PXD012088 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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 |
Dataset History
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. |
Publication List
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] |
Keyword List
submitter keyword: Snake venom, mass spectrometry, enzymes, proteome |
Contact List
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 | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD012088
- Label: PRIDE project
- Name: Comparative analysis of high molecular mass subproteomes of Bothrops snake venoms