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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

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    Authors
    Xia, Y.
    Spence, H.J.
    Moore, Joyce
    Heaney, N.
    McDermott, Lindsay C.
    Cooper, Alan
    Watson, D.G.
    Mei, B.
    Komuniecki, R.
    Kennedy, Malcolm W.
    Affiliation
    University of Glasgow
    University of Louisville
    University of Strathclyde
    University of Toledo
    University of California, Berkeley
    Issue Date
    2000-02-28
    Subjects
    n-3 polyunsaturated fatty acids
    C700 Molecular Biology, Biophysics and Biochemistry
    
    Metadata
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    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.
    Citation
    Xia Y, Spence HJ, Moore J, Heaney N, McDermott L, Cooper A, Watson DG, Mei B, Komuniecki R, Kennedy MW (2000) 'The ABA-1 allergen of Ascaris lumbricoides: sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties', Parasitology, 120 (), pp.211-224.
    Publisher
    Cambridge University Press
    Journal
    Parasitology
    URI
    http://hdl.handle.net/10547/622685
    PubMed ID
    10726282
    Additional Links
    https://www.cambridge.org/core/journals/parasitology/article/aba1-allergen-of-ascaris-lumbricoides-sequence-polymorphism-stage-and-tissuespecific-expression-lipid-binding-function-and-protein-biophysical-properties/0A0BDC6EEFACB82B41FF57F5C3C80DD6
    Type
    Article
    Language
    en
    ISSN
    0031-1820
    Collections
    Biomedical and biological science

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