Lysis of target cells infected with vesicular stomatitis virus (VSV) in the presence of tunicamycin by anti-VSV cytotoxic T lymphocytes

D. T. Harris, A. H. Hale, L. Lefrancois

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

We have analyzed the requirement for the expression of the major surface glycoprotein (G protein) of vesicular stomatitis virus (VSV) on target cells for recognition and lysis by anti-VSV cytotoxic T lymphocytes (CTL). In addition, we have attempted to determine if the carbohydrate moieties on the G protein are required for recognition and lysis by anti-VSV CTL. When VSV (Orsay) is grown at 30°C in the presence of tunicamycin (TM), glycosylation of G protein is inhibited; however, nonglycosylated G protein is found on the surface of the cell and active virus particles are produced. In contrast, VSV (Orsay) grown at 39°C in the presence of TM produces low titers of virus and the presence of G protein on the surface of cells is not detectable. The susceptibility of these target cells to lysis by anti-VSV CTL was analyzed. The results suggest that expression of the G protein is required for target cell lysis by anti-VSV CTL. However, the presence of the carbohydrate moieties on the G protein are not an absolute requirement for recognition by anti-VSV CTL. VSV-infected target cells incubated in the presence of TM were lysed by anti-VSV CTL up to 50 to 80% of the infected target cell control. This result suggests either that some clones of anti-VSV CTL recognize carbohydrate moieties or that carbohydrate moieties play some as yet undefined nonantigenic role in the recognition of the target antigen by the CTL receptor.

Original languageEnglish (US)
Pages (from-to)1914-1918
Number of pages5
JournalJournal of Immunology
Volume126
Issue number5
StatePublished - Jan 1 1981
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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