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

• Published in: Nature immunology Vol. 6; no. 6; pp. 593 - 599
• Main Authors: Srivastava, Pramod K, Binder, Robert J
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.06.2005
• Subjects: Animals; Antigen Presentation; Antigen-presenting cells; Antigens; Antigens - administration & dosage; Antigens - metabolism; CD8 antigen; CD8-Positive T-Lymphocytes - immunology; Cell Line; Female; Heat; Heat shock proteins; Heat-Shock Proteins - metabolism; Immunization; In Vitro Techniques; Lymphocytes T; Lysates; Mice; Mice, Inbred C57BL; Molecular Chaperones - metabolism; Multiprotein Complexes; Ovalbumin; Ovalbumin - immunology; Peptides; Peptides - immunology; Proteins; Shock; β-Galactosidase
• ISSN: 1529-2908; 1529-2916
• DOI: 10.1038/ni1201

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.