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Cross-presentation enables dendritic cells to present on their MHC class I molecules antigenic peptides derived from exogenous material, through a mechanism that remains partly unclear. It is particularly efficient with long peptides, which are used in cancer vaccines. We studied the mechanism of long-peptide cross-presentation using human dendritic cells and specific CTL clones against melanoma Ags gp100 and Melan-A/MART1. We found that cross-presentation of those long peptides does not depend on the proteasome or the transporter associated with Ag processing, and therefore follows a vacuolar pathway. We also observed that it makes use of newly synthesized MHC class I molecules, through peptide exchange in vesicles distinct from the endoplasmic reticulum and classical secretory pathway, in an SEC22b- and CD74-independent manner. Our results indicate a nonclassical secretion pathway followed by nascent HLA-I molecules that are used for cross-presentation of those long melanoma peptides in the vacuolar pathway. Our results may have implications for the development of vaccines based on long peptides.

Original publication




Journal article


Journal of immunology (Baltimore, Md. : 1950)

Publication Date





1711 - 1720


Ludwig Institute for Cancer Research, Brussels B-1200, Belgium; Walloon Excellence in Life Sciences and Biotechnology, Brussels B-1200, Belgium; de Duve Institute, Université Catholique de Louvain, Brussels B-1200, Belgium;


Dendritic Cells, T-Lymphocytes, Cytotoxic, Cells, Cultured, Cell Line, Vacuoles, Humans, Proteasome Endopeptidase Complex, Peptides, Histocompatibility Antigens Class I, Cross-Priming, Antigen Presentation, gp100 Melanoma Antigen