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低温电子显微镜揭示了一个单域抗体,具有独特的结合表位在纤维细胞激活蛋白α上

Zhen Xu¹, Akesh Sinha², Darpan N Pandya²

¹Protein and Crystallography Facility, University of Iowa, Iowa City, Iowa, 52242, USA.

bioRxiv : the preprint server for biology

|October 28, 2024

概括

研究人员描述了一种与纤维细胞激活蛋白α (FAP) 的新型单域抗体 (sdAb) 相互作用. 这种结构性洞察力为开发新的诊断和治疗FAP向剂提供了基础.

科学领域:

生物化学生物化学
结构生物学结构生物学
免疫学免疫学免疫学

背景情况:

纤维细胞激活蛋白α (FAP) 是一种蛋白酶,在各种病理中表达过度,特别是癌症.
准FAP为诊断和治疗提供了机会,但有效的药物仍然难以捉摸.
了解FAP相互作用对于开发新的生物医学工具至关重要.

研究的目的:

在结构上描述一种新型单域抗体 (sdAb),I3和FAP之间的相互作用.
为FAP-sdAb相互作用提供详细的结构基础.
为了指导改进的FAP准剂的合理设计.

主要方法:

使用冷电子显微镜 (cryo-EM) 来确定I3-FAP复合物的结构.
高分辨率 (2.7 Å) 的重建揭示了sdAb与FAP二分体的独特结合模式.
进行了sdAb的互补性确定区域3 (CDR3) 的位点定向突变发生.

主要成果:

该研究阐明了与FAP结合的sdAb的第一个报告的结构.
观察到两个不同的群体:一个与一个I3分子结合,另一个与两个I3分子结合FAP二分体.
sdAbs与一个独特的表位结合,与FAP活性部位分开.
在CDR3循环中的理性突变显示出增强亲和力和选择性的潜力.

结论:

这项工作提供了sdAb-FAP复合体的第一个结构描述.
已确定的结合部位和潜在的亲和力增强为针对FAP的诊断和治疗提供了一个有希望的途径.
这些发现为开发下一代FAP准剂奠定了基础.

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