A Leishmania Ortholog of Macrophage Migration Inhibitory Factor Modulates Host Macrophage Responses
Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage migration inhibitory factor (MIF), which is produced by the obligate intracellular parasite, Leishmania major. The Leishmania MIF protein, Lm1740MIF,...
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| Published in | The Journal of immunology (1950) Vol. 180; no. 12; pp. 8250 - 8261 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Am Assoc Immnol
15.06.2008
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage migration inhibitory factor (MIF), which is produced by the obligate intracellular parasite, Leishmania major. The Leishmania MIF protein, Lm1740MIF, shows significant structural homology with human MIF as revealed by a high-resolution x-ray crystal structure (1.03 A). Differences between the two proteins in the N-terminal tautomerization site are evident, and we provide evidence for the selective, species-specific inhibition of MIF by small-molecule antagonists that target this site. Lm1740MIF shows significant binding interaction with the MIF receptor, CD74 (K(d) = 2.9 x 10(-8) M). Like its mammalian counterpart, Lm1740MIF induces ERK1/2 MAP kinase activation in a CD74-dependent manner and inhibits the activation-induced apoptosis of macrophages. The ability of Lm1740MIF to inhibit apoptosis may facilitate the persistence of Leishmania within the macrophage and contribute to its evasion from immune destruction. |
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| AbstractList | Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage migration inhibitory factor (MIF), which is produced by the obligate intracellular parasite, Leishmania major. The Leishmania MIF protein, Lm1740MIF, shows significant structural homology with human MIF as revealed by a high-resolution x-ray crystal structure (1.03 A). Differences between the two proteins in the N-terminal tautomerization site are evident, and we provide evidence for the selective, species-specific inhibition of MIF by small-molecule antagonists that target this site. Lm1740MIF shows significant binding interaction with the MIF receptor, CD74 (K(d) = 2.9 x 10(-8) M). Like its mammalian counterpart, Lm1740MIF induces ERK1/2 MAP kinase activation in a CD74-dependent manner and inhibits the activation-induced apoptosis of macrophages. The ability of Lm1740MIF to inhibit apoptosis may facilitate the persistence of Leishmania within the macrophage and contribute to its evasion from immune destruction. Abstract Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage migration inhibitory factor (MIF), which is produced by the obligate intracellular parasite, Leishmania major. The Leishmania MIF protein, Lm1740MIF, shows significant structural homology with human MIF as revealed by a high-resolution x-ray crystal structure (1.03 Å). Differences between the two proteins in the N-terminal tautomerization site are evident, and we provide evidence for the selective, species-specific inhibition of MIF by small-molecule antagonists that target this site. Lm1740MIF shows significant binding interaction with the MIF receptor, CD74 (Kd = 2.9 × 10−8 M). Like its mammalian counterpart, Lm1740MIF induces ERK1/2 MAP kinase activation in a CD74-dependent manner and inhibits the activation-induced apoptosis of macrophages. The ability of Lm1740MIF to inhibit apoptosis may facilitate the persistence of Leishmania within the macrophage and contribute to its evasion from immune destruction. Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage migration inhibitory factor (MIF), which is produced by the obligate intracellular parasite, Leishmania major. The Leishmania MIF protein, Lm1740MIF, shows significant structural homology with human MIF as revealed by a high-resolution x-ray crystal structure (1.03 Aa). Differences between the two proteins in the N-terminal tautomerization site are evident, and we provide evidence for the selective, species-specific inhibition of MIF by small-molecule antagonists that target this site. Lm1740MIF shows significant binding interaction with the MIF receptor, CD74 (K sub(d) = 2.9 x 10 super(-8) M). Like its mammalian counterpart, Lm1740MIF induces ERK1/2 MAP kinase activation in a CD74-dependent manner and inhibits the activation-induced apoptosis of macrophages. The ability of Lm1740MIF to inhibit apoptosis may facilitate the persistence of Leishmania within the macrophage and contribute to its evasion from immune destruction. |
| Author | Walker, John Trent, John Griffith, Jason Bernhagen, Jurgen Mitchell, Robert A Lolis, Elias Cho, Yoonsang Bucala, Richard McMahon-Pratt, Diane Diaz, Yira Merk, Melanie Chen, Yibang Kamir, Daniela Kwong, Yuen-Kwan Amy McDonald, Courtney Zierow, Swen Xiong, Huabao Vermeire, Jon Cappello, Michael Leng, Lin |
| Author_xml | – sequence: 1 fullname: Kamir, Daniela – sequence: 2 fullname: Zierow, Swen – sequence: 3 fullname: Leng, Lin – sequence: 4 fullname: Cho, Yoonsang – sequence: 5 fullname: Diaz, Yira – sequence: 6 fullname: Griffith, Jason – sequence: 7 fullname: McDonald, Courtney – sequence: 8 fullname: Merk, Melanie – sequence: 9 fullname: Mitchell, Robert A – sequence: 10 fullname: Trent, John – sequence: 11 fullname: Chen, Yibang – sequence: 12 fullname: Kwong, Yuen-Kwan Amy – sequence: 13 fullname: Xiong, Huabao – sequence: 14 fullname: Vermeire, Jon – sequence: 15 fullname: Cappello, Michael – sequence: 16 fullname: McMahon-Pratt, Diane – sequence: 17 fullname: Walker, John – sequence: 18 fullname: Bernhagen, Jurgen – sequence: 19 fullname: Lolis, Elias – sequence: 20 fullname: Bucala, Richard |
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| Snippet | Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage... Abstract Parasitic organisms have evolved specialized strategies to evade immune defense mechanisms. We describe herein an ortholog of the cytokine, macrophage... |
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| SubjectTerms | Amino Acid Sequence Animals Antigens, Differentiation, B-Lymphocyte - genetics Antigens, Differentiation, B-Lymphocyte - metabolism Antigens, Differentiation, B-Lymphocyte - physiology APOPTOSIS Apoptosis Regulatory Proteins - chemistry Apoptosis Regulatory Proteins - genetics Apoptosis Regulatory Proteins - metabolism Apoptosis Regulatory Proteins - physiology Cell Line Cells, Cultured CRYSTAL STRUCTURE Crystallography, X-Ray Histocompatibility Antigens Class II - genetics Histocompatibility Antigens Class II - metabolism Histocompatibility Antigens Class II - physiology Humans Intramolecular Oxidoreductases - chemistry Intramolecular Oxidoreductases - genetics Intramolecular Oxidoreductases - metabolism Intramolecular Oxidoreductases - physiology Leishmania major Leishmania major - chemistry Leishmania major - immunology Leishmania major - metabolism Macrophage Migration-Inhibitory Factors - chemistry Macrophage Migration-Inhibitory Factors - genetics Macrophage Migration-Inhibitory Factors - metabolism Macrophage Migration-Inhibitory Factors - physiology MACROPHAGES Macrophages, Peritoneal - enzymology Macrophages, Peritoneal - immunology Macrophages, Peritoneal - parasitology MATERIALS SCIENCE Mice Mice, Inbred BALB C Mice, Inbred C3H Mice, Knockout Molecular Sequence Data national synchrotron light source PHOSPHOTRANSFERASES PROTEINS Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism Recombinant Proteins - pharmacology Structural Homology, Protein TARGETS |
| Title | A Leishmania Ortholog of Macrophage Migration Inhibitory Factor Modulates Host Macrophage Responses |
| URI | http://www.jimmunol.org/cgi/content/abstract/180/12/8250 https://www.ncbi.nlm.nih.gov/pubmed/18523291 https://search.proquest.com/docview/21045682 https://search.proquest.com/docview/71633675 https://www.osti.gov/biblio/959595 |
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