Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells
- 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
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.
Comment in
-
Escort service for cross-priming.Nat Immunol. 2005 Jun;6(6):543-4. doi: 10.1038/ni0605-543. Nat Immunol. 2005. PMID: 15908932 No abstract available.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials