Design of short peptides to block BTLA/HVEM interactions for promoting anticancer T-cell responses.

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ID: 73717
2017
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Abstract
Antibody based immune-checkpoint blockade therapy is a major breakthrough in oncology, leading to clinical benefit for cancer patients. Among the growing family of inhibitory receptors, the B and T lymphocyte attenuator (BTLA), which interacts with herpes virus entry mediator (HVEM), is a promising target for immunotherapy. Indeed, BTLA inhibits T-cell proliferation and cytokine production. The crystal structure of the BTLA/HVEM complex has shown that the HVEM(26-38) fragment is directly involved in protein binding. We designed and analyzed the capacity of several analogs of this fragment to block the ligation between BTLA and HVEM, using competitive ELISA and cellular assay. We found that the HVEM(23-39) peptide can block BTLA/HVEM ligation. However, the blocking ability was due to the Cys encompassed in this peptide and that even free cysteine targeted the BTLA protein and blocked its interaction with HVEM. These data highlight a Cys-related artefact in vitro, which should be taken in consideration for future development of BTLA/HVEM blocking compounds.
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spodzieja2017designplos Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Spodzieja, Marta;Lach, Sławomir;Iwaszkiewicz, Justyna;Cesson, Valérie;Kalejta, Katarzyna;Olive, Daniel;Michielin, Olivier;Speiser, Daniel E;Zoete, Vincent;Derré, Laurent;Rodziewicz-Motowidło, Sylwia;
Journal PloS one
Year 2017
DOI
DOI not found
URL
http://europepmc.org/articles/PMC5464627?pdf=render
Keywords
Education Biology (General) Medicine Science public aspects of medicine education (general)

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