Abstract
The envelopes of all herpesviruses contain multiple glycoprotein species, each one of which is potentially important to virus entry, to virus egress and to trafficking of virus-producing cells throughout the body. In addition, membrane-associated proteins or glycoproteins that are found in the infected cell, but not in the virion, may influence virus assembly and yield. Thus, as a class these molecules have a major impact on virus tropism and virus load and contribute significantly to the outcome of infection.
Keywords
- Recombinant Virus
- Epithelial Cell Infection
- Herpes Simplex Virus Glycoprotein
- Oral Hairy Leukoplakia
- Neomycin Resistance Cassette
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Anagnastopoulos IMH, Kreschel C, Stein H (1995) Morphology, immunophenotype, and distribution of latently and/or productively Epstein-Barr virus-infected cells in acute infectious mononucleosis: implications for the interindividual infection route of Epstein-Barr virus. Blood 85:744–750
Baer R, Bankier AT, Biggin MD, Deininger PL, Farrell PJ, Gibson TJ, Hatfull G, Hudson GS, Satchwell SC, Seguin C, Tuffnell PS, Barrell BG (1984) DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature 310:207–211
Barnett BC, Dolan A, Telford EAR, Davison AJ, McGeoch DJ (1992) A novel herpes simplex virus gene (UL49A) encodes a putative membrane protein with counterparts in other herpesviruses. J Gen Virol 73:2167–2171
Beisel C, Tanner J, Matsuo T, Thorley-Lawson D, Kezdy F, Kieff E (1985) Two major outer envelope glycoproteins of Epstein-Barr virus are encoded by the same gene. J Virol 54:665–674
Borza C, Hutt-Fletcher LM (1998) Epstein-Barr virus recombinant lacking expression of glycoprotein gp150 infects B cells normally but is enhanced for infection of the epithelial line SVKCR2. J Virol 72:7577–7582
Brack AR, Dijkstra JM, Granzow H, Klupp BG, Mettenleiter TC (1999) Inhibition of virion maturation by simultaneous deletion of glycoproteins E, I, and M of Pseudorabies virus. J Virol 73: 5364–5372
Emini EA, Luka J, Armstrong ME, Keller PM, Ellis RW, Pearson GR (1987) Identification of an Epstein-Barr virus glycoprotein which is antigenically homologous to the varicella-zoster glycoprotein II and the herpes simplex virus glycoprotein B. Virology 157:552–555
Fingeroth JD, Weis JJ, Tedder TF, Strominger JL, Biro PA, Fearon DT (1984) Epstein-Barr virus receptor of human B lymphocytes is the C3d complement CR2. Proc Natl Acad Sci USA 81:4510–4516
Gayle MA, Sims JE, Dower SK, Slack JL (1994) Monoclonal antibody 1994–2001 (also known as ALVA 42) reported to recognize type II IL-1 receptor is specific for HLA-DR alpha and beta chains. Cytokine 6:83–86
Gong M, Kieff E (1990) Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/ 220 and gp110. J Virol 64:1507–1516
Gong M, Ooka T, Matsuo T, Kieff E (1987) Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J Virol 61:499–508
Greenspan JS, Greenspan D, Lennette ET, Abrams DI, Conant MA, Petersen V, Freese UK (1985) Replication of Epstein-Barr virus within the epithelial cells of oral “hairy” leukoplakia, an AIDS-associated lesion. New Engl J Med 313:1564–1571
Gulley ML, Pulitzer DR, Eagan PA, Schneider BG (1996) Epstein-Barr virus infection is an early event in gastric carcinogenesis and is independent of bcl-2 expression and p53 accumulation. Hum Pathol 27:20–27
Haddad RS, Hutt-Fletcher LM (1989) Depletion of glycoprotein gp85 from virosomes made with Epstein-Barr virus proteins abolishes their ability to fuse with virus receptor-bearing cells. J Virol 63:4998–5005
Heineman T, Gong M, Sample J, Kieff E (1988) Identification of the Epstein-Barr virus gp85 gene. J Virol 62:1101–1107
Herrold RE, Marchini A, Frueling S, Longnecker R (1995) Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo. J Virol 70:2049–2054
Jöns A, Granzlow H, Kuchling R, Mettenleiter TC (1996) The UL49.5 gene of Pseudorabies virus codes for an O-glycosylated structural protein of the virus envelope. J Virol 70:1237–1241
Knox PG, Young LS (1995) Epstein-Barr virus infection of CR2-transfected epithelial cells reveals the presence of MHC class II on the virion. Virology 213:147–157
Kurilla MG, Heineman T, Davenport LC, Kieff E, Hutt-Fletcher LM (1995) A novel Epstein-Barr virus glycoprotein gp150 expressed from the BDLF3 open reading frame. Virology 209:108–121
Lake CM, Molesworth SJ, Hutt-Fletcher LM (1998) The Epstein-Barr virus (EBV) gN homolog BLRF1 encodes a 15kDa glycoprotein that cannot be authentically processed unless it is co-expressed with the EBV gM homolog BBRF3. J Virol 72:5559–5564
Lee SK (1999) Four consecutive arginine residues at positions 836–839 of EBV gp110 determine intracellular localization of gp110. Virology 264:350–358
Lee SK, Longnecker R (1997) The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication. J Virol 71:4092–4097
Lemon SM, Hutt LM, Shaw JE, Li J-LH, Pagano JS (1977) Replication of EBV in epithelial cells during infectious mononucleosis. Nature 268:268–270
Li QX, Spriggs MK, Kovats S, Turk SM, Comeau MR, Nepom B, Hutt-Fletcher LM (1997) Epstein-Barr virus uses HLA class II as a cofactor for infection of B lymphocytes. J Virol 71:4657–4662
Li QX, Turk SM, Hutt-Fletcher LM (1995) 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 69:3987–3994
Li QX, Young LS, Niedobitek G, Dawson CW, Birkenbach M, Wang F, Rickinson AB (1992) Epstein-Barr virus infection and replication in a human epithelial system. Nature 356:347–350
Mackett M, Conway MJ, Arrand JR, Haddad RS, Hutt-Fletcher LM (1990) Characterization and expression of a glycoprotein encoded by the Epstein-Barr virus BamHI 1 fragment. J Virol 64:2545–2552
Mellman I, Pierre P, Amigorena S (1995) Lonely MHC molecules seeking immunogenic peptides for meaningful relationships. Current Opinion in Cell Biology 7:564–572
Miller N, Hutt-Fletcher LM (1988) A monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein-Barr virus. Journal of Virology 62:2366–2372
Modrow S, Hoflacker B, Wolf H (1992) Identification of a protein encoded in the EB-viral open reading frame BMRF2. Arch Virol 127:379–386
Nemerow GR, Houghton RA, Moore MD, Cooper NR (1989) Identification of the epitope in the major envelope proteins of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2). Cell 56:369–377
Nemerow GR, Wolfert R, McNaughton M, Cooper NR (1985) Identification and characterization of the Epstein-Barr virus receptor on human B lymphocytes and its relationship to the C3d complement receptor (CR2). J Virol 55:347–351
Niedobitek G, Herbst H, Young LS, Brooks L, Masucci MG, Crooker J, Rickinson A, Stein H (1992) Patterns of Epstein-Barr virus infection in non-neoplastic lymphoid tissue. Blood 79: 2520–2526
Nolan LA, Morgan AJ (1995) The Epstein-Barr virus open reading frame BDLF3 codes for a 100–150kDa glycoprotein. J Gen Virol 76:1381–1392
Oba DE, Hutt-Fletcher LM (1988) Induction of antibodies to the Epstein-Barr virus glycoprotein gp85 with a synthetic peptide corresponding to a sequence in the BXLF2 open reading frame. J Virol 62:1108–1114
Osato T, Imai S (1996) Epstein-Barr virus and gastric carcinoma. Semin Cancer Biol 7:175–182
Papworth MA, Van Dijk AA, Benyon GR, Allen TD, Arrand JR, Mackett M (1997) The processing, transport and heterologous expression of Epstein-Barr virus gp110. J Gen Virol 78:2179–2189
Penaranda ME, Lagenaur LA, Pierek LT, Berline JW, MacPhail LA, Greenspan D, Greenspan J, Palefsky JM (1997) Expression of Epstein-Barr virus BMRF-2 and BDLF-3 genes in hairy leuko-plakia. J Gen Virol 78:3361–3370
Sinclair AJ, Farrell PJ (1995) Host cell requirements for efficient infection of quiescent primary B lymphocytes by Epstein-Barr virus. J Virol 69:5461–5468
Sixbey JW, Nedrud JG, Raab-Traub N, Hanes RA, Pagano JS (1984) Epstein-Barr virus replication in oropharyngeal epithelial cells. New Engl J Med 310:1225–1230
Spear PG (1993) Entry of alphaviruses into cells. Semin Virol 4:167–180
Spriggs MK, Armitage RJ, Comeau MR, Strockbine L, Farrah T, MacDuff B, Ulrich D, Alderson MR, Mullberg J, Cohen JI (1996) The extracellular domain of the Epstein-Barr virus BZLF2 protein binds the HLA-DR beta chain and inhibits antigen presentation. J Virol 70:5557–5563
Strnad BC, Schuster T, Klein R, Hopkins RFI, Witmer T, Neubauer R, Rabin H (1982) Production and characterization of monoclonal antibodies against the Epstein-Barr virus membrane antigen. J Virol 41:258–264
Sugano N, Chen W, Roberts ML, Cooper NR (1997) Epstein-Barr virus binding to CD21 activates the initial viral promoter via NF B induction. J Exp Med 186:731–737
Tanner J, Weis J, Fearon D, Whang Y, Kieff E (1987) Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping and endocytosis. Cell 50:203–213
Tanner J, Whang Y, Sample J, Sears A, Keiff E (1988) Soluble gp350/220 and deletion mutant glycoproteins block Epstein-Barr virus adsorption to lymphocytes. J Virol 62:4452–4464
Thorley-Lawson DA, Miyashita EM, Khan G (1996) Epstein-Barr virus and the B cell: that’s all it takes. Trends Microbiol 4:204–208
Trkola A, Dragic T, Arthos J, Binley JM, Olson WC, Allaway C, Cheng-meyer C, Robinson J, Maddon PJ, Moore JP (1996) CD-4 dependent antibody sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature 384:184–187
Wang X, Hutt-Fletcher LM (1998) Epstein-Barr virus lacking glycoprotein gp42 can bind to B cells but is not able to infect. J Virol 72:158–163
Wang X, Kenyon WJ, Li QX, Mullberg J, Hutt-Fletcher LM (1998) Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells. J Virol 72:5552– 5558
Wu L, Gerard NP, Wyatt R, Choe H, Parolin C, Ruffing N, Borsetti A, Cardoso AA, Desjardin E, Newman W, Gerard C, Sodroski J (1996) CD-4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature 384:179–183
Yaswen LR, Stephens EB, Davenport LC, Hutt-Fletcher LM (1993) Epstein-Barr virus glycoprotein gp85 associates with the BKRF2 gene product and is incompletely processed as a recombinant protein. Virology 195:387–396
Yoshiyama H, Imai S, Shimizu N, Takada K (1997) Epstein-Barr virus infection of human gastric carcinoma cells: implication of the existence of a new virus receptor different from CD21. J Virol 71:5688–5691
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Hutt-Fletcher, L.M., Lake, C.M. (2001). Two Epstein-Barr Virus Glycoprotein Complexes. In: Takada, K. (eds) Epstein-Barr Virus and Human Cancer. Current Topics in Microbiology and Immunology, vol 258. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56515-1_4
Download citation
DOI: https://doi.org/10.1007/978-3-642-56515-1_4
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-62568-8
Online ISBN: 978-3-642-56515-1
eBook Packages: Springer Book Archive