PXD025218

PXD025218 is an original dataset announced via ProteomeXchange.

Title	N-linked glycoproteins from exosome-depleted excretory-secretory products of fourth-stage larval Angiostrongylus cantonensis promotes alternative activation of macrophages through metabolic reprogramming by the PI3K-Akt pathway
Description	Angiostrongylus cantonensis (AC), which parasitizes in the brain of the non-permissive host, such as mouse and human, is an etiologic agent of eosinophilic meningitis. Excretory-secretory (ES) products play an important role in the interaction between parasites and hosts’ immune responses. Inflammatory macrophages are responsible for eosinophilic meningitis induced by AC, and the soluble antigens of Angiostrongylus cantonensis fourth stage larva (AC L4), a mimic of dead AC L4, aggravate eosinophilic meningitis in AC-infected mice model via promoting alternative activation of macrophages. In this study, we investigated the key molecules in the ES products of AC L4 on macrophages and observed the relationship between metabolic reprogramming and the PI3K-Akt pathway. First, a co-culture system of macrophage and AC L4 was established to define the role of AC L4 ES products on macrophage polarization. Then, AC L4 exosome and exosome-depleted excretory-secretory products (exofree) were separated from AC L4 ES products using differential centrifugation, their distinct roles on macrophage polarization were confirmed using qPCR and ELISA experiments. Moreover, AC L4 exofree induced alternative activation of macrophages, which is partially associated with metabolic reprogramming by the PI3K-Akt pathway. Next, lectin blot and deglycosylation assay suggesting the key role of N-linked glycoproteins in exofree. Then, glycoproteomic analysis of exofree and RNA-seq analysis of exofree-treated macrophage were performed. Bi-layer PPI network analysis based on these results identified that macrophage-related protein Hexa as a key molecule in inducing alternative activation of macrophages. Our results indicate a great value for research of helminth-derived immunoregulatory molecules, which might contribute to drug development for immune-related diseases.
HostingRepository	PRIDE
AnnounceDate	2021-07-28
AnnouncementXML	Submission_2021-07-27_22:15:06.807.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sun Xi
SpeciesList	scientific name: Angiostrongylus cantonensis; NCBI TaxID: 6313;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2021-04-06 07:12:31	ID requested
⏵ 1	2021-07-27 22:15:07	announced

Dataset with its publication pending

submitter keyword: Angiostrongylus cantonensis, exosome-depleted excretory-secretory products, N-linked glycoproteins, macrophage polarization, mechanism

Xi Sun
contact affiliation	1Department of Parasitology of Zhongshan School of Medicine, Sun Yat-sen University, No.74 Zhongshan Road.2, Guangzhou, Guangdong, 510080, China. 2Key Laboratory of Tropical Disease Control (SYSU), Ministry of Education, Guangzhou, Guangdong, 510080, China. 3Provincial Engineering Technology Research Center for Biological Vector Control, Guangzhou, Guangdong, 510080, China.
contact email	sunxi2@mail.sysu.edu.cn
lab head
Sun Xi
contact affiliation	SUN YAT-SEN UNIVERSITY
contact email	sunxi2@mail.sysu.edu.cn
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/2021/07/PXD025218

PRIDE project URI

• PRIDE
  1. PXD025218
     1. Label: PRIDE project
     2. Name: N-linked glycoproteins from exosome-depleted excretory-secretory products of fourth-stage larval Angiostrongylus cantonensis promotes alternative activation of macrophages through metabolic reprogramming by the PI3K-Akt pathway