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10.1172/JCI85679 http://scihub22266oqcxt.onion/10.1172/JCI85679 C4887163!4887163!27183389     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Clin+Invest ä ; 126 (6): 2191-204 Nephropedia Template TP {{tp|p=27183389|t=ä. Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity |pdf=|usr=}}{{27183389}} gab.com Text Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity JO: J Clin Invest http://www.kidney.de/pget.php?&tw=1&pmid=27183389 #FOAvip The cross-reactivity of T cells with pathogen- and self-derived peptides has been implicated as a pathway involved in the development of autoimmunity. However, the mechanisms that allow the clonal T cell antigen receptor (TCR) to functionally engage multiple peptide?major histocompatibility complexes (pMHC) are unclear. Here, we studied multiligand discrimination by a human, preproinsulin reactive, MHC class-I?restricted CD8+ T cell clone (1E6) that can recognize over 1 million different peptides. We generated high-resolution structures of the 1E6 TCR bound to 7 altered peptide ligands, including a pathogen-derived peptide that was an order of magnitude more potent than the natural self-peptide. Evaluation of these structures demonstrated that binding was stabilized through a conserved lock-and-key?like minimal binding footprint that enables 1E6 TCR to tolerate vast numbers of substitutions outside of this so-called hotspot. Highly potent antigens of the 1E6 TCR engaged with a strong antipathogen-like binding affinity; this engagement was governed though an energetic switch from an enthalpically to entropically driven interaction compared with the natural autoimmune ligand. Together, these data highlight how T cell cross-reactivity with pathogen-derived antigens might break self-tolerance to induce autoimmune disease. Twit Text FOAVip Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity ????J Clin Invest http://www.kidney.de/pget.php?&tw=1&pmid=27183389 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27183389 #FOAvip English Wikipedia <ref>{{Cite pmid|27183389}}</ref> Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity #MMPMID27183389 Cole DK; Bulek AM; Dolton G; Schauenberg AJ; Szomolay B; Rittase W; Trimby A; Jothikumar P; Fuller A; Skowera A; Rossjohn J; Zhu C; Miles JJ; Peakman M; Wooldridge L; Rizkallah PJ; Sewell AK J Clin Invest ä[]; 126 (6): 2191-204 PMID27183389show ga The cross-reactivity of T cells with pathogen- and self-derived peptides has been implicated as a pathway involved in the development of autoimmunity. However, the mechanisms that allow the clonal T cell antigen receptor (TCR) to functionally engage multiple peptide?major histocompatibility complexes (pMHC) are unclear. Here, we studied multiligand discrimination by a human, preproinsulin reactive, MHC class-I?restricted CD8+ T cell clone (1E6) that can recognize over 1 million different peptides. We generated high-resolution structures of the 1E6 TCR bound to 7 altered peptide ligands, including a pathogen-derived peptide that was an order of magnitude more potent than the natural self-peptide. Evaluation of these structures demonstrated that binding was stabilized through a conserved lock-and-key?like minimal binding footprint that enables 1E6 TCR to tolerate vast numbers of substitutions outside of this so-called hotspot. Highly potent antigens of the 1E6 TCR engaged with a strong antipathogen-like binding affinity; this engagement was governed though an energetic switch from an enthalpically to entropically driven interaction compared with the natural autoimmune ligand. Together, these data highlight how T cell cross-reactivity with pathogen-derived antigens might break self-tolerance to induce autoimmune disease. äHotspot autoimmune T cell receptor binding underlies pathogen and insu(epmc).pdf DeepDyve Pubget Overpricing