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

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

Research output: Contribution to journalArticleResearchpeer-review

14 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)767-784
Number of pages18
JournalCellular Microbiology
Issue number6
Publication statusPublished - Jun 2015
Externally publishedYes

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