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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-.
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.
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:// 4.0/).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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