Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8 + T cells
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-sho...
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Published in | Nature immunology Vol. 6; no. 6; pp. 593 - 599 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Nature Publishing Group
01.06.2005
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Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1529-2908 1529-2916 |
DOI: | 10.1038/ni1201 |