PXD012585

PXD012585 is an original dataset announced via ProteomeXchange.

Title	Comparative proteomics and biochemical analysis of venom of thirteen Bothrops moojeni specimens reveal several individual variations
Description	Snake venoms are complex protein mixtures with different biological activities that can act in both their preys and human victims. Many of these proteins play a role in prey capture and in the digestive process of these animals. It is known that some snakes are resistant to the toxicity of their own venom by mechanisms not yet fully elucidated. However, it was observed in the Laboratory of Herpetology of Instituto Butantan that some Bothrops moojeni individuals injured by the same snake species showed mortalities caused by envenoming effects. This study analyzed the biochemical composition of 13 venom and plasma samples from Bothrops moojeni specimens to assess differences in their protein composition. Application of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed distinct venom protein profiles, but very homogeneous plasma profiles. Western Blotting (WB) was performed with plasma samples, which were submitted to incubation with the respective venom. Some individuals showed an immunorecognized band zone around 25 kDa, indicating interaction between the same individual plasma and venom proteins. Crossed-WB assay using non-self-plasma and venom showed that this variability is due to venom protein composition instead of plasma composition. These venoms presented higher caseinolytic, collagenolytic and coagulant activities than the venoms without these regions recognized by WB. Mass spectrometry analysis revealed that these individuals present, in addition to higher protein concentrations, other exclusive proteins in their composition. When these samples were tested in vivo, the results also showed higher lethality in these venoms, but lower hemorrhagic activity than in the venoms without these regions recognized by WB. In conclusion, some Bothrops moojeni specimens differ in venom composition, which may have implications in envenomation. Moreover, the high individual venom variability found in this species demonstrates the importance to work with individual analysis in studies involving intraspecific venom variability and venom evolution.
HostingRepository	PRIDE
AnnounceDate	2019-09-26
AnnouncementXML	Submission_2019-09-25_22:58:40.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alexandre Keiji Tashima
SpeciesList	scientific name: Bothrops moojeni; NCBI TaxID: 98334;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2019-02-01 01:46:48	ID requested
⏵ 1	2019-09-25 22:59:50	announced

Aguiar WDS, Galizio NDC, Serino-Silva C, Sant'Anna SS, Grego KF, Tashima AK, Nishiduka ES, Morais-Zani K, Tanaka-Azevedo AM, Comparative compositional and functional analyses of Bothrops moojeni specimens reveal several individual variations. PLoS One, 14(9):e0222206(2019) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Bothrops moojeni

snake venom

envenomation

intraspecific venom variability

snake plasma

Alexandre Keiji Tashima
contact affiliation	Escola Paulista de Medicina/UNIFESP
contact email	aktashima@unifesp.br
lab head
Alexandre Keiji Tashima
contact affiliation	Universidade Federal de Sao Paulo
contact email	aktashima@unifesp.br
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD012585
     1. Label: PRIDE project
     2. Name: Comparative proteomics and biochemical analysis of venom of thirteen Bothrops moojeni specimens reveal several individual variations