Vipera aspis
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA594707 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Vipera kaznakovi venom gland raw sequence reads
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Project description:Vipera anatolica senliki Venom Gland Transcriptome and Assembly
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Project description:The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes (Vaa) in particular is, medically, the most relevant snake in Europe. The local and systemic clinical manifestations of poisoning by the venom of this snake are the result of the pathophysiological effects inflicted by enzymatic and non-enzymatic venom components acting, most prominently, on blood, cardiovascular and nerve systems. This venom comprises the most complex mixture of pharmacologically active proteins and peptides of all European snakes. To help improve the current antivenom therapy towards higher specificity and efficiency, and to assist drug discovery, we have constructed, by combining transcriptomic and proteomic analyses, the most comprehensive library yet of the Vaa venom proteins and peptides. At the protein level, 57 venom proteins belonging to 16 different protein families have been identified and, with SVSPs, sPLA2s, snaclecs and SVMPs, comprise about 80% of all venom proteins.
2019-05-06 | PXD012752 | Pride
Project description:In order to provide a global insight on the transcripts expressed in the venom gland of the Brazilian ant species Tetramorium bicarinatum and to unveil the potential of its products, high-throughput expressed sequence tags were generated using Illumina paired-end sequencing technology. A total of 212,371,758 pairs of quality-filtered, 100-base-pair Illumina reads were obtained. The de novo assemblies yielded 36,042 contigs for which 27,873 have at least one predicted ORF among which 59.77% produce significant hits in the available databases. The investigation of the reads mapping toxin class revealed a high diversification with the major part consistent with the classical hymenopteran venom protein signature represented by venom allergen (33.3%) followed by a diverse toxin-expression profile including several distinct isoforms of phospholipase A1 and A2, venom serine protease, hyaluronidase, protease inhibitor and secapin. Moreover, our results revealed for the first time the presence of toxin-like peptides that have been previously identified from unrelated venomous animals such as waprin-like (snakes) and agatoxins (spiders and conus). 300 ant specimens from the species Tetramorium bicarinatum were dissected in order to extract the RNA from their venom gland, The whole ant body was used as a reference,
2015-01-08 | E-GEOD-53988 | biostudies-arrayexpress
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.
2016-12-12 | PXD004958 | Pride
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.
2019-07-29 | MSV000084147 | MassIVE
Project description:Combined bottom-up and top-down venom proteomics of a local population of Vipera kaznakovi.
2018-08-23 | MSV000082845 | MassIVE
Project description:Morus alba L. Raw protein sequence reads and sequence
2024-02-08 | PXD049451 | iProX