PHOSPHATIDYLINOSITOL SPECIFIC PHOSPHOLIPASE C FROM GIARDIA LAMBLIA

来自贾第鞭毛虫的磷脂酰肌醇特异性磷脂酶 C

• 批准号: 6271479
• 负责人: SIDDARTHDA DAS
• 金额: $ 9.07万
• 依托单位: UNIVERSITY OF TEXAS EL PASO
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-06-01 至 1999-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6271479
• 关键词: Giardia; antibody; chemical binding; electrolyte balance; enzyme activity; gel electrophoresis; genetic library; giardiasis; high performance liquid chromatography; host organism interaction; human tissue; ion exchange chromatography; laboratory rabbit; molecular cloning; nucleic acid sequence; pathologic process; phosphatidylinositols; phospholipase C; protein structure function; protozoal antigen; structural genes; surface antigens; thin layer chromatography; western blottings

Giardia lamblia is a parasite protozoa and a primitive eukaryote, is responsible for water born enteric infection throughout tropical and temperate zones. The mechanism by which this organism causes diarrhea is currently unknown. It has been postulated that surface antigens of this parasite play an important role during the host-parasite interactions. Recently, we have found an invariant antigen on the surface of Giardia, which is stable and present in different isolates (GP49). GP49 is linked to the outer surface of the plasma membrane with a novel Glycophospholipid anchor and secreted in the culture medium. It has been documented previously that the enzyme PI-PLC is responsible for the cleavage of the Glycophospholipid (GPI) anchored surface antigens of the parasitic protozoa and other eukaryotes. Although the biological function of GP49 is not known, recently we found that intact and soluble GP49 altered the electrolyte fluxes which regulate fluid secretion in the cultured human intestinal epithelial cell line, T84. Therefore it can be postulated that the enzyme, phosphatidylinositol specific phospholipase-C(PI-PLC) of Giardia is responsible for the cleavage and the secretion of GP49. Here we propose to study PI-PLC from G. Lamblia using biochemical and molecular methodologies for the first time.

贾第鞭毛虫是一种寄生原生动物，也是一种原始真核生物， 造成整个热带地区的水源性肠道感染 温带地区。 该微生物引起腹泻的机制是 目前未知。 据推测，该表面抗原 寄生虫在宿主与寄生虫的相互作用中发挥着重要作用。 最近，我们在贾第鞭毛虫表面发现了一种不变的抗原， 它是稳定的并且存在于不同的分离株中（GP49）。 GP49已链接 用新型糖磷脂附着在质膜的外表面 锚定并分泌于培养基中。 已记录在案 以前认为酶 PI-PLC 负责裂解 寄生原生动物的糖磷脂 (GPI) 锚定表面抗原 和其他真核生物。 虽然GP49的生物学功能尚不明确。 众所周知，最近我们发现完整且可溶的 GP49 改变了 调节培养人体液体分泌的电解质通量 肠上皮细胞系，T84。 因此可以假设 酶，磷脂酰肌醇特异性磷脂酶-C(PI-PLC) 贾第鞭毛虫负责 GP49 的裂解和分泌。 在这里我们 提议利用生化和分子研究 G. Lamblia 的 PI-PLC 方法论首次。