Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1974 Sep;14(3):640–651. doi: 10.1128/jvi.14.3.640-651.1974

Proteins Specified by Herpes Simplex Virus XII. The Virion Polypeptides of Type 1 Strains

Jochen W Heine 1,2, Robert W Honess 1,2, Enzo Cassai 1,2, Bernard Roizman 1,2
PMCID: PMC355559  PMID: 4369085

Abstract

The polypeptides from purified virions of a herpes simplex 1 (human herpes-virus 1) strain, F1, which had been passaged a limited number of times in cell culture after isolation, formed 33 bands on electrophoretic separation in polyacrylamide gels cross-linked with N, N′-diallyltartardiamide in contrast to a maximum resolution of only 24 to 25 bands in gels cross-linked with N, N′-methylenebisacrylamide. This increase in the number of bands was due chiefly to an improved separation of glycosylated polypeptides from nonglycosylated polypeptides with which they co-electrophoresed on methylenebisacrylamide cross-linked gels. Purified virions of HSV-1 [F1] had a protein/DNA mass ratio of 10.7 ± 0.96, and based on a DNA molecular mass of 85 × 106 to 100 × 106 the estimated weight of virion polypeptides ranges from 16.4 to 19.4 × 10−16 g. The number of molecules of each polypeptide per virion ranged from less than 50 to 1,500. Comparison of the virion polypeptides of two HSV-1 strains with similar isolation and limited passage history with those of four HSV-1 strains with histories of numerous passages outside the human host showed a number of nonrandom variations in virion polypeptides. Thus, although the virion polypeptides of two strains with similar isolation and limited passage history could not be differentiated, strains with extended passage histories differed markedly from each other and from the limited passage strains in the number and electrophoretic mobility of noncapsid polypeptides and notably in those of the envelope.

Full text

PDF
641

Images in this article

643Image
on p.643
647Image
on p.647
648Image
on p.648
649Image
on p.649

Selected References

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

  1. Anker H. S. A solubilizable acrylamide gel for electrophoresis. FEBS Lett. 1970 Apr 16;7(3):293–293. doi: 10.1016/0014-5793(70)80185-5. [DOI] [PubMed] [Google Scholar]
  2. BURTON K. A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem J. 1956 Feb;62(2):315–323. doi: 10.1042/bj0620315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ejercito P. M., Kieff E. D., Roizman B. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J Gen Virol. 1968 May;2(3):357–364. doi: 10.1099/0022-1317-2-3-357. [DOI] [PubMed] [Google Scholar]
  4. Gibson W., Roizman B. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J Virol. 1972 Nov;10(5):1044–1052. doi: 10.1128/jvi.10.5.1044-1052.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gibson W., Roizman B. Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels. J Virol. 1974 Jan;13(1):155–165. doi: 10.1128/jvi.13.1.155-165.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HOGGAN M. D., ROIZMAN B. The isolation and properties of a variant of Herpes simplex producing multinucleated giant cells in monolayer cultures in the presence of antibody. Am J Hyg. 1959 Sep;70:208–219. doi: 10.1093/oxfordjournals.aje.a120071. [DOI] [PubMed] [Google Scholar]
  7. Honess R. W., Roizman B. Proteins specified by herpes simplex virus. XI. Identification and relative molar rates of synthesis of structural and nonstructural herpes virus polypeptides in the infected cell. J Virol. 1973 Dec;12(6):1347–1365. doi: 10.1128/jvi.12.6.1347-1365.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Keller J. M., Spear P. G., Roizman B. Proteins specified by herpes simplex virus. 3. Viruses differing in their effects on the social behavior of infected cells specify different membrane glycoproteins. Proc Natl Acad Sci U S A. 1970 Apr;65(4):865–871. doi: 10.1073/pnas.65.4.865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kieff E. D., Bachenheimer S. L., Roizman B. Size, composition, and structure of the deoxyribonucleic acid of herpes simplex virus subtypes 1 and 2. J Virol. 1971 Aug;8(2):125–132. doi: 10.1128/jvi.8.2.125-132.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Plummer G., Waner J. L., Phuangsab A., Goodheart C. R. Type 1 and type 2 herpes simplex viruses: serological and biological differences. J Virol. 1970 Jan;5(1):51–59. doi: 10.1128/jvi.5.1.51-59.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. ROIZMAN B., AURELIAN L. ABORTIVE INFECTION OF CANINE CELLS BY HERPES SIMPLEX VIRUS. I. CHARACTERIZATION OF VIRAL PROGENY FROM CO-OPERATIVE INFECTION WITH MUTANTS DIFFERING IN CAPACITY TO MULTIPLY IN CANINE CELLS. J Mol Biol. 1965 Mar;11:528–538. doi: 10.1016/s0022-2836(65)80008-0. [DOI] [PubMed] [Google Scholar]
  14. ROIZMAN B. Polykaryocytosis. Cold Spring Harb Symp Quant Biol. 1962;27:327–342. doi: 10.1101/sqb.1962.027.001.031. [DOI] [PubMed] [Google Scholar]
  15. ROIZMAN B., ROANE P. R., Jr A physical difference between two strains of herpes simplex virus apparent on sedimentation in cesium chloride. Virology. 1961 Sep;15:75–79. doi: 10.1016/0042-6822(61)90079-4. [DOI] [PubMed] [Google Scholar]
  16. ROIZMAN B., ROANE P. R., Jr Demonstration of a surface difference between virions of two strains of herpes simplex virus. Virology. 1963 Feb;19:198–204. doi: 10.1016/0042-6822(63)90009-6. [DOI] [PubMed] [Google Scholar]
  17. Roizman B., Spear P. G. Preparation of herpes simplex virus of high titer. J Virol. 1968 Jan;2(1):83–84. doi: 10.1128/jvi.2.1.83-84.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schwartz J., Roizman B. Similarities and Differences in the Development of Laboratory Strains and Freshly Isolated Strains of Herpes Simplex Virus in HEp-2 Cells: Electron Microscopy. J Virol. 1969 Dec;4(6):879–889. doi: 10.1128/jvi.4.6.879-889.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Spear P. G., Roizman B. Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J Virol. 1972 Jan;9(1):143–159. doi: 10.1128/jvi.9.1.143-159.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wagner E. K., Tewari K. K., Kolodner R., Warner R. C. The molecular size of the herpes simplex virus type 1 genome. Virology. 1974 Feb;57(2):436–447. doi: 10.1016/0042-6822(74)90183-4. [DOI] [PubMed] [Google Scholar]
  21. Wilkie N. M. The synthesis and substructure of herpesvirus DNA: the distribution of alkali-labile single strand interruptions in HSV-1 DNA. J Gen Virol. 1973 Dec;21(3):453–467. doi: 10.1099/0022-1317-21-3-453. [DOI] [PubMed] [Google Scholar]

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

RESOURCES