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Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophila Dot/Icm effector
NP. King, P. Newton, R. Schuelein, DL. Brown, M. Petru, V. Zarsky, P. Dolezal, L. Luo, A. Bugarcic, AC. Stanley, RZ. Murray, BM. Collins, RD. Teasdale, EL. Hartland, JL. Stow,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1999 do Před 2 roky
Medline Complete (EBSCOhost)
od 1999-07-01 do 2021-12-31
Wiley Free Content
od 1999 do 2021
ROAD: Directory of Open Access Scholarly Resources
od 1999
PubMed
25488819
DOI
10.1111/cmi.12405
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny metabolismus MeSH
- buněčné linie MeSH
- epitelové buňky mikrobiologie MeSH
- faktory virulence metabolismus MeSH
- interakce hostitele a patogenu * MeSH
- Legionella pneumophila fyziologie MeSH
- lidé MeSH
- makrofágy mikrobiologie MeSH
- molekulární mimikry * MeSH
- myši MeSH
- rozpustné proteiny pro vazbu faktoru citlivého k N-ethylmaleimidu metabolismus MeSH
- sekvenční homologie aminokyselin MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.
Department of Parasitology Charles University Prague Czech Republic
Institute for Molecular Bioscience The University of Queensland Brisbane Qld Australia
Citace poskytuje Crossref.org
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