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

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. and Stow, Jennifer L. (2015) Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophila Dot/Icm effector. Cellular Microbiology, 17 6: 767-784. doi:10.1111/cmi.12405

Author 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.
Title Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophila Dot/Icm effector
Journal name Cellular Microbiology   Check publisher's open access policy
ISSN 1462-5814
Publication date 2015-01-24
Sub-type Article (original research)
DOI 10.1111/cmi.12405
Open Access Status
Volume 17
Issue 6
Start page 767
End page 784
Total pages 18
Place of publication Chichester, West Sussex, United Kingdom
Publisher Wiley-Blackwell Publishing
Collection year 2016
Language eng
Formatted abstract
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 SNARE homologs: the bacterial LseA and viral VshA 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 amongst 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.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 6 times in Thomson Reuters Web of Science Article | Citations
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Created: Mon, 15 Dec 2014, 15:11:43 EST by Susan Allen on behalf of Institute for Molecular Bioscience