GLYCOSAMINOGLYCAN-PROTEIN INTERACTIONS IN MALARIA PARASITE INFECTION

疟疾寄生虫感染中的糖胺聚糖-蛋白质相互作用

• 批准号: 8361799
• 负责人: JAMES H. PRESTEGARD
• 金额: $ 0.18万
• 依托单位: UNIVERSITY OF GEORGIA
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-02-01 至 2012-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361799
• 关键词: Anisotropy; Binding; Cell surface; Chemicals; Chondroitin Sulfate A; Complex; Erythrocytes; Funding; Glycosaminoglycans; Grant; Human Resources; Infection; Label; Laboratories; Malaria; Methods; National Center for Research Resources; Parasites; Placenta; Plasmids; Plasmodium falciparum; Play; Pregnant Women; Principal Investigator; Proteins; Protocols documentation; Research; Research Infrastructure; Residual state; Resources; Sampling; Source; Specificity; Tertiary Protein Structure; Testing; United States National Institutes of Health; Work; cost; stem

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. The malaria parasite, Plasmodium falciparum, is believed to cause binding of infected erythrocytes to the placenta in pregnant women through interactions of certain domains of the VAR2CSA protein with cell-surface glycosaminoglycans, specifically chondroitin 4-sulfate (C4S). DBL3X domain has been predicted to play key roles in the binding of VAR2CSA to C4S. Dr Gowda's laboratory has provided plasmids and protocols for expressing the DBLX3 domain of the protein for the purpose of testing and characterizing these hypothesized interactions. Personnel at the Resource are producing 13C-labeled forms of specific C4S oligomers that can be used in assessing the specificity of interactions and will express appropriately labeled forms of the protein. The NMR methods that allow use of 13C chemical shift anisotropy offsets in aligned samples to return geometry information on the complexes stem from pre8vious Resource supported work on residual dipolar couplings (RDCs).

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 据信，疟疾寄生虫疟原虫通过VAR2CSA蛋白与细胞表面糖胺聚糖的某些结构的相互作用，在孕妇中引起感染红细胞与胎盘的结合。 预计DBL3X域在VAR2CSA与C4S的结合中起关键作用。 Gowda博士的实验室提供了表达蛋白质的DBLX3结构域的质粒和方案，目的是测试和表征这些假设的相互作用。 资源的人员正在产生13C标记的特定C4寡聚物形式，这些形式可用于评估相互作用的特异性，并将表达适当标记的蛋白质形式。 允许使用13c化学移动各向异性偏移的NMR方法在对齐样品中返回有关络合物的几何信息，源于8. vious Predvious资源支持的残留偶性偶联（RDC）的工作。