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• W1900280231 endingPage "784" @default.
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• W1900280231 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 soluble NSF attachment protein receptor (SNARE) homologs: the bacterial Legionella SNARE 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." @default.
• W1900280231 created "2016-06-24" @default.
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• W1900280231 date "2015-01-24" @default.
• W1900280231 modified "2023-10-17" @default.
• W1900280231 title "Soluble NSF attachment protein receptor molecular mimicry by a<i>L</i><i>egionella pneumophila</i> Dot/Icm effector" @default.
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• W1900280231 doi "https://doi.org/10.1111/cmi.12405" @default.
• W1900280231 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25488819" @default.
• W1900280231 hasPublicationYear "2015" @default.
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