Resveratrol targets PD-L1 glycosylation and dimerization to enhance antitumor T-cell immunity
Identifieur interne : 000062 ( Main/Exploration ); précédent : 000061; suivant : 000063Resveratrol targets PD-L1 glycosylation and dimerization to enhance antitumor T-cell immunity
Auteurs : Sara Verdura [Espagne] ; Elisabet Cuyàs [Espagne] ; Eric Cortada [Espagne] ; Joan Brunet [Espagne] ; Eugeni Lopez-Bonet [Espagne] ; Bego A Martin-Castillo [Espagne] ; Joaquim Bosch-Barrera [Espagne] ; José Antonio Encinar [Espagne] ; Javier A. Menendez [Espagne]Source :
- Aging (Albany NY) [ 1945-4589 ] ; 2020.
Abstract
New strategies to block the immune evasion activity of programmed death ligand-1 (PD-L1) are urgently needed. When exploring the PD-L1-targeted effects of mechanistically diverse metabolism-targeting drugs, exposure to the dietary polyphenol resveratrol (RSV) revealed its differential capacity to generate a distinct PD-L1 electrophoretic migration pattern. Using biochemical assays, computer-aided docking/molecular dynamics simulations, and fluorescence microscopy, we found that RSV can operate as a direct inhibitor of glyco-PD-L1-processing enzymes (α-glucosidase/α-mannosidase) that modulate
Url:
DOI: 10.18632/aging.102646
PubMed: 31901900
PubMed Central: 6977679
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>New strategies to block the immune evasion activity of programmed death ligand-1 (PD-L1) are urgently needed. When exploring the PD-L1-targeted effects of mechanistically diverse metabolism-targeting drugs, exposure to the dietary polyphenol resveratrol (RSV) revealed its differential capacity to generate a distinct PD-L1 electrophoretic migration pattern. Using biochemical assays, computer-aided docking/molecular dynamics simulations, and fluorescence microscopy, we found that RSV can operate as a direct inhibitor of glyco-PD-L1-processing enzymes (α-glucosidase/α-mannosidase) that modulate <italic>N</italic>
-linked glycan decoration of PD-L1, thereby promoting the endoplasmic reticulum retention of a mannose-rich, abnormally glycosylated form of PD-L1. RSV was also predicted to interact with the inner surface of PD-L1 involved in the interaction with PD-1, almost perfectly occupying the target space of the small compound BMS-202 that binds to and induces dimerization of PD-L1. The ability of RSV to directly target PD-L1 interferes with its stability and trafficking, ultimately impeding its targeting to the cancer cell plasma membrane. Impedance-based real-time cell analysis (xCELLigence) showed that cytotoxic T-lymphocyte activity was notably exacerbated when cancer cells were previously exposed to RSV. This unforeseen immunomodulating mechanism of RSV might illuminate new approaches to restore T-cell function by targeting the PD-1/PD-L1 immunologic checkpoint with natural polyphenols.</p>
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<affiliations><list><country><li>Espagne</li>
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<name sortKey="Bosch Barrera, Joaquim" sort="Bosch Barrera, Joaquim" uniqKey="Bosch Barrera J" first="Joaquim" last="Bosch-Barrera">Joaquim Bosch-Barrera</name>
<name sortKey="Bosch Barrera, Joaquim" sort="Bosch Barrera, Joaquim" uniqKey="Bosch Barrera J" first="Joaquim" last="Bosch-Barrera">Joaquim Bosch-Barrera</name>
<name sortKey="Brunet, Joan" sort="Brunet, Joan" uniqKey="Brunet J" first="Joan" last="Brunet">Joan Brunet</name>
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<name sortKey="Cuyas, Elisabet" sort="Cuyas, Elisabet" uniqKey="Cuyas E" first="Elisabet" last="Cuyàs">Elisabet Cuyàs</name>
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<name sortKey="Encinar, Jose Antonio" sort="Encinar, Jose Antonio" uniqKey="Encinar J" first="José Antonio" last="Encinar">José Antonio Encinar</name>
<name sortKey="Lopez Bonet, Eugeni" sort="Lopez Bonet, Eugeni" uniqKey="Lopez Bonet E" first="Eugeni" last="Lopez-Bonet">Eugeni Lopez-Bonet</name>
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