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).

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