The gp15400 polyprotein antigen of Brugia malayi binds fatty acids and retinoids

Kennedy, Malcolm W.; Allen, Judith E.; Wright, A. N.; McCruden, Alan B.; Cooper, Alan

doi:10.1016/0166-6851(95)00028-y

Cited by 48 publications

(47 citation statements)

References 27 publications

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“…Acyl coenzyme A-binding protein is known from crystal studies also to be predominately helical, but it does not bind free fatty acids, the nucleotide group of the coenzyme being required to shield the aliphatic tail from the solvent environment (41). The only other family of retinoidbinding proteins of similar size and helicity that has been reported are individual units of the polyprotein allergens of nematodes (NPAs), such as ABA-1 (26,32,35). These are predicted to be four-helix proteins with no ␤ content, but Ov20 is distinct from the NPAs in that it is not produced as a polyprotein and its primary structure has none of the characteristic features of the NPAs, such as the conserved Trp and pair of Cys residues.…”

Section: Resultsmentioning

confidence: 99%

“…The coiled-coil interactions could presumably act between the two stretches of predicted coiled coil within a single molecule of Ov20, or be involved in intramolecular interactions between other Ov20 molecules, such as in leucine zippers (33,34). The highly helical ABA-1-type of fatty acidbinding protein of nematodes, for instance, are known to form dimers (26,32,35).…”

Section: Resultsmentioning

confidence: 99%

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The Ov20 Protein of the Parasitic Nematode Onchocerca volvulus

Kennedy

Garside

Goodrick

et al. 1997

Journal of Biological Chemistry

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Ov20 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-␣-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 ␤-sheet-rich mammalian retinoland fatty acid-binding proteins. Secondary structure prediction algorithms indicate that a ␣-helix predominates in Ov20, possibly in a coiled coil motif, with no evidence of ␤ structures, and this was confirmed by circular dichroism. The protein is highly stable in solution, requiring temperatures in excess of 90°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.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

The Ov20 Protein of the Parasitic Nematode Onchocerca volvulus

Kennedy

Garside

Goodrick

et al. 1997

Journal of Biological Chemistry

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“…Further, three unigenes show homology to fatty acid-and retinoid-binding proteins of parasitic nematodes. Fatty acids are compounds that play a role in the host defense-signaling pathway (Kennedy et al 1995;Prior et al 2001). As a consequence, nematode proteins that bind such compounds could modulate the host defense to facilitate parasitism.…”

Section: Unigenes Putatively Involved In Parasitismmentioning

confidence: 99%

Exploring the transcriptome of the burrowing nematode Radopholus similis

et al. 2008

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Radopholus similis is an important nematode pest on fruit crops in the tropics. Unraveling the transcriptome of this migratory plant-parasitic nematode can provide insight in the parasitism process and lead to more eYcient control measures. For the Wrst high throughput molecular characterization of this devastating nematode, 5,853 expressed sequence tags from a mixed stage population were generated. Adding 1,154 tags from the EST division of GenBank for subsequent analysis, resulted in a total of 7,007 ESTs, which represent approximately 3,200 genes. The mean G + C content of the nucleotides at the third codon position (GC3%) was calculated to be as high as 64.8%, the highest for nematodes reported to date. BLAST-searches resulted in about 70% of the clustered ESTs having homology to (DNA and protein) sequences from the GenBank database, whereas one-third of them did not match to any known sequence. Roughly 40% of these latter sequences are predicted to be coding, representing putative novel protein coding genes. Functional annotation of the sequences by GO annotation revealed the abundance of genes involved in reproduction and development, which reXects the nematode population biology. Genes with a role in the parasitism process are identiWed, as well as genes essential for nematode survival, providing information useful for parasite control. No evidence was found for the presence of trans-spliced leader sequences commonly occurring in nematodes, despite the use of various approaches. In conclusion, we found three diVerent sources for the EST sequences: the majority has a nuclear origin, approximately 1% of the EST sequences are derived from the mitochondrial transcriptome, and interestingly, 1% of the tags are with high probability derived from Wolbachia, providing the Wrst molecular indication for the presence of this endosymbiont in a plant-parasitic nematode.Keywords Expressed sequence tag analysis · Trans-spliced leader · Parasitism · G + C content · Wolbachia · Endoparasitic migratory nematode

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“…These are the polyprotein allergen proteins of nematodes (NPAs) which bind fatty acids and retinol [11][12][13][14][15][16][17][18]. Some NPAs exhibit dramatic differences in the sequences of the repeated units, although each possesses conserved signature amino acid positions [15,16].…”

Section: Introductionmentioning

confidence: 99%

Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris suum have similar fatty-acid- and retinol-binding properties but different binding-site environments

Moore

McDermott

Price

et al. 1999

Biochemical Journal

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Polyproteins comprise long polypeptides that are posttranslationally cleaved into proteins of different function, or tandemly repetitive polypeptides which are processed into multiple versions of proteins which are presumed to have the same function. In the latter case the individual units of the polyprotein can differ substantially in sequence. Identity of function between the different units therefore cannot be assumed. Here we have examined the ABA-1 polyprotein allergen of the parasitic nematode Ascaris suum and found it to contain units which show a 50 % difference in amino acid sequence. The parasite therefore produces at least two radically different forms of the allergen encoded within the polyprotein array. In fluorescence-based ligand-binding assays, recombinant polypeptides representing the two forms (designated ABA-1A1 and ABA-1B1) showed similar binding affinities for a range of fluorescent active-site probes [retinol, dansylundecanoic acid, dansyl--α-amino-

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The gp15400 polyprotein antigen of Brugia malayi binds fatty acids and retinoids

Cited by 48 publications

References 27 publications

The Ov20 Protein of the Parasitic Nematode Onchocerca volvulus

The Ov20 Protein of the Parasitic Nematode Onchocerca volvulus

Exploring the transcriptome of the burrowing nematode Radopholus similis

Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris suum have similar fatty-acid- and retinol-binding properties but different binding-site environments

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