title: Functional dissection of SiiE, a giant non-fimbrial adhesin of Salmonella enterica.
abstract: 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 β-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.
authors: Abteilung Mikrobiologie, Universität Osnabrück, Osnabrück, Germany.
authors: Carolin
authors: C
authors: Wagner
authors: Melanie
authors: M
authors: Polke
authors: Roman G
authors: RG
authors: Gerlach
authors: Dirk
authors: D
authors: Linke
authors: York-Dieter
authors: YD
authors: Stierhof
authors: Heinz
authors: H
authors: Schwarz
authors: Michael
authors: M
authors: Hensel
mesh_terms: D018829:Adhesins, Bacterial / Q000235:genetics* / Q000378:metabolism*; D004252:DNA Mutational Analysis; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012486:Salmonella typhimurium / Q000235:genetics* / Q000502:physiology*
chemical_list: D018829:Adhesins, Bacterial; C059826:adhesin, Salmonella