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N-terminal peptides of LAG-3 (WT, V20A, and L14Q/V20A) were quantified by PRM

ABSTRACT: The abundance of N-terminal fragments starting from V21 (pV21–W33), S22 (pS22–W33), S23 (pS23–W33), and G24 (pG24–W33) along with three control peptides (Ctrl1, pH81–Y95; Ctrl2, pR106–L118; Ctrl3, pH113–L123) were measured by parallel reaction monitoring (PRM), an MS/MS-based targeted quantification method using high-resolution MS. Targeted MS/MS scans were acquired by a time-scheduled inclusion list, and time alignment and relative quantification of the transitions of three biological replicates were performed with PinPoint version 1.4 (Thermo Fisher Scientific).

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hidetaka Kosako

PROVIDER: PXD023930 | JPOST Repository | Mon Apr 11 00:00:00 BST 2022

REPOSITORIES: jPOST

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			Action	DRS
	1_PRM_2_WT.raw	Raw
	200626_LAG3_PRM_n3_BR.xlsx	Xlsx
	2_PRM_5_WT.raw	Raw
	3_PRM_8_WT.raw	Raw
	4_PRM_3_V20A.raw	Raw

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Publications

Binding of LAG-3 to stable peptide-MHC class II limits T cell function and suppresses autoimmunity and anti-cancer immunity.

Maruhashi Takumi T Sugiura Daisuke D Okazaki Il-Mi IM Shimizu Kenji K Maeda Takeo K TK Ikubo Jun J Yoshikawa Harunori H Maenaka Katsumi K Ishimaru Naozumi N Kosako Hidetaka H Takemoto Tatsuya T Okazaki Taku T

Immunity 20220411 5

Lymphocyte activation gene-3 (LAG-3) is a potent inhibitory co-receptor; yet, its functional ligand remains elusive, with distinct potential ligands identified. Here, we investigated the relative contribution of potential ligands, stable peptide-MHC class II complexes (pMHCII) and fibrinogen-like protein 1 (FGL1), to LAG-3 activity in vitro and in vivo. Binding of LAG-3 to stable pMHCII but not to FGL1 induced T cell suppression in vitro. Consistently, LAG-3 mutants lacking FGL1-binding capacity ...[more]

PMID: 35413245

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