The ability of Treponema pallidum to disseminate throughout the host and exit from the vasculature is crucial to its pathogenesis. This process is governed by T. pallidum proteins, including TP0751 (also known as pallilysin), that mediate attachment to the host extracellular matrix (ECM). However, the molecular mechanisms that underlie TP0751–ECM interactions are incompletely understood. Parker, Houston et al. solved the crystal structure of TP0751 to a resolution of 2.15 Å and reported that TP0751 adopts an eight-stranded β-barrel-containing lipocalin structure. Using a peptide library that represents the full TP0751 sequence they showed that binding to host ECM components was mediated by the lipocalin domain. The TP0751 ECM-binding peptides could inhibit the adhesion of a TP0751-expressing Borrelia burgdorferi strain to host cells. Thus, targeting defined regions of TP0751 could control the dissemination of T. pallidum.
References
Parker, M. L., Houston, S. et al. The structure of Treponema pallidum Tp0751 (pallilysin) reveals a non-canonical lipocalin fold that mediates adhesion to extracellular matrix components and interactions with host cells. PLoS Pathog. 12, e1005919 (2016)
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Du Toit, A. Spirochete spreading. Nat Rev Microbiol 14, 667 (2016). https://doi.org/10.1038/nrmicro.2016.155
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DOI: https://doi.org/10.1038/nrmicro.2016.155