PXD010461

PXD010461 is an original dataset announced via ProteomeXchange.

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.
HostingRepository	PRIDE
AnnounceDate	2019-04-15
AnnouncementXML	Submission_2019-04-15_07:10:27.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Farnusch Kaschani
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

Revision	Datetime	Status	ChangeLog Entry
0	2018-07-17 08:16:52	ID requested
⏵ 1	2019-04-15 07:10:29	announced

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]

curator keyword: Biological

submitter keyword: beta-galactosidase, Pseudomonas syringae, flagellin, O-glycosylation, viosamine

Farnusch Kaschani
contact affiliation	Analytics Core Facility Essen (ACE), Chemische Biologie, Universität 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

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/04/PXD010461

PRIDE project URI

• PRIDE
  1. PXD010461
     1. Label: PRIDE project
     2. Name: Re-annotated role of beta-Galactosidase in Flagellin deglycosylation