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Intact mass analysis reveals the novel O-linked glycosylation on the stalk region of PD-1 protein

Programmed cell death protein 1 (PD-1) is a key receptor in the immune checkpoint pathway and has emerged to be a promising target for cancer therapy. PD-1 consists of an intracellular domain followed by a transmembrane domain that is connected to the extracellular domain by the stalk region. Althou...

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Detalles Bibliográficos
Autores principales: Tit-oon, Phanthakarn, Wonglangka, Arisa, Boonkanta, Klaichan, Ruchirawat, Mathuros, Fuangthong, Mayuree, Sasisekharan, Ram, Khongmanee, Amnart
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10267102/
https://www.ncbi.nlm.nih.gov/pubmed/37316505
http://dx.doi.org/10.1038/s41598-023-36203-3
Descripción
Sumario:Programmed cell death protein 1 (PD-1) is a key receptor in the immune checkpoint pathway and has emerged to be a promising target for cancer therapy. PD-1 consists of an intracellular domain followed by a transmembrane domain that is connected to the extracellular domain by the stalk region. Although the PD-1 structure has been studied for more than two decades, the posttranslational modification of this protein has been incompletely characterized. In this study, we identified the previously undescribed modification sites of O-linked glycan on the stalk region of PD-1 protein using O-protease digestion coupling with intact mass analysis. The result indicates that T153, S157, S159, and T168 are modified by sialylated mucin-type O-glycan with core 1- and core 2-based structures. This study provides both information on potential novel modification sites on the PD-1 protein and an attractive method for identifying O-linked glycosylation using a specific enzyme and intact mass analysis.