1887

Abstract

The Epstein—Barr virus (EBV) open reading frame BDLF3 is predicted to code for a glycoprotein on the basis that it contains sequences with signal peptide and transdomain characteristics and nine potential -linked glycosylation sites. No sequential or positional homologues of BDLF3 have been located in other herpes-viruses. A bacterial glutathione -transferase (GST)-BDLF3 fusion protein was used to demonstrate that over one–third of EBV-immune human sera tested recognized the fusion protein but not GST alone on Western blots. The fusion protein was used to raise polyclonal sera in rabbits. A BDLF3 recombinant baculovirus was constructed using the full-length BDLF3 sequence (AcBDLF3). Rabbit anti-fusion protein sera and some human EBV-immune sera recognized products of approximately 30 and 55 kDa from AcBDLF3-infected insect cells by Western blotting. A peptide representing the carboxy-terminal amino acids 215–234 of the BDLF3 sequence was used to raise anti-peptide sera in rabbits. Anti-peptide serum detected a product by indirect immunofluorescence in acetone-fixed EBV-infected B cells from all cell lines tested. A diffuse band with a molecular mass of 100–150 kDa was detected by Western blot in B95–8 cell lysates, partially purified B95-8 virus and B95-8-infected cell membranes after probing with anti-BDLF3 peptide serum. This product was shown to be glycosylated after enzymatic deglycosylation of a B95-8 virus preparation using neuraminidase, -glycosidase or -glycosidase F. The BDLF3 protein products have no known function.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-76-6-1381
1995-06-01
2021-10-20
Loading full text...

Full text loading...

/deliver/fulltext/jgv/76/6/JV0760061381.html?itemId=/content/journal/jgv/10.1099/0022-1317-76-6-1381&mimeType=html&fmt=ahah

References

  1. Beisel C., Tanner J., Matsuo T., Thorley-Lawson D., Rezdy F., Kieff E. 1985; Two major outer envelope glycoproteins of Epstein-Barr virus are encoded by the same gene. Journal of Virology 54:665–674
    [Google Scholar]
  2. Bishop D. H. L. 1992; Baculovirus expression vectors. Seminars in Virology 3:253–264
    [Google Scholar]
  3. Cai W., Gu B., Person S. 1988; Role of glycoprotein B of herpes simplex type 1 in viral entry and cell fusion. Journal of Virology 62:2596–2604
    [Google Scholar]
  4. Cranage M. P., Smith G. L., Bell S. E., Hart H., Brown C., Bankier A. T., Tomlinson P., Barrell B. G., Minson A. C. 1988; Identification and expression of a cytomegalovirus glycoprotein with homology to the Epstein–Barr virus BXLF2 product, varicella-zoster virus gpIII, and herpes simplex virus type 1 glycoprotein H. Journal of Virology 62:1416–1422
    [Google Scholar]
  5. Emini E. A., Luka J., Armstrong M. E., Keller P. M., Ellis R. W., Pearson G. R. 1987; 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 157:52–555
    [Google Scholar]
  6. Epstein M. A., Randle B. J., Finerty S., Kirkwood J. K. 1986; Not all potentially neutralizing, vaccine induced antibodies to Epstein–Barr virus ensure protection of susceptible experimental animals. Clinical and Experimental Immunology 63:485–490
    [Google Scholar]
  7. Fingeroth J., Weiss J., Tedder T., Strominger J., Bird P., Fearon D. 1984; Epstein–Barr virus receptor on human Β lymphocytes is the C3d receptor CR2. Proceedings of the National Academy of Sciences, USA 81:4510–4516
    [Google Scholar]
  8. Friede M., Muller S., Briand J. P., Schuber F., van Regen-mortel M. H. V. 1994; Generation of antibodies cross-reactive with proteins by peptide immunization. In Immunotechnology pp 1–11 Edited by Gosling J. P., Reen D. J. London: Portland Press;
    [Google Scholar]
  9. Ghiasi H., Kaiwar R., Nesburn A. B., Slanina S., Wechsler S. L. 1994; Expression of seven herpes simplex virus type 1 glycoproteins (gB, gC, gD, gE, gG, gH, and gI): comparative protection against lethal challenge in mice. Journal of Virology 68:2118–2126
    [Google Scholar]
  10. Gong M., Kieff E. 1990; Intracellular trafficking of two major Epstein–Barr virus glycoproteins, gp350/220 and gpl10. Journal of Virology 64:1507–1516
    [Google Scholar]
  11. Gong M., Ooka T., Matsuo T., Kieff E. 1987; Epstein–Barr virus glycoprotein homologous to herpes simplex virus gB. Journal of Virology 61:499–508
    [Google Scholar]
  12. Haddad R. S., Hutt-Fletcher L. M. 1989; Depletion of glycoprotein gp85 from virosomes made with Epstein–Barr virus proteins abolishes their ability to fuse with virus receptor-bearing cells. Journal of Virology 63:4998–5005
    [Google Scholar]
  13. Heineman T., Gong M., Sample J., Kieff E. 1988; Identification of the Epstein–Barr virus gp85 gene. Journal of Virology 62:1101–1107
    [Google Scholar]
  14. Herrold B. C., WuDunn D., Soltys N., Spear P. 1991; Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. Journal of Virology 65:1090
    [Google Scholar]
  15. Hummel M., Kieff E. 1982; Epstein–Barr virus RNA. VIII. Viral RNA in permissively infected B95–8 cells. Journal of Virology 43:262–272
    [Google Scholar]
  16. King L. A., Possee R. D. 1992; Proceedings of foreign proteins synthesized using baculovirus vectors in insect cells. In The Baculovirus Expression System: A Laboratory Guide pp 37–50 London: Chapman and Hall;
    [Google Scholar]
  17. Klupp B. G., Visser N., Mettenleiter T. C. 1992; Identification and characterization of pseudorabies virus glycoprotein H. Journal of Virology 66:3048–3055
    [Google Scholar]
  18. Klupp B. G., Baumeister J., Karger A., Visser N., Mettenleiter T. C. 1994; Identification and characterization of a novel structural glycoprotein in pseudorabies virus, gL. Journal of Virology 68:3868–3878
    [Google Scholar]
  19. Lau R., Sinclair A. J., Brimmell M., Farrell P. J. 1993; Epstein–Barr virus productive cycle gene expression in vivo . In The Epstein–Barr Virus and Associated Diseases Edited by Tursz T., Pagano J. S., Ablashi D. V. G. de Thé, Lenoir G., Pearson G. R. Paris: Colloque INSERM/John Libbey Eurotext Ltd; 225203–209
    [Google Scholar]
  20. Luckow V. A., Summers M. D. 1988; Trends in the development of baculovirus expression vectors. Bio/Technology 6:47–55
    [Google Scholar]
  21. Mackett M., Conway M. J., Arrand J. R., Haddad R. S., Hutt-Fletcher L. M. 1990; Characterization and expression of a glycoprotein encoded by the Epstein–Barr virus Bam HI I fragment. Journal of Virology 64:2545–2552
    [Google Scholar]
  22. Miller G. 1990; Epstein–Barr virus; biology, pathogenesis and medical aspects. In Virology 2nd edn, pp 1921–1958 Edited by Fields B. N., Knipe D. M., Chanock R. M., Hirsch M. S., Melnick J. L., Monath T. P., Roizman B. New York: Raven Press;
    [Google Scholar]
  23. Miller N., Hutt-Fletcher L. M. 1988; A monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein–Barr virus. Journal of Virology 62:2366–2372
    [Google Scholar]
  24. Morgan A. J., North J. R., Epstein M. A. 1983; Purification and properties of the gp340 component of Epstein–Barr virus membrane antigen in an immunogenic form. Journal of General Virology 64:455–460
    [Google Scholar]
  25. Morgan A. J., Smith A. R., Barker R. N., Epstein M. A. 1984; A structural investigation of the Epstein–Barr (ΕΒ) virus membrane antigen glycoprotein, gp340. Journal of General Virology 65:397–404
    [Google Scholar]
  26. Navarro D., Paz P., Pereira L. 1992; Domains of herpes simplex virus 1 glycoprotein B that functions in virus penetration, cell-to-cell spread, and cell fusion. Virology 186:99–112
    [Google Scholar]
  27. Nemerow G. R., Mold C., Schwend V. K., Tollefson V., Cooper N. R. 1987; Identification of gp340 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. Journal of Virology 61:1416–1420
    [Google Scholar]
  28. Oba D. E., Hutt-Fletcher L. M. 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. Journal of Virology 62:1108–1114
    [Google Scholar]
  29. Pallesen G., Hamilton-Dutoit S. J., Zhou X. 1993; The association of Epstein–Barr virus (EBV) with T cell lympho-proliferations and Hodgkin′s disease: two new developments in the EBV field. Advances in Cancer Research 62:179–239
    [Google Scholar]
  30. Pellet P. E., Biggin M. D., Barrell B., Roizman B. 1985; 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. Journal of Virology 56:807–813
    [Google Scholar]
  31. Pither R., Zhang C. X., Shiels C., Tarlton J., Finerty S., Morgan A. J. 1992a; Mapping of B-cell epitopes on the polypeptide chain of the Epstein–Barr virus major envelope glycoprotein and candidate vaccine molecule gp340. Journal of Virology 66:1246–1251
    [Google Scholar]
  32. Pither R. J., Nolan L., Tarlton J., Walford J., Morgan A. J. 1992b; Distribution of epitopes within the amino acid sequence of the Epstein–Barr virus major envelope glycoprotein, gp340, recognized by hyperimmune rabbit sera. Journal of General Virology 73:1409–1415
    [Google Scholar]
  33. Qualtiere L. F., Decoteau J. F., Hassan Nasr-el-Din M. 1987; Epitope mapping of the major Epstein–Barr virus outer envelope glycoprotein gp350/220. Journal of General Virology 68:535–543
    [Google Scholar]
  34. Rickinson A. B. 1994; EBV infection and EBV-associated tumours. Symposia of the Society for General Microbiology 51:81–100
    [Google Scholar]
  35. Roizman B., Spears A. E. 1993 In The Human Herpesviruses pp 11–68 Edited by Roizman B., Lopez C., Whitley R. J. New York: Raven Press;
    [Google Scholar]
  36. Rowlands D. C., Ito M., Mangham D. C., Reynolds G., FIerbst H., Hallissey M. T., Fielding J. W. L., Newbold K. M., Jones E. L., Young L. S., Niedobitek G. 1993; Epstein–Barr virus and carcinomas: rare association of the virus with gastric adenocarcinomas. British Journal of Cancer 68:1014–1019
    [Google Scholar]
  37. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: A Laboratory Manual New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  38. Sanchez-Pinel A., Bernad J., Rives H., Lapchine L., Icart J., Didier J. 1991; Identification of a novel EBV-induced membrane glycoprotein of 43 kDa with H667 MAb. Virology 180:31–J0
    [Google Scholar]
  39. Sarmiento M., Haffey M., Spear P. G. 1979; Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7. Journal of Virology 29:1149–1158
    [Google Scholar]
  40. Shibata D., Tokunaga M., Uemura Y., Sato E., Tanaka S., Weiss L. M. 1991; Association of Epstein–Barr virus with undifferentiated gastric carcinoma with intense lymphoid infiltration. American Journal of Pathology 139:469–474
    [Google Scholar]
  41. Shieh M. T., Spear P. G. 1994; Herpesvirus-induced cell fusion that is dependent on cell surface heparan sulfate or soluble heparin. Journal of Virology 68:1224–1228
    [Google Scholar]
  42. Shieh M. T., WuDunn D., Montgomery R. I., Esko J. D., Spear P. G. 1992; Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. Journal of Cell Biology 116:1273–1281
    [Google Scholar]
  43. Smith D. B., Johnson K. S. 1988; Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S–transferase. Gene 67:31–40
    [Google Scholar]
  44. Summers M. D., Smith G. E. 1987; A Manual of Methods for Baculovirus Vectors and Insect Cell Culture Procedures. Texas Agricultural Experimental Station Bulletin no. 1555
    [Google Scholar]
  45. 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
    [Google Scholar]
  46. Tanner J., Whang Y., Sample J., Sears A., Kieff E. 1988; Soluble gp350/220 and deletion mutant glycoproteins block Epstein–Barr virus adsorption to lymphocytes. Journal of Virology 62:4452–4464
    [Google Scholar]
  47. Yaswen L. R., Stephens E. B., Davenport L. C., Hutt-Fletcher L. M. 1993; Epstein–Barr virus glycoprotein gp85 associates with the BKRF2 gene product and is incompletely processed as a recombinant protein. Virology 195:387–396
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-76-6-1381
Loading
/content/journal/jgv/10.1099/0022-1317-76-6-1381
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error