222.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1211-1222
    • Herold, B.C.1    Visalli, R.J.2    Susmarski, N.3    Brandt, C.R.4    Spear, P.G.5
  • 27
    • 0026026623 scopus 로고
    • Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity
    • Herold B. C., WuDunn D., Soltys N., Spear P. G. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 65:1991;1090-1098.
    • (1991) J. Virol. , vol.65 , pp. 1090-1098
    • Herold, B.C.1    Wudunn, D.2    Soltys, N.3    Spear, P.G.4
  • 28
    • 0030026762 scopus 로고    scopus 로고
    • Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo
    • Herrold R. E., Marchini A., Fruehling S., Longnecker R. Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo. J. Virol. 70:1996;2049-2054.
    • (1996) J. Virol. , vol.70 , pp. 2049-2054
    • Herrold, R.E.1    Marchini, A.2    Fruehling, S.3    Longnecker, R.4
  • 30
    • 0030923359 scopus 로고    scopus 로고
    • Characterization of a novel third member of the human cytomegalovirus glycoprotein H-glycoprotein L complex
    • Huber M. T., Compton T. Characterization of a novel third member of the human cytomegalovirus glycoprotein H-glycoprotein L complex. J. Virol. 71:1997;5391-5398.
    • (1997) J. Virol. , vol.71 , pp. 5391-5398
    • Huber, M.T.1    Compton, T.2
  • 31
    • 0002424866 scopus 로고
    • Epstein-Barr virus glycoproteins-Beyond gp350/220
    • Hutt-Fletcher L. M. Epstein-Barr virus glycoproteins-Beyond gp350/220. Epstein-Barr Virus Rep. 2:1995;49-53.
    • (1995) Epstein-Barr Virus Rep. , vol.2 , pp. 49-53
    • Hutt-Fletcher, L.M.1
  • 32
    • 0019918329 scopus 로고
    • Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells
    • Johnson D. C., Spear P. G. Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells. J. Virol. 43:1982;1102-1112.
    • (1982) J. Virol. , vol.43 , pp. 1102-1112
    • Johnson, D.C.1    Spear, P.G.2
  • 33
    • 0026590697 scopus 로고
    • A human cytomegalovirus glycoprotein complex designated gC-II is a major heparin-binding component of the envelope
    • Kari B., Gehrz R. A human cytomegalovirus glycoprotein complex designated gC-II is a major heparin-binding component of the envelope. J. Virol. 66:1992;1761-1764.
    • (1992) J. Virol. , vol.66 , pp. 1761-1764
    • Kari, B.1    Gehrz, R.2
  • 34
    • 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. Proteolytic cleavage of bovine herpesvirus 1 (BHV-1) glycoprotein gB is not necessary for its function in BHV-1 or pseudorabies virus. J. Virol. 68:1994;1667-1674.
    • (1994) J. Virol. , vol.68 , pp. 1667-1674
    • Kopp, A.1    Blewett, E.2    Misra, V.3    Mettenleiter, T.C.4
  • 35
    • 0026606722 scopus 로고
    • Stable rescue of a glycoprotein gII deletion mutant of pseudorabies virus by glycoprotein gI of bovine herpesvirus 1
    • Kopp A., Mettenleiter T. C. Stable rescue of a glycoprotein gII deletion mutant of pseudorabies virus by glycoprotein gI of bovine herpesvirus 1. J. Virol. 66:1992;2754-2762.
    • (1992) J. Virol. , vol.66 , pp. 2754-2762
    • Kopp, A.1    Mettenleiter, T.C.2
  • 36
    • 0030029920 scopus 로고    scopus 로고
    • Glycoprotein B of herpes simplex virus type 1 oligomerizes through the intermolecular interaction of a 28-amino-acid domain
    • Laquerre S., Person S., Glorioso J. C. Glycoprotein B of herpes simplex virus type 1 oligomerizes through the intermolecular interaction of a 28-amino-acid domain. J. Virol. 70:1996;1640-1650.
    • (1996) J. Virol. , vol.70 , pp. 1640-1650
    • Laquerre, S.1    Person, S.2    Glorioso, J.C.3
  • 37
    • 0030700579 scopus 로고    scopus 로고
    • Failure to complement infectivity of EBV and HSV-1 glycoprotein B (gB) deletion mutants with gBs from different human herpesvirus subfamilies
    • Lee S. K., Compton T., Longnecker R. Failure to complement infectivity of EBV and HSV-1 glycoprotein B (gB) deletion mutants with gBs from different human herpesvirus subfamilies. Virology. 237:1997;170-181.
    • (1997) Virology , vol.237 , pp. 170-181
    • Lee, S.K.1    Compton, T.2    Longnecker, R.3
  • 38
    • 0030935618 scopus 로고    scopus 로고
    • The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication
    • Lee S. K., Longnecker R. The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication. J. Virol. 71:1997;4092-4097.
    • (1997) J. Virol. , vol.71 , pp. 4092-4097
    • Lee, S.K.1    Longnecker, R.2
  • 39
    • 0030936130 scopus 로고    scopus 로고
    • Glycoprotein H-related complexes of human cytomegalovirus: Identification of a third protein in the gCIII complex
    • Li L., Nelson J. A., Britt W. J. Glycoprotein H-related complexes of human cytomegalovirus: Identification of a third protein in the gCIII complex. J. Virol. 71:1997;3090-3097.
    • (1997) J. Virol. , vol.71 , pp. 3090-3097
    • Li, L.1    Nelson, J.A.2    Britt, W.J.3
  • 40
    • 0029075614 scopus 로고
    • The Epstein-Barr virus (EBV) BZLF2 gene product associates with the gH and gL homologs of EBV and carries an epitope critical to infection of B cells but not of epithelial cells
    • Li Q., Turk S. M., Hutt-Fletcher L. M. The Epstein-Barr virus (EBV) BZLF2 gene product associates with the gH and gL homologs of EBV and carries an epitope critical to infection of B cells but not of epithelial cells. J. Virol. 69:1995;3987-3994.
    • (1995) J. Virol. , vol.69 , pp. 3987-3994
    • Li, Q.1    Turk, S.M.2    Hutt-Fletcher, L.M.3
  • 41
    • 0030938851 scopus 로고    scopus 로고
    • Glycoprotein B of bovine herpesvirus 4 is a major component of the virion, unlike that of two other gammaherpesviruses, Epstein-Barr virus and murine gammaherpesvirus 68
    • Lomonte P., Filee P., Lyaku J. R., Bublot M., Pastoret P.-P., Thiry E. Glycoprotein B of bovine herpesvirus 4 is a major component of the virion, unlike that of two other gammaherpesviruses, Epstein-Barr virus and murine gammaherpesvirus 68. J. Virol. 71:1997;3332-3335.
    • (1997) J. Virol. , vol.71 , pp. 3332-3335
    • Lomonte, P.1    Filee, P.2    Lyaku, J.R.3    Bublot, M.4    Pastoret, P.-P.5    Thiry, E.6
  • 42
    • 0021971623 scopus 로고
    • Demonstration of three major species of pseudorabies virus glycoproteins and identification of a disulfide-linked glycoprotein complex
    • Lukacs N., Thiel H.-J., Mettenleiter T. C., Rziha H.-J. Demonstration of three major species of pseudorabies virus glycoproteins and identification of a disulfide-linked glycoprotein complex. J. Virol. 53:1985;166-173.
    • (1985) J. Virol. , vol.53 , pp. 166-173
    • Lukacs, N.1    Thiel, H.-J.2    Mettenleiter, T.C.3    Rziha, H.-J.4
  • 43
    • 0017752692 scopus 로고
    • Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins
    • Manservigi R., Spear P. G., Buchan A. Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. Proc. Natl. Acad. Sci. USA. 74:1977;3913-3917.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3913-3917
    • Manservigi, R.1    Spear, P.G.2    Buchan, A.3
  • 45
    • 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. Glycoprotein gB (gII) of pseudorabies virus can functionally substitute for glycoprotein gB in herpes simplex virus type 1. J. Virol. 68:1994;500-504.
    • (1994) J. Virol. , vol.68 , pp. 500-504
    • Mettenleiter, T.C.1    Spear, P.G.2
  • 46
    • 0029062875 scopus 로고
    • Unidirectional complementation between glycoprotein B homologues of pseudorabies virus and bovine herpesvirus 1 is determined by the carboxy-terminal part of the molecule
    • Miethke A., Keil G. M., Weiland F., Mettenleiter T. C. Unidirectional complementation between glycoprotein B homologues of pseudorabies virus and bovine herpesvirus 1 is determined by the carboxy-terminal part of the molecule. J. Gen. Virol. 76:1995;1623-1635.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1623-1635
    • Miethke, A.1    Keil, G.M.2    Weiland, F.3    Mettenleiter, T.C.4
  • 47
    • 0023910419 scopus 로고
    • A monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein-Barr virus
    • Miller N., Hutt-Fletcher L. M. A monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein-Barr virus. J. Virol. 62:1988;2366-2372.
    • (1988) J. Virol. , vol.62 , pp. 2366-2372
    • Miller, N.1    Hutt-Fletcher, L.M.2
  • 48
    • 0026696312 scopus 로고
    • Epstein-Barr virus enters B cells and epithelial cells by different routes
    • Miller N., Hutt-Fletcher L. M. Epstein-Barr virus enters B cells and epithelial cells by different routes. J. Virol. 66:1992;3409-3414.
    • (1992) J. Virol. , vol.66 , pp. 3409-3414
    • Miller, N.1    Hutt-Fletcher, L.M.2
  • 49
    • 0026030070 scopus 로고
    • Construction of herpes simplex viruses that are pseudodiploid for the glycoprotein B gene: A strategy for studying the function of an essential herpesvirus gene
    • Misra V., Blewett E. L. Construction of herpes simplex viruses that are pseudodiploid for the glycoprotein B gene: A strategy for studying the function of an essential herpesvirus gene. J. Gen. Virol. 72:1991;385-392.
    • (1991) J. Gen. Virol. , vol.72 , pp. 385-392
    • Misra, V.1    Blewett, E.L.2
  • 50
    • 0023201042 scopus 로고
    • Assembly and processing of the disulfide-linked varicella-zoster virus glycoprotein gpII(140)
    • Montalvo E. A., Grose C. Assembly and processing of the disulfide-linked varicella-zoster virus glycoprotein gpII(140). J. Virol. 61:1987;2877-2884.
    • (1987) J. Virol. , vol.61 , pp. 2877-2884
    • Montalvo, E.A.1    Grose, C.2
  • 52
    • 0027448559 scopus 로고
    • Glycoprotein B of human cytomegalovirus promotes virion penetration into cells, transmission of infection from cell to cell, and fusion of infected cells
    • Navarro D., Paz P., Tugizov S., Topp K., La Vail J., Pereira L. Glycoprotein B of human cytomegalovirus promotes virion penetration into cells, transmission of infection from cell to cell, and fusion of infected cells. Virology. 197:1993a;143-158.
    • (1993) Virology , vol.197 , pp. 143-158
    • Navarro, D.1    Paz, P.2    Tugizov, S.3    Topp, K.4    La Vail, J.5    Pereira, L.6
  • 53
    • 0027180030 scopus 로고
    • Transport and secretion of truncated derivatives of herpes simplex virus 1 glycoprotein B
    • Navarro D., Qadri I., Pereira L. Transport and secretion of truncated derivatives of herpes simplex virus 1 glycoprotein B. Virology. 192:1993b;234-245.
    • (1993) Virology , vol.192 , pp. 234-245
    • Navarro, D.1    Qadri, I.2    Pereira, L.3
  • 54
    • 0021325510 scopus 로고
    • Early events in the infection of human B lymphocytes by Epstein-Barr virus: The internalization process
    • Nemerow G. R., Cooper N. R. Early events in the infection of human B lymphocytes by Epstein-Barr virus: the internalization process. Virology. 132:1984;186-198.
    • (1984) Virology , vol.132 , pp. 186-198
    • Nemerow, G.R.1    Cooper, N.R.2
  • 55
    • 0024965987 scopus 로고
    • Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2)
    • Nemerow G. R., Houghten R. A., Moore M. D., Cooper N. R. Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2). Cell. 56:1989;369-377.
    • (1989) Cell , vol.56 , pp. 369-377
    • Nemerow, G.R.1    Houghten, R.A.2    Moore, M.D.3    Cooper, N.R.4
  • 56
    • 0023183629 scopus 로고
    • Identification of gp350 as the viral glycoprotein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: Sequence homology of gp350 and C3 complement fragment C3d
    • Nemerow G. R., Mold C., Schwend V. K., Tollefson V., Cooper N. R. Identification of gp350 as the viral glycoprotein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: Sequence homology of gp350 and C3 complement fragment C3d. J. Virol. 61:1987;1416-1420.
    • (1987) J. Virol. , vol.61 , pp. 1416-1420
    • Nemerow, G.R.1    Mold, C.2    Schwend, V.K.3    Tollefson, V.4    Cooper, N.R.5
  • 57
    • 0345425475 scopus 로고    scopus 로고
    • Northwestern University, Evanston, IL
    • Novotny, M. J. 1996, Northwestern University, Evanston, IL.
    • (1996)
    • Novotny, M.J.1
  • 58
    • 0022372539 scopus 로고
    • Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions
    • Para M. F., Parish M. L., Noble A. G., Spear P. G. Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions. J. Virol. 55:1985;483-488.
    • (1985) J. Virol. , vol.55 , pp. 483-488
    • Para, M.F.1    Parish, M.L.2    Noble, A.G.3    Spear, P.G.4
  • 59
    • 0022382343 scopus 로고
    • Epstein-Barr virus genome may encode a protein showing significant amino acid and predicted secondary structure homology with glycoprotein B of herpes simplex virus 1
    • Pellett P. E., Biggin M. D., Barrell B., Roizman B. Epstein-Barr virus genome may encode a protein showing significant amino acid and predicted secondary structure homology with glycoprotein B of herpes simplex virus 1. J. Virol. 56:1985a;807-813.
    • (1985) J. Virol. , vol.56 , pp. 807-813
    • Pellett, P.E.1    Biggin, M.D.2    Barrell, B.3    Roizman, B.4
  • 60
    • 0021930782 scopus 로고
    • Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: Primary sequence and predicted protein structure of the wild type and of monoclonal antibody-resistant mutants
    • Pellett P. E., Kousoulas K. G., Pereira L., Roizman B. Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: Primary sequence and predicted protein structure of the wild type and of monoclonal antibody-resistant mutants. J. Virol. 53:1985b;243-253.
    • (1985) J. Virol. , vol.53 , pp. 243-253
    • Pellett, P.E.1    Kousoulas, K.G.2    Pereira, L.3    Roizman, B.4
  • 61
    • 0027933801 scopus 로고
    • Function of glycoprotein B homologues of the familyherpesviridae.
    • Pereira L. Function of glycoprotein B homologues of the familyherpesviridae. Infect Agents Dis. 3:1994;9-28.
    • (1994) Infect Agents Dis. , vol.3 , pp. 9-28
    • Pereira, L.1
  • 62
    • 0024458284 scopus 로고
    • Domain structure of herpes simplex virus 1 glycoprotein B: Neutralizing epitopes map in regions of continuous and discontinuous residues
    • Pereira L., Ali M., Kousoulas K., Huo B., Banks T. Domain structure of herpes simplex virus 1 glycoprotein B: Neutralizing epitopes map in regions of continuous and discontinuous residues. Virology. 172:1989;11-24.
    • (1989) Virology , vol.172 , pp. 11-24
    • Pereira, L.1    Ali, M.2    Kousoulas, K.3    Huo, B.4    Banks, T.5
  • 63
    • 0020638192 scopus 로고
    • A putative signal peptidase recognition site and sequence in eucaryotic and procaryotic signal peptides
    • Perlman D., Halvorson H. O. A putative signal peptidase recognition site and sequence in eucaryotic and procaryotic signal peptides. J. Mol. Biol. 167:1983;391-409.
    • (1983) J. Mol. Biol. , vol.167 , pp. 391-409
    • Perlman, D.1    Halvorson, H.O.2
  • 64
    • 0026083671 scopus 로고
    • Mutations in conformation-dependent domains of herpes simplex virus 1 glycoprotein B affect the antigenic properties, dimerization, and transport of the molecule
    • Qadri I., Gimeno C., Navarro D., Pereira L. Mutations in conformation-dependent domains of herpes simplex virus 1 glycoprotein B affect the antigenic properties, dimerization, and transport of the molecule. Virology. 180:1991;135-152.
    • (1991) Virology , vol.180 , pp. 135-152
    • Qadri, I.1    Gimeno, C.2    Navarro, D.3    Pereira, L.4
  • 65
    • 0018776822 scopus 로고
    • Epstein-Barr virus-induced membrane antigens: Immunochemical characterization of Triton X-100 solubilized viral membrane antigens from EBV-superinfected Raji cells
    • Qualtiere L. F., Pearson G. R. Epstein-Barr virus-induced membrane antigens: Immunochemical characterization of Triton X-100 solubilized viral membrane antigens from EBV-superinfected Raji cells. Int. J. Cancer. 23:1979;808-817.
    • (1979) Int. J. Cancer , vol.23 , pp. 808-817
    • Qualtiere, L.F.1    Pearson, G.R.2
  • 66
    • 0026072796 scopus 로고
    • Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration
    • Rauh I., Mettenleiter T. C. Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration. J. Virol. 65:1991;5348-5356.
    • (1991) J. Virol. , vol.65 , pp. 5348-5356
    • Rauh, I.1    Mettenleiter, T.C.2
  • 67
    • 0025964889 scopus 로고
    • Pseudorabies virus mutants lacking the essential glycoprotein gII can be complemented by glycoprotein gI of bovine herpesvirus 1
    • Rauh I., Weiland F., Fehler F., Keil G. M., Mettenleiter T. C. Pseudorabies virus mutants lacking the essential glycoprotein gII can be complemented by glycoprotein gI of bovine herpesvirus 1. J. Virol. 65:1991;621-631.
    • (1991) J. Virol. , vol.65 , pp. 621-631
    • Rauh, I.1    Weiland, F.2    Fehler, F.3    Keil, G.M.4    Mettenleiter, T.C.5
  • 68
    • 0029876473 scopus 로고    scopus 로고
    • Lytic growth of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) in culture
    • Renne R., Zhong W., Herndier B., McGrath M., Abbey N., Redes D., Ganem D. Lytic growth of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) in culture. Nature Med. 2:1996;342-346.
    • (1996) Nature Med. , vol.2 , pp. 342-346
    • Renne, R.1    Zhong, W.2    Herndier, B.3    McGrath, M.4    Abbey, N.5    Redes, D.6    Ganem, D.7
  • 69
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • B.N. Fields, D.M. Knipe, & P.M. Howley. Philadelphia: Lipincott-Raven
    • Rickinson A. B., Kieff E. Epstein-Barr virus. Fields B. N., Knipe D. M., Howley P. M. Fields Virology. 1996;2397-2446 Lipincott-Raven, Philadelphia.
    • (1996) Fields Virology , pp. 2397-2446
    • Rickinson, A.B.1    Kieff, E.2
  • 70
    • 0024375380 scopus 로고
    • Nucleotide sequence and characterization of the Marek's disease virus homologue of glycoprotein B of herpes simplex virus
    • Ross L. J. N., Sanderson M., Scott S. D., Bins M. M., Doel T., Milne B. Nucleotide sequence and characterization of the Marek's disease virus homologue of glycoprotein B of herpes simplex virus. J. Gen. Virol. 70:1989;1789-1804.
    • (1989) J. Gen. Virol. , vol.70 , pp. 1789-1804
    • Ross, L.J.N.1    Sanderson, M.2    Scott, S.D.3    Bins, M.M.4    Doel, T.5    Milne, B.6
  • 74
    • 0017231934 scopus 로고
    • Membrane proteins specified by herpes simplex viruses. I. Identification of four glycoprotein precursors and their products in type 1-infected cells
    • Spear P. G. Membrane proteins specified by herpes simplex viruses. I. Identification of four glycoprotein precursors and their products in type 1-infected cells. J. Virol. 17:1976;991-1008.
    • (1976) J. Virol. , vol.17 , pp. 991-1008
    • Spear, P.G.1
  • 75
    • 0000929553 scopus 로고
    • Entry of alphaherpesviruses into cells
    • Spear P. G. Entry of alphaherpesviruses into cells. Semin. Virol. 4:1993;167-180.
    • (1993) Semin. Virol. , vol.4 , pp. 167-180
    • Spear, P.G.1
  • 76
    • 0028129026 scopus 로고
    • Characterization of murine gammaherpesvirus 68 glycoprotein B (gB) homolog: Similarity to Epstein-Barr virus gB (gp110)
    • Stewart J. P., Janjua N. J., Sunil-Chandra N. P., Nash A. A., Arrand J. R. Characterization of murine gammaherpesvirus 68 glycoprotein B (gB) homolog: Similarity to Epstein-Barr virus gB (gp110). J. Virol. 68:1994;6496-6504.
    • (1994) J. Virol. , vol.68 , pp. 6496-6504
    • Stewart, J.P.1    Janjua, N.J.2    Sunil-Chandra, N.P.3    Nash, A.A.4    Arrand, J.R.5
  • 77
    • 0026022320 scopus 로고
    • Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicatesin vitro.
    • Swaminathan S., Tomkinson B., Kieff E. Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicatesin vitro. Proc. Natl. Acad. Sci. USA. 88:1991;1546-1550.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1546-1550
    • Swaminathan, S.1    Tomkinson, B.2    Kieff, E.3
  • 78
    • 0023658334 scopus 로고
    • Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping and endocytosis
    • Tanner J., Weis J., Fearon D., Whang Y., Kieff E. Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping and endocytosis. Cell. 50:1987;203-213.
    • (1987) Cell , vol.50 , pp. 203-213
    • Tanner, J.1    Weis, J.2    Fearon, D.3    Whang, Y.4    Kieff, E.5
  • 79
    • 0024266413 scopus 로고
    • Soluble gp350/220 and deletion mutant glycoproteins block Epstein-Barr virus adsorption to lymphocytes
    • Tanner J., Whang Y., Sample J., Sears A., Kieff E. Soluble gp350/220 and deletion mutant glycoproteins block Epstein-Barr virus adsorption to lymphocytes. J. Virol. 62:1988;4452-4464.
    • (1988) J. Virol. , vol.62 , pp. 4452-4464
    • Tanner, J.1    Whang, Y.2    Sample, J.3    Sears, A.4    Kieff, E.5
  • 80
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
    • Teasdale R. D., Jackson M. R. Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu. Rev. Cell Dev. Biol. 12:1996;27-54.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 81
    • 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. Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin. Virology. 206:1995;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
  • 82
    • 0021770334 scopus 로고
    • How signal sequences maintain sequence specificity
    • von Heijne G. How signal sequences maintain sequence specificity. J. Mol. Biol. 173:1984;243-351.
    • (1984) J. Mol. Biol. , vol.173 , pp. 243-351
    • Von Heijne, G.1
  • 83
    • 0025269950 scopus 로고
    • The export pathway of the pseurabies 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. The export pathway of the pseurabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the golgi apparatus. J. Virol. 64:1990;1946-1955.
    • (1990) J. Virol. , vol.64 , pp. 1946-1955
    • Whealy, M.E.1    Robbins, A.K.2    Enquist, L.W.3
  • 84
    • 0027320563 scopus 로고
    • Epstein-Barr virus glycoprotein gp85 associates with the BKRF2 gene product and is incompletely processed as a recombinant protein
    • Yaswen L. R., Stephens E. B., Davenport L. C., Hutt-Fletcher L. M. Epstein-Barr virus glycoprotein gp85 associates with the BKRF2 gene product and is incompletely processed as a recombinant protein. Virology. 195:1993;387-396.
    • (1993) Virology , vol.195 , pp. 387-396
    • Yaswen, L.R.1    Stephens, E.B.2    Davenport, L.C.3    Hutt-Fletcher, L.M.4
  • 85
    • 0029798646 scopus 로고    scopus 로고
    • Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding
    • Zheng Z., Maidji E., Tugizov S., Pereira L. Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding. J. Virol. 70:1996;8029-8040.
    • (1996) J. Virol. , vol.70 , pp. 8029-8040
    • Zheng, Z.1    Maidji, E.2    Tugizov, S.3    Pereira, L.4


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