Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function

Amy D H Doody, Joseph T. Kovalchin, Marianne A. Mihalyo, Adam T. Hagymasi, Charles G. Drake, Adam J. Adler

Research output: Contribution to journalArticle

Abstract

The ability of mature T lymphocytes to develop effector capacity after encounter with cognate Ag is generally dependent upon inflammatory signals associated with infection that induce dendritic cell activation maturation. These inflammatory signals can derive directly from pathogens or can be expressed by host cells in response to infection. Heat shock proteins (HSPs) are a class of host-derived inflammatory mediators that perform the duel function of both chaperoning MHC class I-restricted epitopes into the cross-presentation pathway of DCs and inducing the activation/maturation of these DCs to allow priming of cognate CD8+ T cell effector responses. Although the ability of HSPs to elicit effector CD8 cell responses has been well established, their potential to prime CD4 cell effector responses has been relatively unexplored. In the current study we compared the ability of the endoplasmic reticilum-resident HSP gp96 to prime CD4 vs CD8 cells using TCR transgenic adoptive transfer systems and soluble gp96-peptide complexes. As expected, gp96 facilitated the cross-presentation of a class I-restricted peptide and priming of effector function in cognate CD8 cells. Interestingly, gp96 also facilitated the in vivo presentation of a class II- restricted peptide; however, the resulting CD4 cell response did not involve the development of effector function. Taken together, these data suggest that gp96 is an inflammatory mediator that selectively primes CD8 cell effector function.

Original languageEnglish (US)
Pages (from-to)6087-6092
Number of pages6
JournalJournal of Immunology
Volume172
Issue number10
StatePublished - May 15 2004

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Epitopes
Glycoproteins
T-Lymphocytes
Heat-Shock Proteins
Cross-Priming
Peptides
Adoptive Transfer
Infection
Dendritic Cells

ASJC Scopus subject areas

  • Immunology

Cite this

Doody, A. D. H., Kovalchin, J. T., Mihalyo, M. A., Hagymasi, A. T., Drake, C. G., & Adler, A. J. (2004). Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function. Journal of Immunology, 172(10), 6087-6092.

Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function. / Doody, Amy D H; Kovalchin, Joseph T.; Mihalyo, Marianne A.; Hagymasi, Adam T.; Drake, Charles G.; Adler, Adam J.

In: Journal of Immunology, Vol. 172, No. 10, 15.05.2004, p. 6087-6092.

Research output: Contribution to journalArticle

Doody, ADH, Kovalchin, JT, Mihalyo, MA, Hagymasi, AT, Drake, CG & Adler, AJ 2004, 'Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function', Journal of Immunology, vol. 172, no. 10, pp. 6087-6092.
Doody, Amy D H ; Kovalchin, Joseph T. ; Mihalyo, Marianne A. ; Hagymasi, Adam T. ; Drake, Charles G. ; Adler, Adam J. / Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function. In: Journal of Immunology. 2004 ; Vol. 172, No. 10. pp. 6087-6092.
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