1887

Abstract

SUMMARY

We constructed a recombinant herpes simplex virus (HSV) containing the transcribed coding and non-coding sequences of HSV-1 strain F glycoprotein B (gB) gene, a gene, fused to the promoter-regulatory sequences of the HSV-1 4 gene and inserted into the thymidine kinase gene of RH1G44, an HSV-1 × HSV-2 recombinant that contains an HSV-2 gB gene at the natural locus. Phenotypic analyses of the insertion mutant, R3145, showed that the gB gene was transcribed in the presence of cycloheximide but underwent partial conversion to the HSV-2 form. Nucleotide sequencing of the gene indicated that the 5′ crossover occurred between nucleotides 107 and 117 upstream from the translation initiation site and that the 3′ crossover occurred between the sequences specifying amino acids 402 and 412 of the HSV-1 gB. The chimeric protein consisted of an N-terminal 405 to 415 amino acids encoded by the HSV-2 gene and a C-terminal 462 to 472 amino acids encoded by the HSV-1 gene. Comparison of the reactivity of the parental and recombinant gB with type-specific monoclonal antibodies indicated that the chimeric gB lost reactivity with four HSV-1-specific antibodies but gained reactivity with three HSV-2-specific antibodies.

Keyword(s): glycoprotein B , HSV-1 and recombinant
Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-70-3-735
1989-03-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/jgv/70/3/JV0700030735.html?itemId=/content/journal/jgv/10.1099/0022-1317-70-3-735&mimeType=html&fmt=ahah

References

  1. Bzik D. J., Fox B. A., Deluca N. A., Person S. 1984; Nucleotide sequence specifying the glycoprotein gene, gB, of herpes simplex virus type 1. Virology 133:301–314
    [Google Scholar]
  2. Bzik D. J., Debroy C, Fox B. A., Pederson N. E., Person S. 1986; The nucleotide sequence of the gB glycoprotein gene of HSV-2 and comparison with the corresponding gene of HSV-1. Virology 155:322–333
    [Google Scholar]
  3. Chapsal J. M., Pereira L. 1988; Characterization of epitopes on native and denatured forms of herpes simplex virus glycoprotein B. Virology 164:427–434
    [Google Scholar]
  4. Kousoulas K. G., Pellett P. E., Pereira L., Roizman B. 1984; Mutations affecting conformation or sequence of neutralizing epitopes identified by reactivity of viable plaques segregated from syn and ts domains of HSV-1 (F) gB gene. Virology 135:379–394
    [Google Scholar]
  5. Kousoulas K., Bin H., Pereira L. 1988; Antibody resistant mutations in cross-reactive and type-specific epitopes of herpes simplex virus 1 glycoprotein B map in separate domains. Virology 166:423–431
    [Google Scholar]
  6. Little S. P., Jofre J. T., Courtney R. J., Schaffer P. A. 1981; A virion-associated glycoprotein essential for infectivity of herpes simplex virus type 1. Virology 115:149–160
    [Google Scholar]
  7. Manservigi R., Spear P. G., Buchan A. 1977; Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. Proceedings of the National Academy of SciencesU.S.A 743913–3917
    [Google Scholar]
  8. Pellett P. E., Kousoulas K. G., Pereira L., Roizman B. 1985; 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. Journal of Virology 53:243–253
    [Google Scholar]
  9. Pereira L., Dondero D., Norrild B., Roizman B. 1981; Differential immunologic and electrophoretic properties of glycoproteins gA and gB of HSV-2 produced in HEp-2 and Vero cells. Proceedings of the National Academy of SciencesU.S.A 785202–5206
    [Google Scholar]
  10. Pereira L., Dondero D., Gallo D., Devlin V., Woodie J. D. 1982; Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies. Infection and Immunity 35:363–367
    [Google Scholar]
  11. Pogue-Geile K. L., Spear P. G. 1986; Enhanced rate of conversion or recombination of markers within a region of unique sequence in the herpes simplex virus genome. Journal of Virology 58:704–708
    [Google Scholar]
  12. Post L. E., Conley A. J., Mocarski E. S., Roizman B. 1980; Cloning of reiterated and nonreiterated herpes simplex virus 1 sequences as BamHI fragments. Proceedings of the National Academy of SciencesU.S.A 774201–4205
    [Google Scholar]
  13. Roizman B. 1979; The structure and isomerization of herpes simplex virus genomes. Cell 16:481–494
    [Google Scholar]
  14. Ruyechan T. W., Morse L. S., Knipe D. M., Roizman B. 1979; Molecular genetics of herpes simplex virus. II. Mapping of the major viral glycoproteins and of the genetic loci specifying the social behavior of infected cells. Journal of Virology 29:677–697
    [Google Scholar]
  15. Sarmiento M., Spear P. G. 1979; Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7 (B2). Journal of Virology 29:1159–1167
    [Google Scholar]
  16. Sarmiento M., Haffey M., Spear P. G. 1979; Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7 (B2) in virion infectivity. Journal of Virology 29:1149–1158
    [Google Scholar]
  17. Stuve L. L., Brown-Shimer S., Pachl C, Najarian R., Dina D., Burke R. L. 1987; Structure and expression of the herpes simplex virus type 2 glycoprotein gB gene. Journal of Virology 61:326–335
    [Google Scholar]
  18. Tognon M., Furlong D., Conley A. J., Roizman B. 1981; Molecular genetics of herpes simplex virus. V. Characterization of a mutant defective in ability to form plaques at low temperatures and in a viral function which prevents accumulation of coreless capsids at nuclear pores late in infection. Journal of Virology 40:870–880
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-70-3-735
Loading
/content/journal/jgv/10.1099/0022-1317-70-3-735
Loading

Data & Media loading...

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