BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells.

We report the functional characterization of BipA, a GTPase that undergoes tyrosine phosphorylation in an enteropathogenic Escherichia coli (EPEC) strain. BipA mutants adhere to cultured epithelial cells but fail to trigger the characteristic cytoskeletal rearrangements found in cells infected with wild-type EPEC. In contrast, increased expression of BipA enhances actin remodelling and results in the hyperformation of pseudopods. BipA appears to be the first example of a new class of virulence regulator, as it also controls flagella-mediated cell motility and resistance to the antibacterial effects of a human host defence protein. Its striking sequence similarity to ribosome-binding elongation factors suggests that it uses a novel mechanism to modulate gene expression.

158-microJ pulses from a single-transverse-mode, large-mode-area erbium-doped fiber amplifier.

We report the amplification of 10-100-pJ semiconductor diode pulses to an energy of 158 microJ and peak powers >100 kW in a multistage fiber amplifier chain based on a single-mode, large-mode-area erbium-doped amplifier design. To our knowledge these results represent the highest single-mode pulse energy extracted from any doped-fiber system.