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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 1 - Protein Evolution (A. Lupas)     Display Documents



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ID: 591420.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
Functional dissection of SiiE, a giant non-fimbrial adhesin of Salmonella enterica
Authors:Wagner, C.; Polke, M.; Gerlach, R. G.; Linke, D.; Stierhof, Y. D.; Schwarz, H.; Hensel, M.
Date of Publication (YYYY-MM-DD):2011-08
Title of Journal:Cell Microbiol
Volume:13
Issue / Number:8
Start Page:1286
End Page:1301
Review Status:not specified
Audience:Not Specified
Abstract / Description:Salmonella enterica deploys the giant non-fimbrial adhesin SiiE to adhere to the apical side of polarized epithelial cells. The establishment of close contact is a prerequisite for subsequent invasion mediated by translocation of effector proteins of the Salmonella Pathogenicity Island 1 (SPI1)-encoded type III secretion system (T3SS). Although SiiE is secreted into the culture medium, the adhesin is retained on the bacterial envelope in the phase of highest bacterial invasiveness. To dissect the structural requirements for secretion, retention and adhesive properties, comprehensive deletional and functional analyses of various domains of SiiE were performed. We observed that beta-sheet and coiled-coil domains in the N-terminal moiety of SiiE are required for the control of SiiE retention on the surface and co-ordinated release. These results indicate a novel molecular mechanism for the control of surface display of a T1SS-secreted adhesin that acts cooperatively with the SPI1-T3SS.
Free Keywords:Adhesins, Bacterial/*genetics/*metabolism; DNA Mutational Analysis; Microscopy, Electron; Microscopy, Fluorescence; Models, Molecular; Protein Structure, Tertiary; Salmonella typhimurium/*genetics/*physiology
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
External Affiliations:%G eng
Identifiers:ISSN:1462-5822 (Electronic) 1462-5814 (Linking) %R 10.1... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/21729227 [ID No:2]
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