PXD013657

PXD013657 is an original dataset announced via ProteomeXchange.

Title	Protein N-glycosylation is sex-related in Nilaparvata lugens adults
Description	Nilaparvata lugens, or the brown planthopper, is one of the most notorious pest insects of cultured rice, and a model for hemimetabolous development. Recently, the N-glycome of N. lugens was explored throughout post-embryonic development and reproductive stages, which revealed differential protein N-glycosylation events between adult sexes. Identifying the proteins carrying these differential carbohydrate structures would point to the functionality of sex-dependent N-glycosylation. Furthermore, potential effects of the adult wing type on protein N-glycosylation are of interest. Here, a comprehensive investigation of the N-glycosylation sites from the adult stages of N. lugens was conducted, allowing a qualitative and quantitative comparison between sexes and wing forms at the glycopeptide level. N-glycopeptide enrichment using the N-glyco-FASP method with the high mannose/paucimannose-binding lectin Concanavalin A, or the Rhizoctonia solani agglutinin which interacts with complex N-glycans led to the identification of over 1,300 N-glycosylation sites derived from over 600 glycoproteins. Comparison of these N-glycopeptides revealed striking differences in protein N-glycosylation between sexes, while almost no differences were observed between wing types. Male- and female-specific N-glycosylation sites were identified, and some of these sex-specific N-glycosites were shown to be derived from proteins with a putative role in insect reproduction. Transcript expression experiments with complete insects and insect tissues confirmed the sex-related N-glycosylation of proteins, and expression of glycoproteins in reproductive tissues. In conclusion, this study provides original data on N-glycosylation sites of N. lugens adults, providing novel insights into planthopper’s biology and revealing that protein N-glycosylation is sex-related in this insect.
HostingRepository	PRIDE
AnnounceDate	2020-01-17
AnnouncementXML	Submission_2020-01-17_06:05:44.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	An Staes
SpeciesList	scientific name: Nilaparvata lugens; NCBI TaxID: 108931;
ModificationList	complex glycosylation
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-04-29 02:14:33	ID requested
⏵ 1	2020-01-17 06:05:46	announced

Scheys F, Van Damme EJM, Pauwels J, Staes A, Gevaert K, Smagghe G, ). Mol Cell Proteomics, 19(3):529-539(2020) [pubmed]

submitter keyword: N-linked glycosylation, N-glycosylation sites, Nilaparvata lugens, pest insect

Guy Smagghe
contact affiliation	Department of Plants and Crops, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, B-9000 Ghent, Belgium
contact email	Guy.Smagghe@UGent.be
lab head
An Staes
contact affiliation	Medical Protein Chemistry
contact email	an.staes@vib-ugent.be
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/2020/01/PXD013657

PRIDE project URI

• PRIDE
  1. PXD013657
     1. Label: PRIDE project
     2. Name: Protein N-glycosylation is sex-related in Nilaparvata lugens adults