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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
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dc.creatorPeters, Britta-
dc.creatorStein, Johanna-
dc.creatorKlingl, Stefan-
dc.creatorSander, Nathalie-
dc.creatorSandmann, Achim-
dc.creatorTaccardi, Niccola-
dc.creatorSticht, Heinrich-
dc.creatorGerlach, Roman G.-
dc.creatorMuller, Yves A.-
dc.creatorHensel, Michael-
dc.date.accessioned2018-01-05T11:14:18Z-
dc.date.available2018-01-05T11:14:18Z-
dc.date.issued2018-01-05T11:14:18Z-
dc.identifier.citationPlos Pathogens 13(5) 2017:e1006418-
dc.identifier.urihttps://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2018010516499-
dc.description.abstractThe 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.relationhttp://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006418-
dc.rightsNamensnennung 4.0 International-
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/-
dc.subjectsecretioneng
dc.subjectsecretion systemseng
dc.subjectadhesinseng
dc.subjectprotein secretionger
dc.subjectcrystal structureeng
dc.subjectSalmonellaeng
dc.subjectmutant strainseng
dc.subjecttryptophaneng
dc.subject.ddc570 - Biowissenschaften, Biologie-
dc.titleStructural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella entericaeng
dc.typeEinzelbeitrag in einer wissenschaftlichen Zeitschrift [article]ger
dc.identifier.doi10.1371/journal. ppat.1006418-
vCard.ORGFB5-
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