2os5: Difference between revisions

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==Overview==

Hookworms, parasitic nematodes that infect nearly one billion people, worldwide, are a major cause of anemia and malnutrition. We hypothesize, that hookworms actively manipulate the host immune response through the, production of specific molecules designed to facilitate infection by, larval stages and adult worm survival within the intestine. A full-length, cDNA encoding a secreted orthologue of the human cytokine, Macrophage, Migration Inhibitory Factor (MIF) has been cloned from the hookworm, Ancylostoma ceylanicum. Elucidation of the three-dimensional crystal, structure of recombinant AceMIF (rAceMIF) revealed an overall structural, homology with significant differences in the tautomerase sites of the, human and hookworm proteins. The relative bioactivities of human and, hookworm MIF proteins were compared using in vitro assays of tautomerase, activity, macrophage migration, and binding to MIF receptor CD74. The, activity of rAceMIF was not inhibited by the ligand ISO-1, which was, previously determined to be an inhibitor of the catalytic site of human, MIF. These data define unique immunological, structural, and functional, characteristics of AceMIF, thereby establishing the potential for, selectively inhibiting the hookworm cytokine as a means of reducing, parasite survival and disease pathogenesis.

Hookworms, parasitic nematodes that infect nearly one billion people worldwide, are a major cause of anemia and malnutrition. We hypothesize that hookworms actively manipulate the host immune response through the production of specific molecules designed to facilitate infection by larval stages and adult worm survival within the intestine. A full-length cDNA encoding a secreted orthologue of the human cytokine, Macrophage Migration Inhibitory Factor (MIF) has been cloned from the hookworm Ancylostoma ceylanicum. Elucidation of the three-dimensional crystal structure of recombinant AceMIF (rAceMIF) revealed an overall structural homology with significant differences in the tautomerase sites of the human and hookworm proteins. The relative bioactivities of human and hookworm MIF proteins were compared using in vitro assays of tautomerase activity, macrophage migration, and binding to MIF receptor CD74. The activity of rAceMIF was not inhibited by the ligand ISO-1, which was previously determined to be an inhibitor of the catalytic site of human MIF. These data define unique immunological, structural, and functional characteristics of AceMIF, thereby establishing the potential for selectively inhibiting the hookworm cytokine as a means of reducing parasite survival and disease pathogenesis.

==About this Structure==

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[[Category: nematode]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Hookworms, parasitic nematodes that infect nearly one billion people, worldwide, are a major cause of anemia and malnutrition. We hypothesize, that hookworms actively manipulate the host immune response through the, production of specific molecules designed to facilitate infection by, larval stages and adult worm survival within the intestine. A full-length, cDNA encoding a secreted orthologue of the human cytokine, Macrophage, Migration Inhibitory Factor (MIF) has been cloned from the hookworm, Ancylostoma ceylanicum. Elucidation of the three-dimensional crystal, structure of recombinant AceMIF (rAceMIF) revealed an overall structural, homology with significant differences in the tautomerase sites of the, human and hookworm proteins. The relative bioactivities of human and, hookworm MIF proteins were compared using in vitro assays of tautomerase, activity, macrophage migration, and binding to MIF receptor CD74. The, activity of rAceMIF was not inhibited by the ligand ISO-1, which was, previously determined to be an inhibitor of the catalytic site of human, MIF. These data define unique immunological, structural, and functional, characteristics of AceMIF, thereby establishing the potential for, selectively inhibiting the hookworm cytokine as a means of reducing, parasite survival and disease pathogenesis.
+Hookworms, parasitic nematodes that infect nearly one billion people worldwide, are a major cause of anemia and malnutrition. We hypothesize that hookworms actively manipulate the host immune response through the production of specific molecules designed to facilitate infection by larval stages and adult worm survival within the intestine. A full-length cDNA encoding a secreted orthologue of the human cytokine, Macrophage Migration Inhibitory Factor (MIF) has been cloned from the hookworm Ancylostoma ceylanicum. Elucidation of the three-dimensional crystal structure of recombinant AceMIF (rAceMIF) revealed an overall structural homology with significant differences in the tautomerase sites of the human and hookworm proteins. The relative bioactivities of human and hookworm MIF proteins were compared using in vitro assays of tautomerase activity, macrophage migration, and binding to MIF receptor CD74. The activity of rAceMIF was not inhibited by the ligand ISO-1, which was previously determined to be an inhibitor of the catalytic site of human MIF. These data define unique immunological, structural, and functional characteristics of AceMIF, thereby establishing the potential for selectively inhibiting the hookworm cytokine as a means of reducing parasite survival and disease pathogenesis.
 ==About this Structure==
@@ Line 21: / Line 21: @@
 [[Category: nematode]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:13:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:54 2008''