Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1986 Nov;60(2):803–806. doi: 10.1128/jvi.60.2.803-806.1986

Oligomerization of herpes simplex virus glycoprotein B.

L Claesson-Welsh, P G Spear
PMCID: PMC288962  PMID: 3022014

Abstract

Glycoprotein B (gB) specified by herpes simplex virus can be extracted from virions or infected cells in the form of detergent-stable, heat-dissociable oligomers. The composition of the oligomers and requirements for their formation were investigated. Evidence is presented that the faster-migrating forms of the oligomers are homodimers of gB. Dimerization was shown to occur within minutes of polypeptide synthesis and did not depend on glycosylation, the expression of other viral proteins, or virion morphogenesis. The multiple, electrophoretically distinct forms of gB dimers differ in extent or rate of N-linked oligosaccharide processing and also have other differences that influence electrophoretic mobility.

Full text

PDF
803

Images in this article

804Image
on p.804
804Image
on p.804
805Image
on p.805
805Image
on p.805
805Image
on p.805

Selected References

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

  1. Edson C. M., Hosler B. A., Respess R. A., Waters D. J., Thorley-Lawson D. A. Cross-reactivity between herpes simplex virus glycoprotein B and a 63,000-dalton varicella-zoster virus envelope glycoprotein. J Virol. 1985 Oct;56(1):333–336. doi: 10.1128/jvi.56.1.333-336.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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. 1980 Jul;35(1):114–128. doi: 10.1128/jvi.35.1.114-128.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Heine J. W., Honess R. W., Cassai E., Roizman B. Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J Virol. 1974 Sep;14(3):640–651. doi: 10.1128/jvi.14.3.640-651.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Holland L. E., Sandri-Goldin R. M., Goldin A. L., Glorioso J. C., Levine M. Transcriptional and genetic analyses of the herpes simplex virus type 1 genome: coordinates 0.29 to 0.45. J Virol. 1984 Mar;49(3):947–959. doi: 10.1128/jvi.49.3.947-959.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hubenthal-Voss J., Roizman B. Herpes simplex virus 1 reiterated S component sequences (c1) situated between the a sequence and alpha 4 gene are not essential for virus replication. J Virol. 1985 May;54(2):509–514. doi: 10.1128/jvi.54.2.509-514.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Johnson D. C., Spear P. G. O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Cell. 1983 Mar;32(3):987–997. doi: 10.1016/0092-8674(83)90083-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Little S. P., Jofre J. T., Courtney R. J., Schaffer P. A. A virion-associated glycoprotein essential for infectivity of herpes simplex virus type 1. Virology. 1981 Nov;115(1):149–160. doi: 10.1016/0042-6822(81)90097-0. [DOI] [PubMed] [Google Scholar]
  8. Marsden H. S., Buckmaster A., Palfreyman J. W., Hope R. G., Minson A. C. Characterization of the 92,000-dalton glycoprotein induced by herpes simplex virus type 2. J Virol. 1984 May;50(2):547–554. doi: 10.1128/jvi.50.2.547-554.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Mulligan R. C., Berg P. Selection for animal cells that express the Escherichia coli gene coding for xanthine-guanine phosphoribosyltransferase. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2072–2076. doi: 10.1073/pnas.78.4.2072. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Norrild B., Ludwig H., Rott R. Identification of a common antigen of herpes simplex virus bovine herpes mammillitis virus, and B virus. J Virol. 1978 Jun;26(3):712–717. doi: 10.1128/jvi.26.3.712-717.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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. 1985 Aug;55(2):483–488. doi: 10.1128/jvi.55.2.483-488.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Persson R. H., Bacchetti S., Smiley J. R. Cells that constitutively express the herpes simplex virus immediate-early protein ICP4 allow efficient activation of viral delayed-early genes in trans. J Virol. 1985 May;54(2):414–421. doi: 10.1128/jvi.54.2.414-421.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rafield L. F., Knipe D. M. Characterization of the major mRNAs transcribed from the genes for glycoprotein B and DNA-binding protein ICP8 of herpes simplex virus type 1. J Virol. 1984 Mar;49(3):960–969. doi: 10.1128/jvi.49.3.960-969.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sarmiento M., Haffey M., Spear P. G. Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7(B2) in virion infectivity. J Virol. 1979 Mar;29(3):1149–1158. doi: 10.1128/jvi.29.3.1149-1158.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sarmiento M., Spear P. G. Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7(B2). J Virol. 1979 Mar;29(3):1159–1167. doi: 10.1128/jvi.29.3.1159-1167.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Serafini-Cessi F., Campadelli-Fiume G. Studies on benzhydrazone, a specific inhibitor of herpesvirus glycoprotein synthesis. Size distribution of glycopeptides and endo-beta-N-acetylglucosaminidase-H treatment. Arch Virol. 1981;70(4):331–343. doi: 10.1007/BF01320248. [DOI] [PubMed] [Google Scholar]
  18. Snowden B. W., Kinchington P. R., Powell K. L., Halliburton I. W. Antigenic and biochemical analysis of gB of herpes simplex virus type 1 and type 2 and of cross-reacting glycoproteins induced by bovine mammillitis virus and equine herpesvirus type 1. J Gen Virol. 1985 Feb;66(Pt 2):231–247. doi: 10.1099/0022-1317-66-2-231. [DOI] [PubMed] [Google Scholar]
  19. 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. 1976 Mar;17(3):991–1008. doi: 10.1128/jvi.17.3.991-1008.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wenske E. A., Bratton M. W., Courtney R. J. Endo-beta-N-acetylglucosaminidase H sensitivity of precursors to herpes simplex virus type 1 glycoproteins gB and gC. J Virol. 1982 Oct;44(1):241–248. doi: 10.1128/jvi.44.1.241-248.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES