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  • Probing the equatorial groove of the hookworm protein and vaccine candidate antigen, Na-ASP-2

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    Author(s)
    Mason, Lyndel
    Tribolet, Leon
    Simon, Anne
    von Gnielinski, Natascha
    Nienaber, Lisa
    Taylor, Paul
    Willis, Charlene
    Jones, Malcolm K
    Sternberg, Paul W
    Gasser, Robin B
    Loukas, Alex
    Hofmann, Andreas
    Griffith University Author(s)
    Hofmann, Andreas
    Willis, Charlene
    Mason, Lyndel
    von Gnielinski, Natascha S.
    Nienaber, Lisa M.
    Jones, Malcolm K.
    Year published
    2014
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    Abstract
    Hookworm activation-associated secreted proteins can be structurally classified into at least three different groups. The hallmark feature of Group 1 activation-associated secreted proteins is a prominent equatorial groove, which is inferred to form a ligand binding site. Furthermore, a conserved tandem histidine motif is located in the centre of the groove and believed to provide or support a yet to be determined catalytic activity. Here, we report three-dimensional crystal structures of Na-ASP-2, an L3-secreted activation-associated secreted protein from the human hookworm Necator americanus, which demonstrate transition ...
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    Hookworm activation-associated secreted proteins can be structurally classified into at least three different groups. The hallmark feature of Group 1 activation-associated secreted proteins is a prominent equatorial groove, which is inferred to form a ligand binding site. Furthermore, a conserved tandem histidine motif is located in the centre of the groove and believed to provide or support a yet to be determined catalytic activity. Here, we report three-dimensional crystal structures of Na-ASP-2, an L3-secreted activation-associated secreted protein from the human hookworm Necator americanus, which demonstrate transition metal binding ability of the conserved tandem histidine motif. We further identified moderate phosphohydrolase activity of recombinant Na-ASP-2, which relates to the tandem histidine motif. By panning a random 12-mer peptide phage library, we identified a peptide with high similarity to the human calcium-activated potassium channel SK3, and confirm binding of the synthetic peptide to recombinant Na-ASP-2 by differential scanning fluorimetry. Potential binding modes of the peptide to Na-ASP-2 were studied by molecular dynamics simulations which clearly identify a preferred topology of the Na-ASP-2:SK3 peptide complex.
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    Journal Title
    The International Journal of Biochemistry & Cell Biology
    Volume
    50
    DOI
    https://doi.org/10.1016/j.biocel.2014.03.003
    Copyright Statement
    © 2014 Elsevier Ltd. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
    Subject
    Biochemistry and cell biology
    Medical biochemistry and metabolomics
    Medical parasitology
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/62346
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    • Journal articles

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