Please use this identifier to cite or link to this item: https://doi.org/10.3390/biom11071056
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dc.titleCan glycosylation mask the detection of mhc expressing p53 peptides by t cell receptors?
dc.contributor.authorThanh Binh Nguyen
dc.contributor.authorLane, David P.
dc.contributor.authorVerma, Chandra S.
dc.date.accessioned2022-10-11T07:56:06Z
dc.date.available2022-10-11T07:56:06Z
dc.date.issued2021-07-19
dc.identifier.citationThanh 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. https://doi.org/10.3390/biom11071056
dc.identifier.issn2218-273X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/232058
dc.description.abstractProteins 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.
dc.publisherMDPI AG
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2021
dc.subjectGlycosylation
dc.subjectHLA-A24
dc.subjectMolecular dynamics
dc.subjectP53
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.3390/biom11071056
dc.description.sourcetitleBiomolecules
dc.description.volume11
dc.description.issue7
dc.description.page1056
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