Department of Pediatrics, The University of Texas MD Anderson Cancer Center, Houston, Texas, United States of America.
PLoS One. 2022 Oct 6;17(10):e0274601. doi: 10.1371/journal.pone.0274601. eCollection 2022.
Receptor-ligand binding has been analyzed at the protein level using isothermal titration calorimetry and surface plasmon resonance and at the cellular level using interaction-associated downstream gene induction/suppression. However, no currently available technique can characterize this interaction directly through visualization. In addition, all available assays require a large pool of cells; no assay capable of analyzing receptor-ligand interactions at the single-cell level is publicly available. Here, we describe a new microfluidic chip-based technique for analyzing and visualizing these interactions at the single-cell level. First, a protein is immobilized on a glass slide and a low-flow-rate pump is used to isolate cells that express receptors that bind to the immobilized ligand. Specifically, we demonstrate the efficacy of this technique by immobilizing biotin-conjugated FGL2 on an avidin-coated slide chip and passing a mixture of GFP-labeled wild-type T cells and RFP-labeled FcγRIIB-knockout T cells through the chip. Using automated scanning and counting, we found a large number of GFP+ T cells with binding activity but significantly fewer RFP+ FcγRIIB-knockout T cells. We further isolated T cells expressing a membrane-anchored, tumor-targeted IL-12 based on the receptor's affinity to vimentin to confirm the versatility of our technique. This protocol allows researchers to isolate receptor-expressing cells in about 4 hours for further downstream processing.
已经使用等温滴定量热法和表面等离子体共振在蛋白质水平上,以及使用与相互作用相关的下游基因诱导/抑制在细胞水平上分析了受体-配体结合。然而,目前没有一种技术可以通过可视化直接表征这种相互作用。此外,所有可用的检测方法都需要大量的细胞;没有能够在单细胞水平上分析受体-配体相互作用的检测方法是公开可用的。在这里,我们描述了一种新的基于微流控芯片的技术,用于在单细胞水平上分析和可视化这些相互作用。首先,将蛋白质固定在载玻片上,然后使用低流速泵分离表达与固定配体结合的受体的细胞。具体来说,我们通过将生物素缀合的 FGL2 固定在亲和素涂层的载玻片芯片上,并使 GFP 标记的野生型 T 细胞和 RFP 标记的 FcγRIIB 敲除 T 细胞混合物通过芯片,证明了该技术的有效性。通过自动扫描和计数,我们发现了大量具有结合活性的 GFP+T 细胞,但具有 RFP+FcγRIIB 敲除 T 细胞的数量明显较少。我们进一步分离了基于受体对波形蛋白的亲和力表达膜锚定、肿瘤靶向 IL-12 的 T 细胞,以确认我们技术的多功能性。该方案允许研究人员在大约 4 小时内分离表达受体的细胞,以进行进一步的下游处理。