Please use this identifier to cite or link to this item:
|Title:||Can glycosylation mask the detection of MHC expressing p53 peptides by T cell receptors?||Authors:||Nguyen, Thanh Binh
Lane, David P.
Verma, Chandra Shekhar
|Keywords:||Science::Biological sciences||Issue Date:||2021||Source:||Nguyen, T. B., Lane, D. P. & Verma, C. S. (2021). Can glycosylation mask the detection of MHC expressing p53 peptides by T cell receptors?. Biomolecules, 11(7), 1056-. https://dx.doi.org/10.3390/biom11071056||Journal:||Biomolecules||Abstract:||Proteins of the major histocompatibility complex (MHC) class I, or human leukocyte antigen (HLA) in humans interact with endogenous peptides and present them to T cell receptors (TCR), which in turn tune the immune system to recognize and discriminate between self and foreign (non-self) peptides. Of especial importance are peptides derived from tumor-associated antigens. T cells recognizing these peptides are found in cancer patients, but not in cancer-free individuals. What stimulates this recognition, which is vital for the success of checkpoint based therapy? A peptide derived from the protein p53 (residues 161-169 or p161) was reported to show this behavior. T cells recognizing this unmodified peptide could be further stimulated in vitro to create effective cancer killing CTLs (cytotoxic T lymphocytes). We hypothesize that the underlying difference may arise from post-translational glycosylation of p161 in normal individuals, likely masking it against recognition by TCR. Defects in glycosylation in cancer cells may allow the presentation of the native peptide. We investigate the structural consequences of such peptide glycosylation by investigating the associated structural dynamics.||URI:||https://hdl.handle.net/10356/160817||ISSN:||2218-273X||DOI:||10.3390/biom11071056||Schools:||School of Biological Sciences||Organisations:||Bioinformatics Institute, A*STAR
National University of Singapore
|Rights:||© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
Updated on Sep 25, 2023
Web of ScienceTM
Updated on Sep 26, 2023
Updated on Sep 23, 2023
Updated on Sep 23, 2023
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.