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C100007200v1
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Papers In Press, published online ahead of print January 10, 2001
J. Biol. Chem, 10.1074/jbc.C100007200
Submitted on January 6, 2001
Revised on January 10, 2001
Accepted on January 10, 2001

Plasmodium falciparum glycosylphosphatidylinositol-induced TNF-alpha secretion by macrophages is mediated without membrane insertion or endocytosis

Matam Vijaykumar, Ramachandra S. Naik, and D. Channe Gowda

Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, DC 20007

Corresponding Author: gowda{at}bc.georgetown.edu

The glycosylphosphatidylinositols (GPIs) of Plasmodium falciparum are believed to contribute to malaria pathogenesis by inducing the secretion of proinflammatory cytokines by macrophages. Previous studies have shown that P. falciparum GPIs elicit toxic immune responses by PTK- and PKC-mediated cell signaling pathways, which are activated by the carbohydrate and acyl moieties of the intact GPIs, respectively. In this study, we show that induction of TNF-alpha by P. falciparum GPIs in macrophages is mediated by the recognition of the distal fourth mannose residue. This event is critical but not sufficient for the productive cell signaling; interaction by the acylglycerol moiety of GPIs is also required. These novel interactions are coupled to previously demonstrated PTK and PKC pathways since the specific inhibitors of these kinases effectively blocked the GPI-induced TNF-alpha production. Surprisingly, sn-2 lyso-GPIs were also able to elicit TNF-alpha secretion. Contrary to the prevailing notion, GPIs are neither inserted to the plasma membranes nor endocytosized. Thus, this study defines the GPI structural requirements and reveals a novel mechanism for the outside-in activation of cell signaling by P. falciparum GPIs in inducing proinflammatory responses


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