PXD011371-1

PXD011371 is an original dataset announced via ProteomeXchange.

Title	binding specificity of Native Odorant-Binding Protein isoforms is driven by phosphorylation and O-N-acetylglucosamiylation in the pig (sus scrofa)
Description	In pig, phosphorylation drives binding specificity of recombinant OBP (stricto sensu, referred as OBP in this text) isoforms (Brimau et al., 2010) that are not O-GlcNAcylated, contrary to native OBP, purified from nasal tissue (Nagnan-Le Meillour et al., 2014). In order to precise the role of both PTM in OBP binding abilities to pheromone components in pig, we purified OBP isoforms by HPLC and performed structure-function relationship study. We have identified phosphorylation and O-GlcNAcylation on 4 OBP isoforms by immunodetection with specific antibodies, with careful controls. The binding properties of the 4 isoforms were monitored by fluorescence spectroscopy in exactly the same conditions previously used for recombinant OBP isoforms (Brimau et al., 2010). The PTM sites were mapped by CID-nano-LC-MS/MS and BEMAD (for phosphorylation) to link the binding affinities to phosphorylation and O-GlcNAcylation patterns of native OBP isoforms. Comparison of binding affinities between recombinant (only phosphorylated) and native (also O-GlcNAcylated) isoforms indicates that O-GlcNAcylation increases the binding specificity to pheromone components. This is the first time that such PTM sites are localized in OBP by high-resolution mass spectrometry, and that a demonstration of their involvement in odorant molecules discrimination by OBP isoforms is given
HostingRepository	PRIDE
AnnounceDate	2019-02-15
AnnouncementXML	Submission_2019-02-15_08:43:09.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD011371
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Alexandre Joly
SpeciesList	scientific name: Sus scrofa domesticus (domestic pig); NCBI TaxID: 9825;
ModificationList	Phospho; Glu->pyro-Glu; Deamidated; Oxidation; HexNAc; Carbamidomethyl; Gln->pyro-Glu
Instrument	maXis

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-16 06:28:45	ID requested
⏵ 1	2019-02-15 08:43:11	announced

Nagnan-Le Meillour P, Joly A, Le Danvic C, Marie A, Zirah S, Cornard JP, . Front Endocrinol (Lausanne), 9():816(2018) [pubmed]

submitter keyword: O-GlcNAc, Odorant-Binding Protein, Phosphorylation, CID-nano-LC-MS/MS, Fluorescence spectroscopy, Pheromone

Patricia Nagnan-Le Meillour
contact affiliation	Unité de Glycobiologie Structurale et Fonctionnelle, UMR8576 CNRS-Université de Lille, USC-UGSF INRA 1409, Lille, Fr
contact email	patricia.nagnan@univ-lille.fr
lab head
Alexandre Joly
contact affiliation	CNRS
contact email	joly.alexandre14@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD011371
     1. Label: PRIDE project
     2. Name: binding specificity of Native Odorant-Binding Protein isoforms is driven by phosphorylation and O-N-acetylglucosamiylation in the pig (sus scrofa)