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Title: Can glycosylation mask the detection of mhc expressing p53 peptides by t cell receptors?
Authors: Thanh Binh Nguyen
Lane, David P.
Verma, Chandra S. 
Keywords: Glycosylation
Molecular dynamics
Issue Date: 19-Jul-2021
Publisher: MDPI AG
Citation: Thanh Binh Nguyen, Lane, David P., Verma, Chandra S. (2021-07-19). Can glycosylation mask the detection of mhc expressing p53 peptides by t cell receptors?. Biomolecules 11 (7) : 1056. ScholarBank@NUS Repository.
Rights: Attribution 4.0 International
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 pep-tide. We investigate the structural consequences of such peptide glycosylation by investigating the associated structural dynamics. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
Source Title: Biomolecules
ISSN: 2218-273X
DOI: 10.3390/biom11071056
Rights: Attribution 4.0 International
Appears in Collections:Staff Publications

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