Thursday 23 February 2012

Domain organization of Legionella effector SetA

Domain organization of Legionella effector SetA - Jank - 2012 - Cellular Microbiology - Wiley Online LibrarySkip to Main Content

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DOI: 10.1111/j.1462-5822.2012.01761.x

© 2012 Blackwell Publishing Ltd

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How to CiteJank, T., Böhmer, K. E., Tzivelekidis, T., Schwan, C., Belyi, Y. and Aktories, K. (2012), Domain organization of Legionella effector SetA. Cellular Microbiology. doi: 10.1111/j.1462-5822.2012.01761.x

Author Information1

Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, Albertstr. 25, Freiburg D-79104, Germany

2

Gamaleya Research Institute, Ulitsa Gamalei 18, Moscow 123098, Russia

* E-mail klaus.aktories@pharmakol.uni-freiburg.de; Tel. (+49) 761 203 5301; Fax (+49) 761 203 5311.

Publication HistoryArticle first published online: 21 FEB 2012Accepted manuscript online: 31 JAN 2012 04:43AM ESTReceived 25 November, 2011; revised 13 January, 2012; accepted 17 January, 2012. SEARCH Search Scope All contentPublication titlesIn this journalIn this issue Search String Advanced >Saved Searches > SEARCH BY CITATION Volume: Issue: Page: ARTICLE TOOLSGet PDF (2198K)Save to My ProfileE-mail Link to this ArticleExport Citation for this ArticleGet Citation AlertsRequest Permissions AbstractArticleReferencesSupporting InformationCited By View Full Article with Supporting Information (HTML) Get PDF (2198K) Summary

Legionella pneumophila is a human pathogen causing severe pneumonia called Legionnaires' disease. Multiple Legionella effectors are type IV-secreted into the host cell to establish a specific vesicular compartment for pathogen replication. Recently, it has been reported that the Legionella effector SetA shares sequence similarity with glycosyltransferases and interferes with vesicular trafficking of host cells. Here we show that SetA possesses glycohydrolase and mono-O-glucosyltransferase activity by using UDP-glucose as a donor substrate. Whereas the catalytic activity is located at the N terminus of SetA, the C terminus (amino acids 401–644) is essential for guidance of SetA to vesicular compartments of host cells. EGFP-SetA expressed in HeLa cells localizes to early endosomes by interacting with phosphatidylinositol 3-phosphate. EGFP-SetA, transiently expressed in RAW 264.7 macrophages, associates with early phagosomes after infection with Escherichia coli and L. pneumophila. Only the combined expression of the C- and N-terminal domains induces growth defects in yeast similar to full-length SetA. The data indicate that SetA is a multidomain protein with an N-terminal glucosyltransferase domain and a C-terminal phosphatidylinositol 3-phosphate-binding domain, which guides the Legionella effector to the surface of the Legionella-containing vacuole. Both, the localization and the glucosyltransferase domains of SetA are crucial for cellular functions.

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