Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophila Dot/Icm effector. (24th January 2015)

• Record Type: Journal Article
• Authors: 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.
• Is Part Of: Cellular microbiology. Volume 17:Number 6(2015:Jun.)
• Page Start: 767
• Page End: 784
• Publication Date: 2015-01-24
• Subjects: Microbiology -- Periodicals; Cytology -- Periodicals; Host-parasite relationships -- Periodicals; Microbiology -- Periodicals; Cells -- Periodicals; Microbiologie -- Périodiques; Microbiologie; Relation hôte-parasite; Cytologie; Cellule; Réponse cellulaire; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); 579.05
• DOI: 10.1111/cmi.12405
• Languages: English
• ISSNs: 1462-5814

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>Upon infection, <italic>L</italic><italic>egionella pneumophila</italic> uses the Dot/Icm type IV secretion system to translocate effector proteins from the <italic>L</italic><italic>egionella</italic>‐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 <underline>s</underline>oluble <underline>N</underline>SF <underline>a</underline>ttachment protein <underline>re</underline>ceptor (SNARE) homologs: the bacterial <italic>L</italic><italic>egionella</italic> SNARE effector A (LseA) and viral SNARE homolog A proteins. We characterized LseA as a Dot/Icm effector of <italic>L</italic><italic>. pneumophila</italic>, which has close homology to the Qc‐SNARE subfamily. The <italic>lseA</italic> gene was present in multiple sequenced <italic>L</italic><italic>. pneumophila</italic> strains including Corby and was well distributed among <italic>L</italic><italic>. pneumophila</italic> 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.</p> </abstract>