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Vaccinia Virus WR induces rapid surface expression of a host molecule detected by the antibody 4C7 that is distinct from CLEC2D

  • Author(s) / Creator(s)
  • Poxviruses generally limit production of cellular proteins, which provides a mechanism for natural killer (NK) cells to detect infection through loss of cell surface proteins that engage NK cell inhibitory receptors. In this study we examined the effect of active infection with vaccinia virus Western Reserve (VACV WR) on expression of the NK inhibitory ligand, CLEC2D. CLEC2D is induced by Respiratory Syncytial virus (RSV) infection or by various inflammatory stimuli. Following VACV infection of 221 cells, the prototypic NK cell tumour target, we detected a dramatic increase in surface proteins using the antibody 4C7. The infection did not promote NK cell detection of a CLEC2D ligand. Out of four CLEC2D antibodies tested, only 4C7 detected a large increase in surface proteins suggesting that the bulk of the signal is from a protein distinct from any of the known transmembrane isoforms of CLEC2D. The initial increase in 4C7 signal does not depend on new transcription or translation of either a cellular or viral protein. Increased 4C7 signal occurs within five minutes of exposure to the virus and an intracellular pool of a 4C7 reactive molecule is detectable in 221 cells. Sustained surface expression of the 4C7 reactive protein is diminished at late time points with inhibition of DNA replication, and UV-inactivation. Inhibitors of virus binding also prevent its upregulation. This increase in 4C7 signal is not seen with other viruses tested here and is much more pronounced with VACV WR than with VACV Copenhagen. To our knowledge, this is the first report of a poxvirus leading to rapid externalization of a host protein.

  • Date created
    2016
  • Subjects / Keywords
  • Type of Item
    Article (Published)
  • DOI
    https://doi.org/10.7939/R3N010816
  • License
    Attribution-NoDerivatives 4.0 International