Paradigm Shift Therapeutics LLC, Rockville, Maryland, United States of America.
Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
PLoS One. 2020 Apr 2;15(4):e0226661. doi: 10.1371/journal.pone.0226661. eCollection 2020.
CD47 is an immune checkpoint protein that downregulates both the innate and adaptive anti-tumor immune response via its counter receptor SIRPα. Biologics, including humanized CD47 monoclonal antibodies and decoy SIRPα receptors, that block the SIRPα-CD47 interaction, are currently being developed as cancer immunotherapy agents. However, adverse side effects and limited penetration of tumor tissue associated with their structure and large size may impede their clinical application. We recently developed a quantitative high throughput screening assay platform to identify small molecules that disrupt the binding of SIRPα and CD47 as an alternative approach to these protein-based therapeutics. Here, we report on the development and optimization of a cell-based binding assay to validate active small molecules from our biochemical screening effort. This assay has a low volume, high capacity homogenous format that relies on laser scanning cytometry (LSC) and associated techniques to enhance signal to noise measurement of cell surface binding. The LSC assay is specific, concentration dependent, and validated for the two major human SIRPα variants (V1 and V2), with results that parallel those of our biochemical data as well as published studies. We also utilized the LSC assay to confirm published studies showing that the inhibition of amino-terminal pyroglutamate formation on CD47 using the glutaminyl cyclase inhibitor SEN177 disrupts SIRPα binding. The SIRPα-CD47 interaction could be quantitatively measured in live and fixed tumor cells. Use of fixed cells reduces the burden of cell maintenance and provides stable cell standards to control for inter- and intra-assay variations. We also demonstrate the utility of the assay to characterize the activity of the first reported small molecule antagonists of the SIRPα-CD47 interaction. This assay will support the screening of thousands of compounds to identify or validate active small molecules as hits, develop structure activity relationships and assist in the optimization of hits to leads by a typical iterative medicinal chemistry campaign.
CD47 是一种免疫检查点蛋白,通过其受体 SIRPα 下调先天和适应性抗肿瘤免疫反应。目前正在开发阻断 SIRPα-CD47 相互作用的生物制剂,包括人源化 CD47 单克隆抗体和诱饵 SIRPα 受体,作为癌症免疫疗法。然而,与其结构和尺寸相关的不良反应和肿瘤组织穿透有限可能会阻碍其临床应用。我们最近开发了一种高通量筛选测定平台,以鉴定破坏 SIRPα 和 CD47 结合的小分子,作为这些基于蛋白质的治疗方法的替代方法。在这里,我们报告了开发和优化基于细胞的结合测定法的情况,以验证我们生化筛选工作中的活性小分子。该测定法具有低体积、大容量均相格式,依赖于激光扫描 cytometry(LSC)和相关技术来增强细胞表面结合的信号与噪声测量。LSC 测定法是特异性的、浓度依赖性的,并且针对两种主要的人类 SIRPα 变体(V1 和 V2)进行了验证,其结果与我们的生化数据以及已发表的研究结果相平行。我们还利用 LSC 测定法证实了已发表的研究结果,即使用谷氨酰胺环化酶抑制剂 SEN177 抑制 CD47 的 N 端焦谷氨酸形成会破坏 SIRPα 结合。可以在活细胞和固定肿瘤细胞中定量测量 SIRPα-CD47 相互作用。使用固定细胞可以减少细胞维持的负担,并提供稳定的细胞标准来控制分析内和分析间的变异性。我们还证明了该测定法在表征 SIRPα-CD47 相互作用的第一种报道的小分子拮抗剂的活性方面的用途。该测定法将支持筛选数千种化合物,以鉴定或验证作为命中的活性小分子,开发结构活性关系,并通过典型的迭代药物化学运动协助命中物向先导物的优化。