Kirsten Niebuhr

TL;DR: The contact hemolytic activity of Shigella flexneri was used to investigate its putative translocator and electron microscopy analysis indicated that secretons were constitutively assembled at 37°C before any host contact.

TL;DR: It is demonstrated that ActA–EVH1 binding is a paradigm for a novel class of eukaryotic protein–protein interactions involving a proline‐rich ligand that is clearly different from those described for SH3 and WW/WWP domains.

TL;DR: Upon infection of epithelial cells with the Gram‐negative pathogen Shigella flexneri, the virulence factor IpgD is translocated directly into eukaryotic cells and acts as a potent inositol 4‐phosphatase that specifically dephosphorylates phosphatidylinositol4,5‐bisphosphate into phosphatin cytoskeleton organization that then accumulates.

TL;DR: Following Listeria infection the host vasodilator‐stimulated phosphoprotein (VASP), a microfilament‐ and focal adhesion‐associated substrate of both the cAMP‐ and cGMP‐dependent protein kinases, accumulates on the surface of intracytoplasmic bacteria prior to the detection of F‐actin ‘clouds’.

TL;DR: The results identify the ActA polypeptide as a nucleator of the actin cytoskeleton and provide the first insights into the molecular nature of such controlling elements in microfilament organization.