Vipera anatolica
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA560445 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR9990312_1.fastq.gz | Fastqsanger.gz | |||
| SRR9990312_2.fastq.gz | Fastqsanger.gz |
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Project description:Snake venom is a rich source of peptides and proteins with a wide range of actions. Many of the components of the venom are currently being tested for their usefulness in the treatment of many diseases ranging from neurological and cardiovascular to cancer. It is also important to constantly search for new proteins and peptides with properties not yet described. The venom of Vipera berus berus has hemolytic, proteolytic and cytotoxic properties, but its exact composition and the factors responsible for these properties are not known. Therefore, an attempt was made to identify proteins and peptides derived from this species venom by using high resolution two-dimensional electrophoresis and MALDI ToF/ToF mass spectrometry. A total of 11 protein classes have been identified mainly proteases but also L-amino acid oxidases, C-type lectin like proteins, cysteine-rich venom proteins and phospholipases A2 and 5 peptides of molecular weight less than 1500 Da. Most of the identified proteins are responsible for the highly hemotoxic properties of the venom. Presence of venom phospholipases A2 and L- amino acid oxidases cause moderate neuro-, myo- and cytotoxicity. All successfully identified peptides belong to the bradikinin-potentiating peptides family.
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Project description:We report the venom proteome of Vipera anatolica senliki, a newly discovered subspecies of the Anatolian Meadow viper endemic to the Antalya Province in Turkey. Integrative venomics, including venom gland transcriptomics as well as complementary bottom-up and top-down proteomic analyses, were applied to fully characterize the venom of V. a. senliki. Additionally, we extend the top-down venomics approach to elucidate the venom proteome by an in-source decay-driven (ISD) workflow using the reducing matrix 1,5-diaminonaphthalene (DAN). Our venomic in-source decay protocol allowed disulfide bond mapping as well as an effective de novo identification of high molecular weight venom constituents, both of which are difficult to achieve by established top-down approaches. Venom gland transcriptome analysis identified 42 venom genes annotations relating to number 13 venom toxin families. Relative quantitative snake venomics revealed snake venom metalloproteinases (svMP, 42.9%) as most abundant protein family, followed by less abundant toxin families as cysteine-rich secretory proteins (CRISP, 9.9%), phospholipases A2 (PLA2, 8.2%), snake venom serine proteinases (svSP, 7.2%) and C-type lectin-like proteins(CTL, 4.6%) as well as disintegrins (DI, 1.9%), Kunitz-type serine protease inhibitor (KUN, 1.2%), L-amino acid oxidase (LAAO, 0.1%) and non-annotated (n/a, 0.5%) were identified. Furthermore, a high content of diverse peptides (23.5%), e.g. svMP-inhibitor (svMP-i, 5.9%) and bradykinin potentiating peptides (BPP; 0.6%) were found. Top-down venomics showed the presence of DI, KUN, and several PLA2 proteoforms that were also previously reported in the closely related subspecies V. anatolica anatolica.
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