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DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2019-04-15
  • AnnouncementXML: Submission_2019-04-15_07:10:27.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Farnusch Kaschani
  • Title: Re-annotated role of beta-Galactosidase in Flagellin deglycosylation
  • Description: Most Eukaryotes recognise flagellin as a signature of bacterial invasion. In contrast to animals, plants do not recognise flagellin proteins, but conserved peptides released from flagellin (Felix et al., 1999). However, these peptides (e.g. flg22) are folded and buried deeply inside the flagellin polymer and would need to be released before they can interact with cell surface receptors, such as FLS2 (Fliegman & Felix, 2016). Here we discovered that the hydrolytic pathway releasing the flagellin elicitor in plants is initiated by a host-secreted beta-galactosidase (BGAL), which removes the terminal modified viosamine (mVio) from the O-glycan that cloaks the flagellin polymer. BGAL contributes to flagellin-dependent immunity but only against bacterial Pseudomonas syringae strains that carry mVio. Signatures of arms races at this new level of antagonistic interactions are that BGAL is suppressed during infection by a heat stable metabolite secreted by bacteria, and that other P. syringae strains carry BGAL-insensitive O-glycans.
  • SpeciesList: scientific name: Nicotiana benthamiana; NCBI TaxID: 4100; scientific name: Pseudomonas syringae pv. tomato; NCBI TaxID: 323;
  • ModificationList: monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
  • Instrument: LTQ Orbitrap Elite

Dataset History

VersionDatetimeStatusChangeLog Entry
02018-07-17 08:16:52ID requested
12019-04-15 07:10:29announced

Publication List

  1. Buscaill P, Chandrasekar B, Sanguankiattichai N, Kourelis J, Kaschani F, Thomas EL, Morimoto K, Kaiser M, Preston GM, Ichinose Y, van der Hoorn RAL, Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides. Science, 364(6436):(2019) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: beta-galactosidase, Pseudomonas syringae, flagellin, O-glycosylation, viosamine

Contact List

    Farnusch Kaschani
    • contact affiliation: Analytics Core Facility Essen (ACE), Chemische Biologie, Universitšt Duisburg-Essen, ZMB, Germany
    • contact email: farnusch.kaschani@uni-due.de
    • lab head:
    Farnusch Kaschani
    • contact affiliation: University Duisburg-Essen
    • contact email: farnusch.kaschani@uni-due.de
    • dataset submitter:

Full Dataset Link List

  1. Dataset FTP location
  2. PRIDE project URI
Repository Record List

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