Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells - PubMed (original) (raw)

doi: 10.1038/ni1201. Epub 2005 May 1.

Affiliations

PMID: 15864309
DOI: 10.1038/ni1201

Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells

Robert J Binder et al. Nat Immunol. 2005 Jun.

Abstract

The form in which antigens are transferred from cancer cells or infected cells to antigen-presenting cells as a part of the process of priming CD8(+) T cells has been a longstanding unresolved issue. Intact proteins or protein fragments in the form of free peptides or peptides chaperoned by heat-shock protein are possible sources of antigen. We address this here using beta-galactosidase and ovalbumin. Immunization with cell lysates containing intact proteins and heat-shock protein-peptide complexes or with cell lysates depleted of either component demonstrated that protein fragments chaperoned by heat-shock protein and not intact protein were the necessary and sufficient source of antigen transferred to antigen-presenting cells for priming CD8(+) T cell responses.

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Comment in

Escort service for cross-priming.
Melief CJ. Melief CJ. Nat Immunol. 2005 Jun;6(6):543-4. doi: 10.1038/ni0605-543. Nat Immunol. 2005. PMID: 15908932 No abstract available.

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Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells - PubMed (original) (raw)