PXD010894

PXD010894 is an original dataset announced via ProteomeXchange.

Title	LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: phosphoprotein patterns in babesiosis caused by Babesia canis, a case study
Description	Phosphorylation is the most commonly studied protein post-translational modification (PTM) in biological systems due to its importance in controlling cell division, survival, growth, etc. Despite the thorough research in phosphoproteomics of cells and tissues there is little information on circulating phosphoproteins. We compared serum from 10 healthy dogs and 10 dogs affected by B. canis-caused babesiosis with no organ dysfunctions by employing gel-free LC-MS/MS analysis of individual samples and tandem mass tag (TMT) label-based quantitative analyses of pools, both supported by phosphopeptide enrichment. Results showed a moderate number of phosphorylated proteins (50-55), with 89 phosphorylation sites not previously published for dogs although a number of them matched phosphorylation sites found in mammalian orthologs. Three phosphopeptides showed significant variation in babesiosis-affected dog sera compared to controls: Serum amyloid A (SAA) phosphorylated at serine 101 (up-regulation), kininogen 1 phosphorylated at threonine 326, and fibrinogen α phosphorylated at both threonine 20 and serine 22 (down-regulation). 71.9 % of the detected phosphorylated sites were phosphoserine, 16.8 % phosphothreonine and only 11.2 % phosphotyrosine residues. TMT label-based quantitative analysis showed α-2-HS-glycoprotein / Fetuin A to be the most abundant phosphoprotein (50-70% of all phosphoproteins) followed by kininogen-1 (10-20%). The alterations of phosphorylated proteins observed in canine babesiosis caused by Babesia canis suggest new insights into the largely neglected role of extracellular protein phosphorylation in health and disease, encouraging urgent further research on this area. To the best of our knowledge the present study represents the first attempt to characterize canine serum phosphoproteome.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:12:40.141.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Asier Galan
SpeciesList	scientific name: Canis lupus x Canis lupus familiaris; NCBI TaxID: 990119;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2018-08-28 04:02:35	ID requested
1	2018-11-13 02:46:14	announced
2	2018-12-04 03:59:54	announced	Updated project metadata.
3	2019-05-31 02:24:55	announced	Updated project metadata.
⏵ 4	2024-10-22 04:12:42	announced	2024-10-22: Updated project metadata.

10.1371/journal.pone.0207245;

Gal, á, n A, Horvati, ć A, Kule, š J, Bili, ć P, Goti, ć J, Mrljak V, LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study. PLoS One, 13(11):e0207245(2018) [pubmed]

curator keyword: Biological

submitter keyword: Phosphorylation sites, Phosphopeptide enrichment, Babesiosis,Phosphoproteomics, serum phosphopeptides

Vladimir Mrljak
contact affiliation	ERA Chair laboratory, Internal Diseases Clinic, Faculty of Veterinary Medicine, University of Zagreb, Croatia
contact email	vmrljak@vef.hr
lab head
Asier Galan
contact affiliation	1 ERA Chair FP7, Internal diseases, Faculty of Veterinary Medicine, University of Zagreb, Heinzelova 55, 10 000 Zagreb,
contact email	asier_gal@hotmail.com
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/2018/11/PXD010894

PRIDE project URI

• PRIDE
  1. PXD010894
     1. Label: PRIDE project
     2. Name: LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: phosphoprotein patterns in babesiosis caused by Babesia canis, a case study