@article{FischerHarrisonRamirezetal.2017,
  author    = {Fischer, Annette and Harrison, Kelly S and Ramirez, Yesid and Auer, Daniela and Chowdhury, Suvagata Roy and Prusty, Bhupesh K and Sauer, Florian and Dimond, Zoe and Kisker, Caroline and Hefty, P Scott and Rudel, Thomas},
  title     = {Chlamydia trachomatis-containing vacuole serves as deubiquitination platform to stabilize Mcl-1 and to interfere with host defense},
  series = {eLife},
  volume    = {6},
  journal   = {eLife},
  number    = {e21465},
  doi       = {10.7554/eLife.21465},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-171073},
  year      = {2017},
  abstract  = {Obligate intracellular Chlamydia trachomatis replicate in a membrane-bound vacuole called inclusion, which serves as a signaling interface with the host cell. Here, we show that the chlamydial deubiquitinating enzyme (Cdu) 1 localizes in the inclusion membrane and faces the cytosol with the active deubiquitinating enzyme domain. The structure of this domain revealed high similarity to mammalian deubiquitinases with a unique α-helix close to the substrate-binding pocket. We identified the apoptosis regulator Mcl-1 as a target that interacts with Cdu1 and is stabilized by deubiquitination at the chlamydial inclusion. A chlamydial transposon insertion mutant in the Cdu1-encoding gene exhibited increased Mcl-1 and inclusion ubiquitination and reduced Mcl-1 stabilization. Additionally, inactivation of Cdu1 led to increased sensitivity of C. trachomatis for IFNγ and impaired infection in mice. Thus, the chlamydial inclusion serves as an enriched site for a deubiquitinating activity exerting a function in selective stabilization of host proteins and protection from host defense.},
  language  = {en}
}
@article{WuPonsGoudetetal.2017,
  author    = {Wu, Yu and Pons, Val{\´e}rie and Goudet, Am{\´e}lie and Panigai, Laetitia and Fischer, Annette and Herweg, Jo-Ana and Kali, Sabrina and Davey, Robert A. and Laporte, J{\´e}r{\^o}me and Bouclier, C{\´e}line and Yousfi, Rahima and Aubenque, C{\´e}line and Merer, Goulven and Gobbo, Emilie and Lopez, Roman and Gillet, Cynthia and Cojean, Sandrine and Popoff, Michel R. and Clayette, Pascal and Le Grand, Roger and Boulogne, Claire and Tordo, No{\"e}l and Lemichez, Emmanuel and Loiseau, Philippe M. and Rudel, Thomas and Sauvaire, Didier and Cintrat, Jean-Christophe and Gillet, Daniel and Barbier, Julien},
  title     = {ABMA, a small molecule that inhibits intracellular toxins and pathogens by interfering with late endosomal compartments},
  series = {Scientific Reports},
  volume    = {7},
  journal   = {Scientific Reports},
  doi       = {10.1038/s41598-017-15466-7},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-173170},
  year      = {2017},
  abstract  = {Intracellular pathogenic microorganisms and toxins exploit host cell mechanisms to enter, exert their deleterious effects as well as hijack host nutrition for their development. A potential approach to treat multiple pathogen infections and that should not induce drug resistance is the use of small molecules that target host components. We identifed the compound 1-adamantyl (5-bromo-2-methoxybenzyl) amine (ABMA) from a cell-based high throughput screening for its capacity to protect human cells and mice against ricin toxin without toxicity. This compound efciently protects cells against various toxins and pathogens including viruses, intracellular bacteria and parasite. ABMA provokes Rab7-positive late endosomal compartment accumulation in mammalian cells without affecting other organelles (early endosomes, lysosomes, the Golgi apparatus, the endoplasmic reticulum or the nucleus). As the mechanism of action of ABMA is restricted to host-endosomal compartments, it reduces cell infection by pathogens that depend on this pathway to invade cells. ABMA may represent a novel class of broad-spectrum compounds with therapeutic potential against diverse severe infectious diseases.},
  language  = {en}
}