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J Immunol. 2009 Oct 1;183(7):4205-10. doi: 10.4049/jimmunol.0901828. Epub 2009 Sep 14.

Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent.

Author information

1
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.

Erratum in

  • J Immunol. 2010 Jul 1;185(1):770.

Abstract

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.

PMID:
19752220
PMCID:
PMC2749969
DOI:
10.4049/jimmunol.0901828
[Indexed for MEDLINE]
Free PMC Article

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