PXD001217

PXD001217 is an original dataset announced via ProteomeXchange.

Title	Snake venom serine proteinases specificity mapping by proteomic identification of cleavage sites
Description	Serine proteinases have been shown to play the role of toxins in the venoms of many snakes. They act mainly on components of the coagulation cascade, and fibrinolytic and kallikrein-kinin systems to trigger various pathological effects observed in the envenomation. Despite showing high similarity in terms of primary structure snake venom serine proteinases (SVSPs) show exquisite specificity towards macromolecular substrates. Therefore, the characterization of their peptide bond specificity is important for understanding the active site preference associated with effective proteolysis as well as for the design of peptide substrates and inhibitors. Bothrops jararaca contains various SVSPs among which Bothrops protease A (BPA) is a specific fibrinogenolytic agent and PA-BJ is a platelet-activating enzyme. In this study we used proteome derived peptide libraries in the Proteomic Identification of protease Cleavage Sites (PICS) approach to explore the peptide bond specificity of BPA and PA-BJ in order to determine their individual peptide cleavage sequences. A total of 371 cleavage sites (208 for BPA and 163 for PA-BJ) were detected and both proteinases displayed a clear preference for arginine at the P1 position. Moreover, the analysis of the specificity profiles of BPA and PA-BJ revealed subtle differences in the preferences along P6-P6’, despite a common preference for Pro at P2. Taken together, these results illustrate the subsite specificity of both SVSPs and shed light in the functional differences between these proteinases.
HostingRepository	PRIDE
AnnounceDate	2014-10-30
AnnouncementXML	Submission_2015-06-01_06:19:31.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Andre Zelanis
SpeciesList	scientific name: Bothrops jararaca (Jararaca) (Bothrops jajaraca); NCBI TaxID: 8724;
ModificationList	biotinylated residue; iodoacetamide derivatized residue; thioacylation of primary amines - site N-term; dimethylated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2014-08-11 01:21:20	ID requested
1	2014-10-30 01:29:20	announced
⏵ 2	2015-06-01 06:19:32	announced	Updated publication reference for PubMed record(s): 25452133.

Zelanis A, Huesgen PF, Oliveira AK, Tashima AK, Serrano SM, Overall CM, Snake venom serine proteinases specificity mapping by proteomic identification of cleavage sites. J Proteomics, 113():260-7(2015) [pubmed]

curator keyword: Biological

submitter keyword: snake venom, proteinase, serine proteinase, mass spectrometry, pProteomic Identification of protease Cleavage Sites

Solange M. T. Serrano
contact affiliation	Laboratório Especial de Toxinologia Aplicada Instituto Butantan Av. Vital Brasil 1500, 05503-000, São Paulo, Brazil Tel 55 11 2627 9732 Fax 55 11 3726 1024
contact email	solange.serrano@butantan.gov.br
lab head
Andre Zelanis
contact affiliation	Instituto de Ciencia e Tecnologia, Universidade Federal de Sao Paulo, Sao Jose dos Campos-SP, Brazil
contact email	zelanis@gmail.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/2014/10/PXD001217

PRIDE project URI

• PRIDE
  1. PXD001217
     1. Label: PRIDE project
     2. Name: Snake venom serine proteinases specificity mapping by proteomic identification of cleavage sites