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Model of the potential role of pallilysin in <i>T. pallidum</i> dissemination.

By Simon Houston (147985), Rebecca Hof (147988), Lisa Honeyman (147990), Julia Hassler (147994) and Caroline E. Cameron (147998)


<p>(i) Surface-exposed pallilysin (C<sup>24</sup>-P<sup>237</sup>) mediates attachment of <i>T. pallidum</i> (<$>\scale 60%\raster="rg1"<$>) to host components, including the laminin-rich basement membrane (BM) that underlies the endothelial cells (EC) of blood vessels and to fibrinogen/fibrin clots. The N-terminal pro-domain of pallilysin is removed via host thrombin-mediated cleavage (cleavage at S<sup>78</sup>) or autocatalytic activation (cleavage at T<sup>93</sup>), which results in release of pallilysin from the treponemal surface into the external host milieu. (ii) Released pallilysin (S<sup>78</sup>-P<sup>237</sup> and/or T<sup>93</sup>-P<sup>237</sup>) degrades host components located in the vicinity of the disseminating treponemes, including the laminin-rich BM and fibrin clots.</p

Topics: Biochemistry, Microbiology, Cell Biology, pallilysin
Year: 2012
DOI identifier: 10.1371/journal.ppat.1002822.g010
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Provided by: FigShare
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