PXD030370

PXD030370 is an original dataset announced via ProteomeXchange.

Title	Dissecting post-translational modifications in Leptospira proteome to elucidate novel insights into pathogen-host interaction using bioinformatics approach
Description	Leptospirosis is a zoonotic disease caused by Leptospira spp. that cause serious health burden. Humans are accidental host gets infected from water contaminated with Leptospira from urine of reservoir hosts like rodents and other mammals. Currently there is no effective vaccine available for leptospirosis. Investigations on post-translational modifications (PTMs) provide insights into the bacterial pathophysiology and functional consequences during bacterial infection and that can provide significant contribution in the search for better vaccine candidates. PTMs are decisive factors in the structure, function, and localization of proteins in both prokaryotic and eukaryotic organisms. In our previous investigations, we have identified PXD016204 (Thoduvayil et al., 2020) and PXD026044 (Sarma et al., 2021) from Leptospira interrogans serovar Copenhageni (strain Fiocruz L1-130). In this project, a systematic reanalysis of unassigned spectra were carried out from our previous total proteome data (PXD016204 and PXD026044) for multi-PTM analysis. We have identified a total of 3,693 unique high-confidence PTM sites corresponding to 1,266 proteins (PTM-Pro probability cut-off value is ≥75%). There were two objectives for the study. The first objective was the functional characterization of PTM proteins, through the identification of protein-protein interactions (PPI). This will enable us to understand the type and functions of PTMs. This analysis was supported by additional characteristics like gene ontology (GO), cluster of autologous groups (COG), other protein features and functions. The second objective was to find the relationship of PTMs with the subcellular localization of leptospiral proteins. We have analyzed the PTM containing proteins identified in Triton X-114 fractions and used the iBAQ values and number of PTM containing peptides that correlate with the sub-cellular localization of leptospiral proteins.
HostingRepository	PRIDE
AnnounceDate	2022-08-12
AnnouncementXML	Submission_2022-08-12_00:31:48.983.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Madathiparambil G. Madanan
SpeciesList	scientific name: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130; NCBI TaxID: 267671;
ModificationList	phosphorylated residue; acetylated residue; deamidated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-12-13 09:50:54	ID requested
⏵ 1	2022-08-12 00:31:49	announced

Phukan H, Sarma A, Rex DAB, Rai AB, Prasad TSK, Madanan MG, . ACS Omega, 7(22):18569-18576(2022) [pubmed]

submitter keyword: Leptospira

protein modification

drug target

diagnosis

mass spectrometry

proteome discoverer

Madathiparambil G. Madanan
contact affiliation	Dr Madathiparambil G. Madanan, Scientist E, Indian Council of Medical Research, Regional Medical Research Centre, Dollygunj, Port Blair - 744 103, Andaman & Nicobar Islands,INDIA. Phone: Office: +91-3192-251158 Cell: +91-9434284576 (lab head)
contact email	madananmg@icmr.org.in
lab head
Madathiparambil G. Madanan
contact affiliation	Indian Council of Medical Research - Regional Medical Research Centre, Port Blair
contact email	madananmg@icmr.org.in
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/2022/08/PXD030370

PRIDE project URI

• PRIDE
  1. PXD030370
     1. Label: PRIDE project
     2. Name: Dissecting post-translational modifications in Leptospira proteome to elucidate novel insights into pathogen-host interaction using bioinformatics approach