INVESTIGATING NEUTRALIZING ANTIBODY INDUCED CONFORMATIONAL CHANGES AND MATURATIO

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 已知结构的对照蛋白和几种gp 140三聚体形式的先前SAXS结果表明，SAXS是我们掌握的一种易于处理的分析方法。所有样品都可以在短时间内制备，用于SAXS数据收集，目前正在进行常规生产，以支持其他研究。通过SEC同时进行静态/动态光散射以及多种形式的定量/定性Ab结合试验监测蛋白质单分散性。 我们期望获得不同gp 140-NAb复合物的整体形状和大小信息，如果可能的话，生成包膜尖峰的功能形式的模型，并通过冷冻电镜结构的Env尖峰和晶体结构的gp 120和gp 41进行验证。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Prior SAXS results with control proteins of known structure and several gp140 trimer forms show that SAXS is a tractable method of analysis in our hands. All samples can be prepared on short notice for SAXS data collection and are currently in routine production to support other studies. Protein monodispersity is monitored by SEC with simultaneous static/dynamic light scattering as well as quantitative/qualitative Ab binding assays in a variety of formats. We expect to obtain overall shape and size information of different gp140-NAb complexes, generate models for the functional form of envelope spike if possible, and verify by cryo-EM structures of Env spikes and crystal structures of gp120 and gp41.