N-LINKED GLYCOSYLATION SITE MAPPING OF HIV-1 GP120

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 博士Zhou的团队对识别HIV-1 gp 120上聚糖的VRC 05抗体的结合相互作用感兴趣。 通过混合糖基化gp 120和VRC 05 Fab制备HIV-1 gp 120-VRC 05复合物，然后用EndoH处理以除去非相互作用聚糖。 VRC 05的存在保护很少的聚糖免于EndoH消化。 这些聚糖对于VRC 05与HIV-1 gp 120的结合至关重要。 在本研究中，我们对该蛋白复合物的糖基化位点进行了研究。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Dr. Zhou's group is interested in the binding interaction of VRC05 antibody that recognizes glycans on HIV-1 gp120. The HIV-1 gp120-VRC05 complex was prepared by mixing glycosylated gp120 and VRC05 Fab, and then treated with EndoH to remove non-interacting glycans. The presence of VRC05 protected few glycans from EndoH digestion. Those glycans are critical for VRC05 binding to HIV-1 gp120. In this study, we took the part of investigating the site of glycosylation of this protein complex.