ArticleThe Journal of biological chemistry2007
Structural and functional characterization of a secreted hookworm Macrophage Migration Inhibitory Factor (MIF) that interacts with the human MIF receptor CD74.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
51 citing papers in PubMed, 100 citations in OpenAlex.
- Helminth proteins recapitulate key structural motifs of MIF to facilitate immunomodulation of host receptors.iScience · 2026Article
- Hookworm genes encoding intestinal excreted-secreted proteins are transcriptionally upregulated in response to the host's immune system.PLoS neglected tropical diseases · 2026Article
- Crystal structure of N-terminally hexahistidine-tagged Onchocerca volvulus macrophage migration inhibitory factor-1.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Unveiling the unexplored novel signatures for osteoporosis via a detailed bioinformatics and molecular experiments based approach.American journal of translational research · 2024Article
- Hookworms dynamically respond to loss of Type 2 immune pressure.PLoS pathogens · 2023Article
- Hookworm infections: Reappraising the evidence for a role of neutrophils in light of NETosis.Parasite immunology · 2022Review
- Nematode Orthologs of Macrophage Migration Inhibitory Factor (MIF) as Modulators of the Host Immune Response and Potential Therapeutic Targets.Pathogens (Basel, Switzerland) · 2022Review
- Parasitomimetics: Can We Utilize Parasite-Derived Immunomodulatory Molecules for Interventions to Immunological Disorders?Frontiers in immunology · 2022Review
- Functional Characterization of the Wheat Macrophage Migration Inhibitory Factor TaMIF1 in Wheat-Stripe Rust (Biology · 2021Article
- A Complex Proteomic Response of the Parasitic Nematode Anisakis simplex s.s. to Escherichia coliLipopolysaccharide.Molecular & cellular proteomics : MCP · 2021Article
- Effectors of Root-Knot Nematodes: An Arsenal for Successful Parasitism.Frontiers in plant science · 2021Review
- The Functional Parasitic Worm Secretome: Mapping the Place ofPathogens (Basel, Switzerland) · 2020Review
- Role of Host and Parasite MIF Cytokines duringTropical medicine and infectious disease · 2020Review
- Twenty-five-year research progress in hookworm excretory/secretory products.Parasites & vectors · 2020Review
- Cross-kingdom mimicry of the receptor signaling and leukocyte recruitment activity of a human cytokine by its plant orthologs.The Journal of biological chemistry · 2020Article
- A selective small-molecule inhibitor of macrophage migration inhibitory factor-2 (MIF-2), a MIF cytokine superfamily member, inhibits MIF-2 biological activity.The Journal of biological chemistry · 2019Article
- A MIF-like effector suppresses plant immunity and facilitates nematode parasitism by interacting with plant annexins.Journal of experimental botany · 2019Article
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- Neutralization of the Plasmodium-encoded MIF ortholog confers protective immunity against malaria infection.Nature communications · 2018Article
- Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.