Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1997 May;71(5):4092–4097. doi: 10.1128/jvi.71.5.4092-4097.1997

The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication.

S K Lee 1, R Longnecker 1
PMCID: PMC191563  PMID: 9094688

Abstract

To investigate the importance of the Epstein-Barr virus (EBV) glycoprotein 110 (gp110) tail domain in the intracellular localization of gp110 and virus lytic replication, three carboxy-terminal truncation mutants of gp110 were constructed. Deletion of 16 amino acids from the carboxyl-terminal tail resulted in gp110 intracellular localization which was indistinguishable from that of wild-type gp110, whereas deletion of either 41 or 56 amino acids from the carboxyl-terminal tail of gp110 resulted in loss of retention of gp110 in the endoplasmic reticulum and nuclear membrane. None of the gp110 truncation mutants was able to complement EBV(gp110-)+ lymphoblastoid cell lines in transformation assays, indicating the importance of the gp110 tail domain in virus lytic replication. In electron microscopy analysis, no nucleocapsids or enveloped viruses were detected in EBV(gp110-)+ lymphoblastoid cell lines induced for lytic replication.

Full Text

The Full Text of this article is available as a PDF (1.6 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baghian A., Huang L., Newman S., Jayachandra S., Kousoulas K. G. Truncation of the carboxy-terminal 28 amino acids of glycoprotein B specified by herpes simplex virus type 1 mutant amb1511-7 causes extensive cell fusion. J Virol. 1993 Apr;67(4):2396–2401. doi: 10.1128/jvi.67.4.2396-2401.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cai W. H., Gu B., Person S. Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. J Virol. 1988 Aug;62(8):2596–2604. doi: 10.1128/jvi.62.8.2596-2604.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cai W. Z., Person S., DebRoy C., Gu B. H. Functional regions and structural features of the gB glycoprotein of herpes simplex virus type 1. An analysis of linker insertion mutants. J Mol Biol. 1988 Jun 5;201(3):575–588. doi: 10.1016/0022-2836(88)90639-0. [DOI] [PubMed] [Google Scholar]
  4. Cai W. Z., Person S., Warner S. C., Zhou J. H., DeLuca N. A. Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1. J Virol. 1987 Mar;61(3):714–721. doi: 10.1128/jvi.61.3.714-721.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Campadelli-Fiume G., Farabegoli F., Di Gaeta S., Roizman B. Origin of unenveloped capsids in the cytoplasm of cells infected with herpes simplex virus 1. J Virol. 1991 Mar;65(3):1589–1595. doi: 10.1128/jvi.65.3.1589-1595.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Desai P., Homa F. L., Person S., Glorioso J. C. A genetic selection method for the transfer of HSV-1 glycoprotein B mutations from plasmid to the viral genome: preliminary characterization of transdominance and entry kinetics of mutant viruses. Virology. 1994 Oct;204(1):312–322. doi: 10.1006/viro.1994.1536. [DOI] [PubMed] [Google Scholar]
  7. 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. 1987 Apr;157(2):552–555. doi: 10.1016/0042-6822(87)90300-x. [DOI] [PubMed] [Google Scholar]
  8. Gilbert R., Ghosh K., Rasile L., Ghosh H. P. Membrane anchoring domain of herpes simplex virus glycoprotein gB is sufficient for nuclear envelope localization. J Virol. 1994 Apr;68(4):2272–2285. doi: 10.1128/jvi.68.4.2272-2285.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Goepfert P. A., Wang G., Mulligan M. J. Identification of an ER retrieval signal in a retroviral glycoprotein. Cell. 1995 Aug 25;82(4):543–544. doi: 10.1016/0092-8674(95)90026-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gong M., Kieff E. Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. J Virol. 1990 Apr;64(4):1507–1516. doi: 10.1128/jvi.64.4.1507-1516.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gong M., Ooka T., Matsuo T., Kieff E. Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J Virol. 1987 Feb;61(2):499–508. doi: 10.1128/jvi.61.2.499-508.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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. 1989 Dec;63(12):4998–5005. doi: 10.1128/jvi.63.12.4998-5005.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hanover J. A. The nuclear pore: at the crossroads. FASEB J. 1992 Mar;6(6):2288–2295. doi: 10.1096/fasebj.6.6.1312045. [DOI] [PubMed] [Google Scholar]
  14. Heineman T., Gong M., Sample J., Kieff E. Identification of the Epstein-Barr virus gp85 gene. J Virol. 1988 Apr;62(4):1101–1107. doi: 10.1128/jvi.62.4.1101-1107.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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. 1996 Mar;70(3):2049–2054. doi: 10.1128/jvi.70.3.2049-2054.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Huff V., Cai W., Glorioso J. C., Levine M. The carboxy-terminal 41 amino acids of herpes simplex virus type 1 glycoprotein B are not essential for production of infectious virus particles. J Virol. 1988 Nov;62(11):4403–4406. doi: 10.1128/jvi.62.11.4403-4406.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kalderon D., Roberts B. L., Richardson W. D., Smith A. E. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. doi: 10.1016/0092-8674(84)90457-4. [DOI] [PubMed] [Google Scholar]
  18. Kreis T. E., Lowe M., Pepperkok R. COPs regulating membrane traffic. Annu Rev Cell Dev Biol. 1995;11:677–706. doi: 10.1146/annurev.cb.11.110195.003333. [DOI] [PubMed] [Google Scholar]
  19. 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. 1995 Jul;69(7):3987–3994. doi: 10.1128/jvi.69.7.3987-3994.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Marchini A., Tomkinson B., Cohen J. I., Kieff E. BHRF1, the Epstein-Barr virus gene with homology to Bc12, is dispensable for B-lymphocyte transformation and virus replication. J Virol. 1991 Nov;65(11):5991–6000. doi: 10.1128/jvi.65.11.5991-6000.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Menezes J., Leibold W., Klein G., Clements G. Establishment and characterization of an Epstein-Barr virus (EBC)-negative lymphoblastoid B cell line (BJA-B) from an exceptional, EBV-genome-negative African Burkitt's lymphoma. Biomedicine. 1975 Jul;22(4):276–284. [PubMed] [Google Scholar]
  22. Miller G., Lipman M. Release of infectious Epstein-Barr virus by transformed marmoset leukocytes. Proc Natl Acad Sci U S A. 1973 Jan;70(1):190–194. doi: 10.1073/pnas.70.1.190. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Miller G., Shope T., Lisco H., Stitt D., Lipman M. Epstein-Barr virus: transformation, cytopathic changes, and viral antigens in squirrel monkey and marmoset leukocytes. Proc Natl Acad Sci U S A. 1972 Feb;69(2):383–387. doi: 10.1073/pnas.69.2.383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Miller N., Hutt-Fletcher L. M. A monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein-Barr virus. J Virol. 1988 Jul;62(7):2366–2372. doi: 10.1128/jvi.62.7.2366-2372.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Miller N., Hutt-Fletcher L. M. Epstein-Barr virus enters B cells and epithelial cells by different routes. J Virol. 1992 Jun;66(6):3409–3414. doi: 10.1128/jvi.66.6.3409-3414.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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. 1989 Feb 10;56(3):369–377. doi: 10.1016/0092-8674(89)90240-7. [DOI] [PubMed] [Google Scholar]
  27. 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. 1987 May;61(5):1416–1420. doi: 10.1128/jvi.61.5.1416-1420.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. 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. 1985 Dec;56(3):807–813. doi: 10.1128/jvi.56.3.807-813.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Pereira L. Function of glycoprotein B homologues of the family herpesviridae. Infect Agents Dis. 1994 Feb;3(1):9–28. [PubMed] [Google Scholar]
  30. 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. 1979 Jun 15;23(6):808–817. doi: 10.1002/ijc.2910230612. [DOI] [PubMed] [Google Scholar]
  31. Rasile L., Ghosh K., Raviprakash K., Ghosh H. P. Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring. J Virol. 1993 Aug;67(8):4856–4866. doi: 10.1128/jvi.67.8.4856-4866.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Swaminathan S., Tomkinson B., Kieff E. Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicates in vitro. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1546–1550. doi: 10.1073/pnas.88.4.1546. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. 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. 1987 Jul 17;50(2):203–213. doi: 10.1016/0092-8674(87)90216-9. [DOI] [PubMed] [Google Scholar]
  34. 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. 1988 Dec;62(12):4452–4464. doi: 10.1128/jvi.62.12.4452-4464.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES