PXD012088

PXD012088 is an original dataset announced via ProteomeXchange.

Title	Comparative analysis of high molecular mass subproteomes of Bothrops snake venoms
Description	Snake venoms are extremely active biological secretions containing primarily various classes of enzymes. The genus Bothrops comprises various pit viper species that represent the most medically significant taxa in Central and South America, accounting for more human envenomations and fatalities than any other snake taxa. Venom proteomes of many Bothrops species have been characterized but, although proteins of molecular mass higher than 100 kDa have been documented in Bothrops venoms, these large proteins have not yet been closely investigated. This study sought to achieve detailed identification of major components in the high molecular mass subproteome of venoms from eight Bothrops species (B. brazili, B. cotiara, B. insularis, B. jararaca, B. jararacussu, B. leucurus, B. moojeni and B. neuwiedi). The identification of proteins eluting in the first fractions of a size-exclusion chromatography of these venoms revealed that they are comprised mainly of enzymes, including minor components such as 5'-nucleotidase, aminopeptidase, phosphodiesterase, and phospholipases A2 and B, but with metalloproteinases and L-amino acid oxidases representing the most abundant components. Most of these components disappeared in electrophoretic profiles under reducing conditions suggesting that they may be composed of more than one polypeptide chain. A significant shift in the molecular masses of these protein bands was observed after enzymatic N-deglycosylation, indicating that they may contain N-glycans. Furthermore, the finding that none of the high molecular mass proteins is shared by all eight species reveals a high level of interspecies venom variability among these components.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:00:43.048.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Solange Serrrano
SpeciesList	scientific name: Bothrops jararacussu; NCBI TaxID: 8726; scientific name: Bothrops moojeni; NCBI TaxID: 98334; scientific name: Bothrops jararaca (Jararaca) (Bothrops jajaraca); NCBI TaxID: 8724; scientific name: Bothrops cotiara; NCBI TaxID: 8727; scientific name: Acyrthosiphon pisum (Pea aphid); NCBI TaxID: 7029; scientific name: Bothrops neuwiedi; NCBI TaxID: 95648; scientific name: Bothrops leucurus; NCBI TaxID: 157295; scientific name: Bothrops brazili; NCBI TaxID: 157546; scientific name: Bothrops insularis; NCBI TaxID: 8723;
ModificationList	No PTMs are included in the dataset
Instrument	LTQ Orbitrap Velos; Q-Tof Ultima

Revision	Datetime	Status	ChangeLog Entry
0	2018-12-17 07:14:48	ID requested
1	2019-03-05 00:52:11	announced
⏵ 2	2024-10-22 04:00:43	announced	2024-10-22: Updated project metadata.

10.1016/j.cbd.2019.01.012;

Gren ECK, Kitano ES, Andrade-Silva D, Iwai LK, Reis MS, Menezes MC, Serrano SMT, Comparative analysis of the high molecular mass subproteomes of eight Bothrops snake venoms. Comp Biochem Physiol Part D Genomics Proteomics, 30():113-121(2019) [pubmed]

submitter keyword: Snake venom, mass spectrometry, enzymes, proteome

Solange Maria de Toledo Serrano
contact affiliation	Butantan Institute
contact email	solange.serrano@butantan.gov.br
lab head
Solange Serrrano
contact affiliation	Butantan Institute
contact email	solange.serrano@butantan.gov.br
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/2019/03/PXD012088

PRIDE project URI

• PRIDE
  1. PXD012088
     1. Label: PRIDE project
     2. Name: Comparative analysis of high molecular mass subproteomes of Bothrops snake venoms