Benoit Van den EyndeLudwig Institute for Cancer Research, Université Catholique de Louvain, Brussels, Belgium F1000 Faculty Member (since 07 September 2010)
Director of the Ludwig Institute for Cancer Research Brussels Branch, Belgium
EDUCATION AND BACKGROUND:
Dr Van den Eynde earned his degree in medicine with the highest honors and, subsequently, his PhD from University College London.
He is a full member of the Royal Academy of Medicine of Belgium and the Academy of Cancer Immunology.
He has received several awards during his career, including the Prize of the 165th anniversary of the Royal Academy of Medicine of Belgium in 2001, the Francqui Chair at the Université libre de Bruxelles in 2005 and most recently the 2007 GlaxoSmithKline prize.
Dr Van den Eynde was one of the investigators involved in the first identification of cancer antigens recognized by T lymphocytes on mouse and human tumors. He subsequently gained a strong international recognition for his research on antigen processing and tumor immunology.
Among Dr Van den Eyndes most remarkable recent discoveries is that of a new mode of antigenic peptide processing. Cytolytic T lymphocytes (CTLs; immune cells that destroy cancer cells and other compromised cells) recognize antigens that are displayed on the cell surface by major histocompatibility complexes (MHC). The antigens are peptides produced by the cleavage and processing of cellular proteins by an intracellular protease complex called the proteasome. Dr Van den Eynde and his colleagues discovered that the proteasome was able not only to cleave proteins into peptidic fragments but also to splice peptidic fragments together, either in the right or the reverse order. This explains the production of 'spliced' antigenic peptides derived from non-contiguous protein fragments. Together with a previously described spliced peptide, the two spliced peptides described by the group in Science in 2004 and 2006 cast aside the paradigm that a peptide sequence is always determined by the DNA sequence encoding the protein from which the peptide is derived. The team of Dr Van den Eynde has also described differences in peptide processing between normal cells and certain immune cells, which express a distinct variant of the proteasome.
Dr Van den Eyndes team has also discovered a mechanism that suppresses immunity to tumors and may hamper the effect of current immunotherapies. This mechanism, which was previously described in the placenta, is based on the expression of the enzyme IDO, which rapidly degrades tryptophan and paralyzes lymphocytes by starving them of tryptophan. Dr Van den Eynde recently initiated a consortium, called Cantol, of several research units in Belgium working in collaboration with Olivier Michielin from LICR Lausanne Branch with the goal of developing small molecule inhibitors of IDO for cancer immunotherapy.
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