ArticleProtein science : a publication of the Protein Society2009
The crystal structures of macrophage migration inhibitory factor from Plasmodium falciparum and Plasmodium berghei.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
- Crystal structure of Plasmodium vivax macrophage migration inhibitory factor.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Advances in mRNA vaccines.International review of cell and molecular biology · 2022Review
- Macrophage migration inhibitory factor of Syrian golden hamster shares structural and functional similarity with human counterpart and promotes pancreatic cancer.Scientific reports · 2019Article
- Neutralization of the Plasmodium-encoded MIF ortholog confers protective immunity against malaria infection.Nature communications · 2018Article
- Interaction between parasite-encoded JAB1/CSN5 and macrophage migration inhibitory factor proteins attenuates its proinflammatory function.Scientific reports · 2018Article
- Structural characterization of As-MIF and hJAB1 during the inhibition of cell-cycle regulation.BMB reports · 2017Article
- The non-mammalian MIF superfamily.Immunobiology · 2017Review
- Susceptibility to Plasmodium yoelii preerythrocytic infection in BALB/c substrains is determined at the point of hepatocyte invasion.Infection and immunity · 2015Article
- Crystallographic and receptor binding characterization of Plasmodium falciparum macrophage migration inhibitory factor complexed to two potent inhibitors.Journal of medicinal chemistry · 2014Article
- Diversification of MIF immune regulators in aphids: link with agonistic and antagonistic interactions.BMC genomics · 2014Article
- The macrophage migration inhibitory factor homolog of Entamoeba histolytica binds to and immunomodulates host macrophages.Infection and immunity · 2014Article
- Crystal structure of a macrophage migration inhibitory factor from Giardia lamblia.Journal of structural and functional genomics · 2013Article
- Virtual screening and optimization yield low-nanomolar inhibitors of the tautomerase activity of Plasmodium falciparum macrophage migration inhibitory factor.Journal of medicinal chemistry · 2012Article
- A Plasmodium-encoded cytokine suppresses T-cell immunity during malaria.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Plasmodium yoelii macrophage migration inhibitory factor is necessary for efficient liver-stage development.Infection and immunity · 2012Article
- Macrophage migration inhibitory factor in protozoan infections.Journal of parasitology research · 2012Article
- Generation, analysis and functional annotation of expressed sequence tags from the ectoparasitic mite Psoroptes ovis.Parasites & vectors · 2011Article
- Elevated levels of the Plasmodium yoelii homologue of macrophage migration inhibitory factor attenuate blood-stage malaria.Infection and immunity · 2010Article
- A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body.Acta crystallographica. Section D, Biological crystallography · 2010Article
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8 authors.
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Abstract
Malaria, caused by Plasmodium falciparum and related parasites, is responsible for millions of deaths each year, mainly from complications arising from the blood stages of its life cycle. Macrophage migration inhibitory factor (MIF), a protein expressed by the parasite during these stages, has been characterized in mammals as a cytokine involved in a broad spectrum of immune responses. It also possesses two catalytic activities, a tautomerase and an oxidoreductase, though the physiological significance of neither reaction is known. Here, we have determined the crystal structure of MIF from two malaria parasites, Plasmodium falciparum and Plasmodium berghei at 2.2 A and 1.8 A, respectively. The structures have an alpha/beta fold and each reveals a trimer, in agreement with the results of analytical ultracentrifugation. We observed open and closed active sites, these being distinguished by movements of proline-1, the catalytic base in the tautomerase reaction. These states correlate with the covalent modification of cysteine 2 to form a mercaptoethanol adduct, an observation confirmed by mass spectrometry. The Plasmodium MIFs have a different pattern of conserved cysteine residues to the mammalian MIFs and the side chain of Cys58, which is implicated in the oxidoreductase activity, is buried. This observation and the evident redox reactivity of Cys2 suggest quite different oxidoreductase characteristics. Finally, we show in pull-down assays that Plasmodium MIF binds to the cell surface receptor CD74, a known mammalian MIF receptor implying that parasite MIF has the ability to interfere with, or modulate, host MIF activity through a competitive binding mechanism.
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