Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica
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https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2018010516499
Full metadata record
DC Field | Value | Language |
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dc.creator | Peters, Britta | - |
dc.creator | Stein, Johanna | - |
dc.creator | Klingl, Stefan | - |
dc.creator | Sander, Nathalie | - |
dc.creator | Sandmann, Achim | - |
dc.creator | Taccardi, Niccola | - |
dc.creator | Sticht, Heinrich | - |
dc.creator | Gerlach, Roman G. | - |
dc.creator | Muller, Yves A. | - |
dc.creator | Hensel, Michael | - |
dc.date.accessioned | 2018-01-05T11:14:18Z | - |
dc.date.available | 2018-01-05T11:14:18Z | - |
dc.date.issued | 2018-01-05T11:14:18Z | - |
dc.identifier.citation | Plos Pathogens 13(5) 2017:e1006418 | - |
dc.identifier.uri | https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2018010516499 | - |
dc.description.abstract | The giant non-fimbrial adhesin SiiE of Salmonella enterica mediates the first contact to the apical site of epithelial cells and enables subsequent invasion. SiiE is a 595 kDa protein composed of 53 repetitive bacterial immunoglobulin (BIg) domains and the only known substrate of the SPI4-encoded type 1 secretion system (T1SS). The crystal structure of BIg50- 52 of SiiE revealed two distinct Ca2+-binding sites per BIg domain formed by conserved aspartate or glutamate residues. In a mutational analysis Ca2+-binding sites were disrupted by aspartate to serine exchange at various positions in the BIg domains of SiiE. Amounts of secreted SiiE diminish with a decreasing number of intact Ca2+-binding sites. BIg domains of SiiE contain distinct Ca2+-binding sites, with type I sites being similar to other T1SSsecreted proteins and type II sites newly identified in SiiE. We functionally and structurally dissected the roles of type I and type II Ca2+-binding sites in SiiE, as well as the importance of Ca2+-binding sites in various positions of SiiE. Type I Ca2+-binding sites were critical for efficient secretion of SiiE and a decreasing number of type I sites correlated with reduced secretion. Type II sites were less important for secretion, stability and surface expression of SiiE, however integrity of type II sites in the C-terminal portion was required for the function of SiiE in mediating adhesion and invasion. | eng |
dc.relation | http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006418 | - |
dc.rights | Namensnennung 4.0 International | - |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | - |
dc.subject | secretion | eng |
dc.subject | secretion systems | eng |
dc.subject | adhesins | eng |
dc.subject | protein secretion | ger |
dc.subject | crystal structure | eng |
dc.subject | Salmonella | eng |
dc.subject | mutant strains | eng |
dc.subject | tryptophan | eng |
dc.subject.ddc | 570 - Biowissenschaften, Biologie | - |
dc.title | Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica | eng |
dc.type | Einzelbeitrag in einer wissenschaftlichen Zeitschrift [article] | ger |
dc.identifier.doi | 10.1371/journal. ppat.1006418 | - |
vCard.ORG | FB5 | - |
Appears in Collections: | FB05 - Hochschulschriften Open-Access-Publikationsfonds |
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Artikel_ppat_13_5_2017_Hensel.pdf | 7,91 MB | Adobe PDF | Artikel_ppat_13_5_2017_Hensel.pdf View/Open |
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