PXD009050

PXD009050 is an original dataset announced via ProteomeXchange.

Title	Proteomic approach and expression analysis revealed the differential expression of leptospiral proteases capable of ECM degradation
Description	Leptospira, the causative agent of leptospirosis is known to have several proteases with potential to degrade extracellular matrix. However, a multipronged approach to identify, classify, characterize and elucidate their role has not been attempted. In this study, we carried out in-depth proteomic analysis of Triton X-114 fractions of Leptospira interrogans using high-resolution LC-MS/MS. Our analysis resulted in the identification of 104 of 130 proteases predicted by MEROPS. Approximately 3.5% of the Leptospira genome complements for proteases, which include catalytic types of metallo-, serine-, cysteine-, aspartic-, threonine- and asparagine- peptidases. Comparison of proteases from different serovars revealed that M04, M09B, M14A, M75, M28A, A01 and U73 protease families are exclusively present in pathogenic form. The M23 and S33 protease families are represented with more than 14 members in Leptospira. In silico prediction and characterization of the proteases revealed that several proteases are membrane anchored and secretory, classical as well as non-classical system. This study demonstrates the diversity and complexity of proteases, while maintaining conservation across the serovars in Leptospira and their differential expression under pathogenic conditions.
HostingRepository	PRIDE
AnnounceDate	2020-09-01
AnnouncementXML	Submission_2020-09-01_04:41:53.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	M. G. Madanan
SpeciesList	scientific name: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130; NCBI TaxID: 267671;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2018-02-27 05:07:00	ID requested
1	2018-04-18 01:52:48	announced
⏵ 2	2020-09-01 04:41:54	announced	2020-09-01: Updated publication reference for PubMed record(s): 29654978, 32846045.

Thoduvayil S, Dhandapani G, Brahma R, Devasahayam Arokia Balaya R, Mangalaparthi KK, Patel K, Kumar M, Tennyson J, Satheeshkumar PK, Kulkarni MJ, Pinto SM, Prasad TSK, Madanan MG, Triton X-114 Fractionated Subcellular Proteome of Leptospira interrogans Shows Selective Enrichment of Pathogenic and Outer Membrane Proteins in the Detergent Fraction. Proteomics, 20(19-20):e2000170(2020) [pubmed]

Dhandapani G, Sikha T, Pinto SM, Kiran Kumar M, Patel K, Kumar M, Kumar V, Tennyson J, Satheeshkumar PK, Gowda H, Keshava Prasad TS, Madanan MG, Proteomic approach and expression analysis revealed the differential expression of predicted leptospiral proteases capable of ECM degradation. Biochim Biophys Acta Proteins Proteom, 1866(5-6):712-721(2018) [pubmed]

curator keyword: Biological

submitter keyword: Leptospira, protease, pathogenesis, metalloprotease, high resolution proteomics

M. G. Madanan
contact affiliation	Regional Medical Research Centre, Indian Council of Medical Research, Port Blair, India
contact email	madananmg@icmr.org.in
lab head
M. G. Madanan
contact affiliation	Regional Medical Research Centre, Indian Council of Medical Research
contact email	madananmg@icmr.org.in
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD009050
     1. Label: PRIDE project
     2. Name: Proteomic approach and expression analysis revealed the differential expression of leptospiral proteases capable of ECM degradation