Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent.
Cross-priming, the activation of naive CD8+ T cells by dendritic cells presenting Ags synthesized by other cells, is believed to play an important role in the generation of antiviral and antitumor responses. The molecular mechanism(s) underlying cross-priming remain poorly defined and highly controversial. GRP94 (gp96), an abundant endoplasmic reticulum chaperone with innate immune-activating capacity, has been widely reported to play a major role in cross-priming. In this study, we show that cells whose expression of GRP94 is silenced via transient or stable transfection with GRP94-directed small interfering RNAs demonstrate no reduction in their abilities to generate class I peptide complexes in cultured cells or to prime antiviral CD8+ T cell responses in vivo. In demonstrating the dispensability of GRP94, our finding points to the importance of alternative mechanisms for generation of class I peptide complexes from endogenous and exogenous Ags and immunogens.
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- Vesicular stomatitis Indiana virus
- Vaccinia virus
- RNA, Small Interfering
- Peptide Fragments
- Mice, Transgenic
- Mice, Inbred C57BL
- Mice
- Membrane Glycoproteins
- Influenza A virus
- Immunology
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Vesicular stomatitis Indiana virus
- Vaccinia virus
- RNA, Small Interfering
- Peptide Fragments
- Mice, Transgenic
- Mice, Inbred C57BL
- Mice
- Membrane Glycoproteins
- Influenza A virus
- Immunology