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overview and general information about: background; i) role of the plasmodium pbm in infection; ii) plasmodium pbm structure and function; iii) plasmodium pbm structure and function; iv) plasmodium pbm in invasion and host cell lipid metabolism. the plasmodium pbm is a novel fatty acid binding protein with key roles in parasite lipid metabolism and virulence. the parasite plasmodium falciparum possesses a single plasmodial membrane-bound fatty acid binding protein (pfpbm) that has a unique three-dimensional fold and a characteristic ligand-binding cavity. the crystal structure of pfpbm elucidates a detailed molecular-structure portrait, which in turn contributes to a better understanding of this protein s role in parasite-host interactions.. de montigny s, lêpour jm, tamagnan-léger c, ferrari ea, lamblin m, calados a, et al. «ligand binding properties of the fatty acid binding protein of plasmodium falciparum.» plos one. 2015;10(10):e0140373. hey all/ jérôme vissers. 19/ june/ 2020 converter de cfg no ar 15 para mais eficiente. . deb. michelle mello, phd. we are proposing to characterize the function of the parasite plasmodium falciparum-encoded fatty acid binding protein (pfpbm) as a key molecule in lipid metabolism and virulence.the first deoxycytidylate deaminase domain in the plasmodium falciparum genome is highly conserved and has been designated as the pyruvate kinase ‘ (pk) domain. computer-assisted structure determination revealed that the pk domain adopts a novel globular fold and contains distinct structural elements. the globular structure of the pk domain and its shape and sequence similarity with the fatty acid binding domain of the p. falciparum fatty acid binding protein (pffabp) suggested that pfpbm is similar to pffabp in structure and function. therefore, we generated the recombinant plasmodium falciparum fatty acid binding protein (rpffabp) as a positive control and expressed and purified pfpbm. using affinity chromatography, we characterized their fatty acid binding properties. we propose to further investigate their role in host-parasite interactions by generating conditional gene knockout parasites. lipids and their metabolites play crucial roles during parasite development in erythrocytes. the parasite-encoded fatty acid binding protein (pffabp) binds fatty acids and exhibits a preference for arachidonic acid, indicating that it might be involved in lipid metabolism in p. falciparum. here we describe a novel parasite fatty acid binding protein, pffabp, and report that its amino acid sequence is conserved in different strains of p. the expression pattern of the parasite fatty acid binding protein, pffabp is similar to the mammalian fatty acid binding proteins in erythrocytes and the pericellular environment of the parasite. it binds fatty acids with high affinity and appears to function in a similar manner as mammalian fatty acid binding proteins. we propose to investigate the role of this protein in lipid metabolism and parasite-host interactions.. 5ec8ef588b

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