Israel Nisan

TL;DR: A novel EspA‐containing filamentous organelle is described that is present on the bacterial surface during the early stage of A/E lesion formation, forms a physical bridge between the bacterium and the infected eukaryotic cell surface and is required for the translocation of EspB into infected epithelial cells.

TL;DR: It is demonstrated that contact of EPEC with HeLa cells is associated with the induction of production and secretion of EspB, which indicates that EspB is both translocated and required for protein translocation by EPEC.

TL;DR: It is shown that EspH is translocated efficiently into the infected cells by the TTSS and localizes beneath the EPEC microcolonies and is a modulator of the host actin cytoskeleton structure.

TL;DR: A stretch of 15 amino acids (block A) that is located C‐terminally to the repeat region and is essential for the toxic activity of CyaA is identified and suggested that functional complementation occurs because of binding between the Ca2+ binding repeats of the short C‐ terminal polypeptide and the Ca1+ binding repeat of the CyaB mutant lacking block A.

TL;DR: Enteropathogenic Escherichia coli strain 30-5-1(3), which has a transposon insertion within thesepZ gene, forms wild-type A/E lesions including Tir tyrosine phosphorylation, but at a slower rate.