ArticleThe Biochemical journal2015
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- A molecular and cellular understanding of PFDA-exposure-associated outcomes on biological assemblies.Environmental research · 2026Article
- Structure-guided screening of FAR-1 antagonists with multi-stage anthelmintic activity.Antimicrobial agents and chemotherapy · 2026Article
- A secreted fatty acid- and retinol- binding protein frombioRxiv : the preprint server for biology · 2025Article
- Nb-FAR-1: A key developmental protein affects lipid droplet accumulation and cuticle formation in Nippostrongylus brasiliensis.PLoS neglected tropical diseases · 2025Article
- Fatty acid- and retinol-binding protein 6 does not control worm fatty acid content in Caenorhabditis elegans but might play a role in Haemonchus contortus parasitism.Parasites & vectors · 2023Article
- Novel antiinflammatory biologics shaped by parasite-host coevolution.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Function of lipid binding proteins of parasitic helminths: still a long road.Parasitology research · 2022Review
- The FAR protein family of parasitic nematodes.PLoS pathogens · 2022Review
- Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways.PLoS pathogens · 2021Article
- Genus-level evolutionary relationships of FAR proteins reflect the diversity of lifestyles of free-living and parasitic nematodes.BMC biology · 2021Article
- Article
- Twenty-five-year research progress in hookworm excretory/secretory products.Parasites & vectors · 2020Review
- Identification and Characterization of a Fatty Acid- and Retinoid-Binding Protein Gene (International journal of molecular sciences · 2019Article
- Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode.Bioscience reports · 2019Article
- Comparative genomics of the major parasitic worms.Nature genetics · 2019Article
- Ligand binding properties of two Brugia malayi fatty acid and retinol (FAR) binding proteins and their vaccine efficacies against challenge infection in gerbils.PLoS neglected tropical diseases · 2018Article
- Conformational changes, from β-strand to α-helix, of the fatty acid-binding protein ReP1-NCXSQ in anionic lipid membranes: dependence with the vesicle curvature.European biophysics journal : EBJ · 2018Article
- Crystal Structure of Borrelia turicatae protein, BTA121, a differentially regulated gene in the tick-mammalian transmission cycle of relapsing fever spirochetes.Scientific reports · 2017Article
- Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, Dioctophyme renale.Parasites & vectors · 2017Article
- Transcriptome profiling of Cucumis metuliferus infected by Meloidogyne incognita provides new insights into putative defense regulatory network in Cucurbitaceae.Scientific reports · 2017Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual α-helix rich lipid-binding proteins found exclusively in nematodes. They are secreted into host tissues by parasites of plants, animals and humans. The structure of a FAR protein from the free-living nematode Caenorhabditis elegans is available, but this protein [C. elegans FAR-7 (Ce-FAR-7)] is from a subfamily of FARs that does not appear to be important at the host/parasite interface. We have therefore examined [Necator americanus FAR-1 (Na-FAR-1)] from the blood-feeding intestinal parasite of humans, N. americanus. The 3D structure of Na-FAR-1 in its ligand-free and ligand-bound forms, determined by NMR (nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an α-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligand-binding cavity and an additional C-terminal α-helix. Titration of apo-Na-FAR-1 with oleic acid, analysed by NMR chemical shift perturbation, reveals that at least four distinct protein-ligand complexes can be formed. Na-FAR-1 and possibly other FARs may have a wider repertoire for hydrophobic ligand binding, as confirmed in the present study by our finding that a range of neutral and polar lipids co-purify with the bacterially expressed recombinant protein. Finally, we show by immunohistochemistry that Na-FAR-1 is present in adult worms with a tissue distribution indicative of possible roles in nutrient acquisition by the parasite and in reproduction in the male.
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