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丁酰膦蛋白 3 配体的结构-活性关系。

Structure-Activity Relationships of Butyrophilin 3 Ligands.

机构信息

Department of Pharmaceutical Sciences and Institute for Systems Genomics, University of Connecticut, 69N. Eagleville Road, Storrs, CT, 06269, USA.

出版信息

ChemMedChem. 2020 Jun 17;15(12):1030-1039. doi: 10.1002/cmdc.202000198. Epub 2020 May 26.

Abstract

Phosphoantigens (pAgs) are small phosphorus-containing molecules that stimulate Vγ9Vδ2 T cells with sub-nanomolar cellular potency. Recent work has revealed that these compounds work through binding to the transmembrane immunoglobulin butyrophilin 3A1 (BTN3A1) within its intracellular B30.2 domain. Engagement of BTN3A1 is critical to the formation of an immune synapse between cells that contain pAgs and the Vγ9Vδ2 T cells. This minireview summarizes the structure-activity relationships of pAgs and their implications to the mechanisms of butyrophilin 3 activation leading to Vγ9Vδ2 T cell response.

摘要

磷酸抗原(pAgs)是含有少量磷的分子,能以亚纳摩尔级的细胞效力刺激 Vγ9Vδ2 T 细胞。最近的研究表明,这些化合物通过与细胞内 B30.2 结构域内的跨膜免疫球蛋白丁酰磷酸蛋白 3A1(BTN3A1)结合而起作用。BTN3A1 的结合对于含有 pAgs 的细胞与 Vγ9Vδ2 T 细胞之间免疫突触的形成至关重要。这篇小综述总结了 pAg 的结构-活性关系及其对 BTN3A1 激活导致 Vγ9Vδ2 T 细胞反应机制的影响。

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