Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus
- Autores
- Rey Burusco, M. F.; Ibáñez Shimabukuro, Marina; Gabrielsen, M.; Franchini, Gisela Raquel; Roe, A. J.; Griffiths, K.; Zhan, B.; Cooper, A.; Kennedy, M. W.; Córsico, Betina; Smith, B. O.
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual a-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 byNMR(nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an a-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligandbinding cavity and an additional C-terminal a-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.
Instituto de Investigaciones Bioquímicas de La Plata - Materia
-
Ciencias Médicas
Fatty acid-binding protein
Necator americanus
Nematode
Nuclear magnetic resonance (NMR)
Parasite
Protein structure
Retinol-binding protein
X-ray - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/3.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/86299
Ver los metadatos del registro completo
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Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanusRey Burusco, M. F.Ibáñez Shimabukuro, MarinaGabrielsen, M.Franchini, Gisela RaquelRoe, A. J.Griffiths, K.Zhan, B.Cooper, A.Kennedy, M. W.Córsico, BetinaSmith, B. O.Ciencias MédicasFatty acid-binding proteinNecator americanusNematodeNuclear magnetic resonance (NMR)ParasiteProtein structureRetinol-binding proteinX-rayFatty acid and retinol-binding proteins (FARs) comprise a family of unusual a-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 byNMR(nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an a-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligandbinding cavity and an additional C-terminal a-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.Instituto de Investigaciones Bioquímicas de La Plata2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf403-414http://sedici.unlp.edu.ar/handle/10915/86299enginfo:eu-repo/semantics/altIdentifier/issn/0264-6021info:eu-repo/semantics/altIdentifier/doi/10.1042/BJ20150068info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/3.0/Creative Commons Attribution 3.0 Unported (CC BY 3.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:54Zoai:sedici.unlp.edu.ar:10915/86299Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:54.472SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
title |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
spellingShingle |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus Rey Burusco, M. F. Ciencias Médicas Fatty acid-binding protein Necator americanus Nematode Nuclear magnetic resonance (NMR) Parasite Protein structure Retinol-binding protein X-ray |
title_short |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
title_full |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
title_fullStr |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
title_full_unstemmed |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
title_sort |
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus |
dc.creator.none.fl_str_mv |
Rey Burusco, M. F. Ibáñez Shimabukuro, Marina Gabrielsen, M. Franchini, Gisela Raquel Roe, A. J. Griffiths, K. Zhan, B. Cooper, A. Kennedy, M. W. Córsico, Betina Smith, B. O. |
author |
Rey Burusco, M. F. |
author_facet |
Rey Burusco, M. F. Ibáñez Shimabukuro, Marina Gabrielsen, M. Franchini, Gisela Raquel Roe, A. J. Griffiths, K. Zhan, B. Cooper, A. Kennedy, M. W. Córsico, Betina Smith, B. O. |
author_role |
author |
author2 |
Ibáñez Shimabukuro, Marina Gabrielsen, M. Franchini, Gisela Raquel Roe, A. J. Griffiths, K. Zhan, B. Cooper, A. Kennedy, M. W. Córsico, Betina Smith, B. O. |
author2_role |
author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Ciencias Médicas Fatty acid-binding protein Necator americanus Nematode Nuclear magnetic resonance (NMR) Parasite Protein structure Retinol-binding protein X-ray |
topic |
Ciencias Médicas Fatty acid-binding protein Necator americanus Nematode Nuclear magnetic resonance (NMR) Parasite Protein structure Retinol-binding protein X-ray |
dc.description.none.fl_txt_mv |
Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual a-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 byNMR(nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an a-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligandbinding cavity and an additional C-terminal a-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. Instituto de Investigaciones Bioquímicas de La Plata |
description |
Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual a-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 byNMR(nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an a-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligandbinding cavity and an additional C-terminal a-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. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/86299 |
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eng |
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eng |
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openAccess |
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http://creativecommons.org/licenses/by/3.0/ Creative Commons Attribution 3.0 Unported (CC BY 3.0) |
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