Show simple item record

dc.contributor.authorKennedy, Malcolm W.en
dc.contributor.authorGarside, Lisa H.en
dc.contributor.authorGoodrick, Lucy E.en
dc.contributor.authorMcDermott, Lindsay C.en
dc.contributor.authorBrass, Andrewen
dc.contributor.authorPrice, Nicholas C.en
dc.contributor.authorKelly, Sharon M.en
dc.contributor.authorCooper, Alanen
dc.contributor.authorBradley, Jannette E.en
dc.date.accessioned2018-04-27T10:42:15Z
dc.date.available2018-04-27T10:42:15Z
dc.date.issued1997-11-21
dc.identifier.citationKennedy MW, Garside LH, Goodrick LE, McDermott L, Brass A, Price NC, Kelly SM, Cooper A, Bradley JE (1997) 'The Ov20 protein of the parasitic nematode Onchocerca volvulus - A structurally novel class of small helix-rich retinol-binding proteins', Journal of Biological Chemistry, 272 (47), pp.29442-29448.en
dc.identifier.issn0021-9258
dc.identifier.pmid9368002
dc.identifier.doi10.1074/jbc.272.47.29442
dc.identifier.urihttp://hdl.handle.net/10547/622691
dc.description.abstractOv20 is a major antigen of the parasitic nematode Onchocerca volvulus, the causative agent of river blindness in humans, and the protein is secreted into the tissue occupied by the parasite. DNA encoding Ov20 was isolated, and the protein was expressed in Escherichia coli. Fluorescence-based ligand binding assays show that the protein contains a high affinity binding site for retinol, fluorescent fatty acids (11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid, dansyl-DL-alpha-aminocaprylic acid, and parinaric acid) and, by competition, oleic and arachidonic acids, but not cholesterol. The fluorescence emission of dansylated fatty acids is significantly blue-shifted upon binding in comparison to similarly sized beta-sheet-rich mammalian retinol- and fatty acid-binding proteins. Secondary structure prediction algorithms indicate that a alpha-helix predominates in Ov20, possibly in a coiled coil motif, with no evidence of beta structures, and this was confirmed by circular dichroism. The protein is highly stable in solution, requiring temperatures in excess of 90 degrees C or high denaturant concentrations for unfolding. Ov20 therefore represents a novel class of small retinol-binding protein, which appears to be confined to nematodes. The retinol binding activity of Ov20 could possibly contribute to the eye defects associated with onchocerciasis and, because there is no counterpart in mammals, represents a strategic target for chemotherapy.
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relation.urlhttp://www.jbc.org/content/272/47/29442.longen
dc.rightsGreen - can archive pre-print and post-print or publisher's version/PDF
dc.subjectn-3 polyunsaturated fatty acidsen
dc.subjectC700 Molecular Biology, Biophysics and Biochemistryen
dc.titleThe Ov20 protein of the parasitic nematode Onchocerca volvulus - A structurally novel class of small helix-rich retinol-binding proteinsen
dc.typeArticleen
dc.contributor.departmentUniversity of Glasgowen
dc.contributor.departmentSalford Universityen
dc.contributor.departmentUniversity of Manchesteren
dc.contributor.departmentUniversity of Stirlingen
dc.identifier.journalJournal of Biological Chemistryen
dc.date.updated2018-04-27T09:56:49Z
html.description.abstractOv20 is a major antigen of the parasitic nematode Onchocerca volvulus, the causative agent of river blindness in humans, and the protein is secreted into the tissue occupied by the parasite. DNA encoding Ov20 was isolated, and the protein was expressed in Escherichia coli. Fluorescence-based ligand binding assays show that the protein contains a high affinity binding site for retinol, fluorescent fatty acids (11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid, dansyl-DL-alpha-aminocaprylic acid, and parinaric acid) and, by competition, oleic and arachidonic acids, but not cholesterol. The fluorescence emission of dansylated fatty acids is significantly blue-shifted upon binding in comparison to similarly sized beta-sheet-rich mammalian retinol- and fatty acid-binding proteins. Secondary structure prediction algorithms indicate that a alpha-helix predominates in Ov20, possibly in a coiled coil motif, with no evidence of beta structures, and this was confirmed by circular dichroism. The protein is highly stable in solution, requiring temperatures in excess of 90 degrees C or high denaturant concentrations for unfolding. Ov20 therefore represents a novel class of small retinol-binding protein, which appears to be confined to nematodes. The retinol binding activity of Ov20 could possibly contribute to the eye defects associated with onchocerciasis and, because there is no counterpart in mammals, represents a strategic target for chemotherapy.


This item appears in the following Collection(s)

Show simple item record