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The ABA-1 allergen of Ascaris lumbricoides: sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties

Xia, Y., Spence, H.J., Moore, J., Heaney, N., McDermott, L., Cooper, A., Watson, D.G., Mei, B., Komuniecki, R., and Kennedy, M.W. (2000) The ABA-1 allergen of Ascaris lumbricoides: sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties. Parasitology, 120 (2). pp. 211-224. ISSN 0031-1820 (doi:10.1017/S0031182099005363)

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Publisher's URL: http://dx.doi.org/10.1017/S0031182099005363

Abstract

The ABA-1 protein of Ascaris lumbricoides (of humans) and Ascaris suum (of pigs) is abundant in the pseudocoelomic fluid of the parasites and also appears to be released by the tissue- parasitic larvae and the adult stages. The genes encoding the polyprotein precursor of ABA-1 (aba-1) were found to be arranged similarly in the two taxa, comprising tandemly repeating units encoding a large polyprotein which is cleaved to yield polypeptides of approximately 15 kDa which fall into 2 distinct classes, types A and B. The polyprotein possibly comprises only 10 units. The aba-1 gene of A. lumbricoides is polymorphic, and the majority of substitutions observed occur in or near predicted loop regions in the encoded proteins. mRNA for ABA-1 is present in infective larvae within the egg, and in all parasitic stages, but was not detectable in unembryonated eggs. ABA-1 mRNA was confined to the gut of adult parasites, and not in body wall or reproductive tissues. Recombinant protein representing a single A-type unit for the A. lumbricoides aba-1 gene was produced and found to bind retinol (Vitamin A) and a range of fatty acids, including the pharmacologically active lipids lysophosphatidic acid, lysoplatelet activating factor, and there was also evidence of binding to leukotrienes. It failed to bind to any of the anthelmintics screened. Differential Scanning Calorimetry showed that the recombinant protein was highly stable, and unfolded in a single transition at 90.4 degrees C. Analysis of the transition indicated that the protein occurs as a dimer and that the dimer dissociates simultaneously with the unfolding of the monomer units.

Item Type:Article
Status:Published
Refereed:Yes
Glasgow Author(s):Spence, Dr Heather
Authors: Xia, Y., Spence, H.J., Moore, J., Heaney, N., McDermott, L., Cooper, A., Watson, D.G., Mei, B., Komuniecki, R., and Kennedy, M.W.
Subjects:Q Science > QL Zoology
T Technology > TJ Mechanical engineering and machinery
College/School:College of Science and Engineering > School of Chemistry
College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Parasitology
ISSN:0031-1820

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