Details

Autor(en) / Beteiligte

• King, Nathan P
• Newton, Patrice
• Schuelein, Ralf
• Brown, Darren L
• Petru, Marketa
• Zarsky, Vojtech
• Dolezal, Pavel
• Luo, Lin
• Bugarcic, Andrea
• Stanley, Amanda C
• Murray, Rachael Z
• Collins, Brett M
• Teasdale, Rohan D
• Hartland, Elizabeth L
• Stow, Jennifer L

Titel

Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophilaDot/Icm effector

Ist Teil von

• Cellular microbiology, 2015-06, Vol.17 (6), p.767

Ort / Verlag

Oxford: Hindawi Limited

Erscheinungsjahr

2015

Link zum Volltext

Quelle

Wiley Online Library Journals Frontfile Complete

Beschreibungen/Notizen

• Summary Upon infection, Legionella pneumophila uses the Dot/Icm type IV secretion system to translocate effector proteins from the Legionella-containing vacuole (LCV) into the host cell cytoplasm. The effectors target a wide array of host cellular processes that aid LCV biogenesis, including the manipulation of membrane trafficking. In this study, we used a hidden Markov model screen to identify two novel, non-eukaryotic soluble NSF attachment protein receptor (SNARE) homologs: the bacterial LegionellaSNARE effector A (LseA) and viral SNARE homolog A proteins. We characterized LseA as a Dot/Icm effector of L.pneumophila, which has close homology to the Qc-SNARE subfamily. The lseA gene was present in multiple sequenced L.pneumophila strains including Corby and was well distributed among L.pneumophila clinical and environmental isolates. Employing a variety of biochemical, cell biological and microbiological techniques, we found that farnesylated LseA localized to membranes associated with the Golgi complex in mammalian cells and LseA interacted with a subset of Qa-, Qb- and R-SNAREs in host cells. Our results suggested that LseA acts as a SNARE protein and has the potential to regulate or mediate membrane fusion events in Golgi-associated pathways.