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

Nat Immunol. 2005 Jun;6(6):593-9. doi: 10.1038/ni1201. Epub 2005 May 1.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigen Presentation*
  • Antigens / administration & dosage
  • Antigens / metabolism
  • CD8-Positive T-Lymphocytes / immunology*
  • Cell Line
  • Female
  • Heat-Shock Proteins / metabolism*
  • In Vitro Techniques
  • Mice
  • Mice, Inbred C57BL
  • Molecular Chaperones / metabolism*
  • Multiprotein Complexes
  • Ovalbumin / immunology
  • Peptides / immunology*


  • Antigens
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Multiprotein Complexes
  • Peptides
  • Ovalbumin