{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T03:38:58Z","timestamp":1776310738920,"version":"3.50.1"},"reference-count":70,"publisher":"Portland Press Ltd.","issue":"3","license":[{"start":{"date-parts":[[2019,7,25]],"date-time":"2019-07-25T00:00:00Z","timestamp":1564012800000},"content-version":"vor","delay-in-days":1378,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2015,11,1]]},"abstract":"<jats:p>Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual \u03b1-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 \u03b1-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 \u03b1-helix. Titration of apo-Na-FAR-1 with oleic acid, analysed by NMR chemical shift perturbation, reveals that at least four distinct protein\u2013ligand 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.<\/jats:p>","DOI":"10.1042\/bj20150068","type":"journal-article","created":{"date-parts":[[2015,8,29]],"date-time":"2015-08-29T02:24:39Z","timestamp":1440815079000},"page":"403-414","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":34,"title":["Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from <i>Necator americanus<\/i>"],"prefix":"10.1042","volume":"471","author":[{"given":"M.\u00a0Florencia","family":"Rey-Burusco","sequence":"first","affiliation":[{"name":"Instituto de Investigaciones Bioqu\u00edmicas de La Plata, CONICET-UNLP, Facultad de Ciencias M\u00e9dicas, calles 60 y 120, 1900-La Plata, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marina","family":"Ib\u00e1\u00f1ez-Shimabukuro","sequence":"additional","affiliation":[{"name":"Instituto de Investigaciones Bioqu\u00edmicas de La Plata, CONICET-UNLP, Facultad de Ciencias M\u00e9dicas, calles 60 y 120, 1900-La Plata, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mads","family":"Gabrielsen","sequence":"additional","affiliation":[{"name":"Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8QQ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gisela\u00a0R.","family":"Franchini","sequence":"additional","affiliation":[{"name":"Instituto de Investigaciones Bioqu\u00edmicas de La Plata, CONICET-UNLP, Facultad de Ciencias M\u00e9dicas, calles 60 y 120, 1900-La Plata, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew\u00a0J.","family":"Roe","sequence":"additional","affiliation":[{"name":"Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8QQ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kate","family":"Griffiths","sequence":"additional","affiliation":[{"name":"Institute of Biodiversity, Animal Health and Comparative Medicine, University of Glasgow, Glasgow G12 8QQ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bin","family":"Zhan","sequence":"additional","affiliation":[{"name":"National School of Tropical Medicine and Department of Pediatrics, Section of Tropical Medicine, Baylor College of Medicine, Houston, TX 20031, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alan","family":"Cooper","sequence":"additional","affiliation":[{"name":"School of Chemistry, University of Glasgow, Glasgow G12 8QQ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Malcolm\u00a0W.","family":"Kennedy","sequence":"additional","affiliation":[{"name":"Institute of Biodiversity, Animal Health and Comparative Medicine, University of Glasgow, Glasgow G12 8QQ, U.K."},{"name":"Institute of Molecular, Cell & Systems Biology, University of Glasgow, Glasgow G12 8QQ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Betina","family":"C\u00f3rsico","sequence":"additional","affiliation":[{"name":"Instituto de Investigaciones Bioqu\u00edmicas de La Plata, CONICET-UNLP, Facultad de Ciencias M\u00e9dicas, calles 60 y 120, 1900-La Plata, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brian\u00a0O.","family":"Smith","sequence":"additional","affiliation":[{"name":"Institute of Molecular, Cell & Systems Biology, University of Glasgow, Glasgow G12 8QQ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2015,10,16]]},"reference":[{"key":"2021112216240460600_B1","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1146\/annurev.nutr.27.061406.093710","article-title":"The emerging functions and mechanisms of mammalian fatty acid-binding proteins","volume":"28","author":"Storch","year":"2008","journal-title":"Annu. 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