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. 1972 Oct;10(4):578–585. doi: 10.1128/jvi.10.4.578-585.1972

Effect of Vesicular Stomatitis Virus Infection on the Histocompatibility Antigen of L Cells

Toby T Hecht 1, Donald F Summers 1
PMCID: PMC356506  PMID: 4343540

Abstract

When mouse L cells are infected for 22 hr with vesicular stomatitis virus (VSV), a ribonucleic acid-containing enveloped virus, greater than 70% of the major histocompatibility antigen (H-2), is no longer detectable by the method of inhibition of immune cytolysis. Infected cells prelabeled with 14C-glucosamine also show a correspondingly greater loss of trichloroacetic acid-insoluble radioactivity than uninfected cells. The loss of H-2 antigenic activity is not due to the viral inhibition of host cell protein synthesis since cells cultured for 18 hr in the presence of cycloheximide have the same amount of H-2 activity as untreated controls. Also, cells infected with encephalomyocarditis virus, a picornavirus, show no loss of H-2 activity at a time when host cell protein synthesis is completely inhibited. VSV structural proteins associated in vitro with uninfected L-cell plasma membranes do not render H-2 sites inaccessible to the assay. Although antibodies may not combine with all the H-2 antigenic sites on the plasma membrane, anti-H-2 serum reacted with L cells before infection does not prevent a normal infection with VSV. H-2 activity can be detected in virus samples purified from the medium of infected L cells; this virus purified after being mixed with L-cell homogenates shows greater H-2 activity than virus purified after being mixed with HeLa cell homogenates. However, VSV made in HeLa cells shows no H-2 activity when mixed with L-cell homogenates.

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Selected References

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

  1. Atkinson P. H., Summers D. F. Purification and properties of HeLa cell plasma membranes. J Biol Chem. 1971 Aug 25;246(16):5162–5175. [PubMed] [Google Scholar]
  2. Boyse E. A., Old L. J., Stockert E. An approach to the mapping of antigens on the cell surface. Proc Natl Acad Sci U S A. 1968 Jul;60(3):886–893. doi: 10.1073/pnas.60.3.886. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Burge B. W., Huang A. S. Comparison of membrane protein glycopeptides of Sindbis virus and vesicular stomatitis virus. J Virol. 1970 Aug;6(2):176–182. doi: 10.1128/jvi.6.2.176-182.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cohen G. H., Atkinson P. H., Summers D. F. Interactions of vesicular stomatitis virus structural proteins with HeLa plasma membranes. Nat New Biol. 1971 May 26;231(21):121–123. doi: 10.1038/newbio231121a0. [DOI] [PubMed] [Google Scholar]
  5. HOWATSON A. F., WHITMORE G. F. The development and structure of vesicular stomatitis virus. Virology. 1962 Apr;16:466–478. doi: 10.1016/0042-6822(62)90228-3. [DOI] [PubMed] [Google Scholar]
  6. Hecht T. T., Summers D. F. The effect of phleomycin on poliovirus RNA replication. Virology. 1970 Mar;40(3):441–447. doi: 10.1016/0042-6822(70)90187-x. [DOI] [PubMed] [Google Scholar]
  7. Heine J. W., Schnaitman C. A. Entry of vesicular stomatitis virus into L cells. J Virol. 1971 Nov;8(5):786–795. doi: 10.1128/jvi.8.5.786-795.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Holland J. J., Kiehn E. D. Influenza virus effects on cell membrane proteins. Science. 1970 Jan 9;167(3915):202–205. doi: 10.1126/science.167.3915.202. [DOI] [PubMed] [Google Scholar]
  9. Kang C. Y., Prevec L. Proteins of vesicular stomatitis virus. I. Polyacrylamide gel analysis of viral antigens. J Virol. 1969 Apr;3(4):404–413. doi: 10.1128/jvi.3.4.404-413.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Klenk H. D., Choppin P. W. Glycosphingolipids of plasma membranes of cultured cells and an enveloped virus (SV5) grown in these cells. Proc Natl Acad Sci U S A. 1970 May;66(1):57–64. doi: 10.1073/pnas.66.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Klenk H. D., Choppin P. W. Lipids of plasma membranes of monkey and hamster kidney cells and of parainfluenza virions grown in these cells. Virology. 1969 Jun;38(2):255–268. doi: 10.1016/0042-6822(69)90367-5. [DOI] [PubMed] [Google Scholar]
  12. Klenk H. D., Compans R. W., Choppin W. P. An electron microscopic study of the presence or absence of neuraminic acid in enveloped viruses. Virology. 1970 Dec;42(4):1158–1162. doi: 10.1016/0042-6822(70)90368-5. [DOI] [PubMed] [Google Scholar]
  13. McSharry J. J., Compans R. W., Choppin P. W. Proteins of vesicular stomatitis virus and of phenotypically mixed vesicular stomatitis virus-simian virus 5 virions. J Virol. 1971 Nov;8(5):722–729. doi: 10.1128/jvi.8.5.722-729.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. McSharry J. J., Wagner R. R. Carbohydrate composition of vesicular stomatitis virus. J Virol. 1971 Mar;7(3):412–415. doi: 10.1128/jvi.7.3.412-415.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McSharry J., Benzinger R. Concentration and purification of vesicular stomatitis virus by polyethylene glycol "precipitation". Virology. 1970 Mar;40(3):745–746. doi: 10.1016/0042-6822(70)90219-9. [DOI] [PubMed] [Google Scholar]
  16. Mudd J. A., Summers D. F. Protein synthesis in vesicular stomatitis virus-infected HeLa cells. Virology. 1970 Oct;42(2):328–340. doi: 10.1016/0042-6822(70)90277-1. [DOI] [PubMed] [Google Scholar]
  17. Muramatsu T., Nathenson S. G. Studies on the carbohydrate portion of membrane-located mouse H-2 alloantigens. Biochemistry. 1970 Dec 8;9(25):4875–4883. doi: 10.1021/bi00827a008. [DOI] [PubMed] [Google Scholar]
  18. Nathenson S. G. Biochemical properties of histocompatibility antigens. Annu Rev Genet. 1970;4(0):69–90. doi: 10.1146/annurev.ge.04.120170.000441. [DOI] [PubMed] [Google Scholar]
  19. Nathenson S. G., Davies D. A. Solubilization and partial purification of mouse histocompatibility antigens from a membranous lipoprotein fraction. Proc Natl Acad Sci U S A. 1966 Aug;56(2):476–483. doi: 10.1073/pnas.56.2.476. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SANDERSON A. R. CYTOTOXIC REACTIONS OF MOUSE ISO-ANTISERA: PRELIMINARY CONSIDERATIONS. Br J Exp Pathol. 1964 Aug;45:398–408. [PMC free article] [PubMed] [Google Scholar]
  21. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  22. WIGZELL H. QUANTITATIVE TITRATIONS OF MOUSE H-2 ANTIBODIES USING CR-51-LABELLED TARGET CELLS. Transplantation. 1965 May;3:423–431. doi: 10.1097/00007890-196505000-00011. [DOI] [PubMed] [Google Scholar]
  23. Wagner R. R., Kiley M. P., Snyder R. M., Schnaitman C. A. Cytoplasmic compartmentalization of the protein and ribonucleic acid species of vesicular stomatitis virus. J Virol. 1972 Apr;9(4):672–683. doi: 10.1128/jvi.9.4.672-683.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Wallis C., Melnick J. L. Stabilization of enveloped viruses by dimethyl sulfoxide. J Virol. 1968 Sep;2(9):953–954. doi: 10.1128/jvi.2.9.953-954.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Wertz G. W., Youngner J. S. Inhibition of protein synthesis in L cells infected with vesicular stomatitis virus. J Virol. 1972 Jan;9(1):85–89. doi: 10.1128/jvi.9.1.85-89.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Zee Y. C., Hackett A. J., Talens L. Vesicular stomatitis virus maturation sites in six different host cells. J Gen Virol. 1970;7(2):95–102. doi: 10.1099/0022-1317-7-2-95. [DOI] [PubMed] [Google Scholar]

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