N-LINKED GLYCOSYLATION SITE MAPPING OF HIV-1 GP120

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 周博士的团队对识别HIV-1 gp120上的多糖的VRC05抗体的结合作用感兴趣。将糖基化的gp120和VRC05 Fab混合制成HIV-1gp120-VRC05复合体，然后用EndoH处理以去除非相互作用的糖链。VRC05的存在保护了很少的多糖不被内源性消化。这些多糖是VRC05与HIV-1 gp120结合的关键。在本研究中，我们对该蛋白质复合体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.