PXD016503 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Interrogating the higher order structures of snake venom proteins |
Description | Snake venoms contain complex mixtures of proteins that play vital roles in the survival of venomous snakes. In line with their diverse pharmacological activities, the protein compositions of snake venoms can be highly variable, and efforts to characterise the primary structures of such proteins are extensive and ongoing. In addition, a significant knowledge gap exists in terms of higher-order interactionsbetweenproteinsproposedto modulate venom potency, which poses a challenge for treatment of envenomation and development of successful therapeutic applications.Here we use a multifaceted mass spectrometrybased approach to characteriseproteinsfrom the medically significant venomsof Collett’s snake Pseudechis collettiand the puff adder Bitis arietans.Following chromatographic fractionation and bottom-up proteomics identification, native mass spectrometry identified, among other components, a 117 kDa non-covalent L-amino acid oxidase dimer in the P. collettivenom and a 60 kDa C-type lectin tetramer in the B. arietansvenom. Furthermore, a 27.7 kDa covalently-linked phospholipase A2(PLA2) dimer was identified in P. collettivenom, and thePLA2species were shownto adopt a highly compact geometry based on ion mobility measurements. Exploration of the catalytic efficiencies of the monomeric and dimeric forms of PLA2revealed that the dimeric PLA2 possessed greater bioactivity than the monomeric PLA2s.This work contributes to ongoing efforts to catalogue the protein components of snake venoms, and notably,itemphasises the importance of understanding higher-order protein interactions in venomsand the utility of a combined mass spectrometric approachfor this task. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:00:31.742.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Parul Mittal |
SpeciesList | scientific name: Vertebrata ; NCBI TaxID: 7742; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Synapt MS; LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-11-28 03:20:19 | ID requested | |
1 | 2020-02-17 14:23:59 | announced | |
⏵ 2 | 2024-10-22 05:00:32 | announced | 2024-10-22: Updated project metadata. |
Publication List
Wang CR, Bubner ER, Jovcevski B, Mittal P, Pukala TL, Interrogating the higher order structures of snake venom proteins using an integrated mass spectrometric approach. J Proteomics, 216():103680(2020) [pubmed] |
10.1016/j.jprot.2020.103680; |
Keyword List
submitter keyword: Snake venom, LC-MS/MS |
Contact List
Tara L. Pukala |
contact affiliation | Department of Chemistry, School of Physical SciencesUniversity of Adelaide, Adelaide Australia, 5005 |
contact email | tara.pukala@adelaide.edu.au |
lab head | |
Parul Mittal |
contact affiliation | Services & Facilities Officer, Adelaide Proteomic Centre |
contact email | parul.mittal@adelaide.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD016503
- Label: PRIDE project
- Name: Interrogating the higher order structures of snake venom proteins