Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1040254 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR26825348_1.fastq.gz | Fastqsanger.gz | |||
| SRR26825348_2.fastq.gz | Fastqsanger.gz | |||
| SRR26825349_1.fastq.gz | Fastqsanger.gz | |||
| SRR26825349_2.fastq.gz | Fastqsanger.gz | |||
| SRR26825350_1.fastq.gz | Fastqsanger.gz |
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Project description:Elucidating the molecular mechanisms underlying snake venom variability provides important clues for understanding how the biological functions of this powerful toxic arsenal evolve. We analyzed in detail individual transcripts and venom protein isoforms produced by five specimens of a venomous snake (Bothrops atrox) from two nearby but genetically distinct populations from the Brazilian Amazon rainforest which show functional similarities in venom properties. Individual variation was observed among the venoms of these specimens, but the overall abundance of each general toxin family was conserved both in transcript and in venom protein levels. However, when expression of independent paralogues was analyzed, remarkable differences were observed within and among each toxin group, both between individuals and between populations. Transcripts for functionally essential venom proteins (“core function” proteins) were highly expressed in all specimens and showed similar transcription/translation rates. In contrast, other paralogues (“adaptive” proteins) showed lower expression levels and the toxins they coded for varied among different individuals. These results provide support for the inferences that (a) expression and translational differences play a greater role in defining adaptive variation in venom phenotypes than does sequence variation in protein coding genes and (b) convergent adaptive venom phenotypes can be generated through different molecular mechanisms. Significance: Analysis of individual transcripts and venom protein isoforms produced by specimens of a venomous snake (Bothrops atrox), from the Brazilian Amazon rainforest, revealed that transcriptional and translational mechanisms contribute to venom phenotypic variation. Our finding of evidence for high expression of toxin proteins with conserved function supports the hypothesis that the venom phenotype consists of two kinds of proteins: conserved “core function” proteins that provide essential functional activities with broader relevance and less conserved “adaptive” proteins that vary in expression and may permit customization of protein function. These observations allowed us to suggest that genetic mechanisms controlling venom variability are not restricted to selection of gene copies or mutations in structural genes but also to selection of the mechanisms controlling gene expression, contributing to the plasticity of this important phenotype for venomous snakes.
2023-07-04 | PXD043541 | Pride
Project description:Venoms are ecological innovations that have evolved numerous times, on each occasion accompanied by the co-evolution of specialised morphological and behavioural characters for venom production and delivery. The close evolutionary interdependence between these characters is exemplified by animals that control the composition of their secreted venom. This ability depends in part on the production of different toxins in different locations of the venom gland, which was recently documented in venomous snakes. Here, we test the hypothesis that the distinct spatial distributions of toxins in snake venom glands is an adaptation that enables the secretion of venoms with distinct ecological functions.
2022-06-10 | PXD034174 | Pride
Project description:Snake venoms have evolved in a few families of Caenophidae, and their toxins have been fine-tuned over the evolutive process into highly effective biochemical weapons with a particular role as a trophic adaptation. However, there are many outstanding questions on how venom contributes to the success of venomous species and their adaptation to different environments. Here we analyze the venoms from sympatric and generalist specimens of B. hyoprora, B. taeniatus, B. b. smaragdinus, B. brazili, and B. atrox collected in the wild of Alto Juruá region at the Amazon Forest aiming to understand whether the venom composition could be a driver or influence the arboreal habitats of B. taeniatus and B. b. smaragdinus, or the successful dispersion of B. atrox across the Amazon Forest. Venom composition and the primary sequences of toxin isoforms were characterized by venom gland transcriptomics followed by proteomics. The venom composition of the five species conserved the same protein families present in venoms of Bothropoid snakes but with remarkable differences in the chromatographic profiles and in the relative amount of each toxin group: CTLs were the most abundant in the venoms of B. taeniatus (31.6%), B. b. smaragdinus (33.0%), and B. atrox (32.0%) and SVMPs and PLA2s dominated in venoms of B. hyoprora (23.7% and 20.2%) and B. brazili (20.2% and 20.4%). Some peculiarities were also observed: B. hyoprora venom was the least complex, conserving important isoforms shared with B. atrox venom; the presence of one cluster of SVSPs exclusive to B. brazili venom isoforms; and the presence of the K49-PLA2 homologs only in B. b. smaragdinus and particularly in B. brazili venoms. The SVMP, SVSP, and PLA2 enzyme activities were consistent with the abundance and type of isoforms present in the venoms. B. hyoprora, B. taeniatus, B. b. smaragdinus, and B. atrox venoms presented low lethality to small rodents, while B. brazili venom was the most lethal. Concluding, differences were evidenced between the venoms of B. taeniatus and B. b. smaragdinus arboreal species, while B. b. smaragdinus shared a venom with a similar composition to B. atrox venom, mostly terrestrial. Considering the role of venom toxicity in species' success for adaptation in different areas, B. atrox is the most adapted in the whole Amazonian territory and presented the least lethal venom, while the venom of B. brazili was the most lethal despite its small distribution in the same area. Therefore, our data suggest that the selection of venom composition may not influence the success or behavior of snake species. In this way, other biotic or abiotic factors influence their foraging status or their dispersal in different ecological niches.
2024-05-24 | PXD046872 | Pride
Project description:Background: Bothrops atrox is known to be the pitviper responsible for most snakebites and human fatalities in the Amazon region. It can be found in a wide geographical area including the northern South America, the east of Andes and the Amazon basin. Possibly due to its wide distribution range and generalist feeding, intraspecific venom variation was reported by previous proteomics studies. Sex-based and ontogenetic variations on venom compositions of Bothrops snakes were also subject of proteomic and peptidomic analysis. However, the venom peptidome of B. atrox remains unknown. Methods: we conducted a mass spectrometry-based analysis of the venom peptides of individual male and female specimens combining bottom-up and top-down approaches. Results: We identified in B. atrox a total of 105 native peptides in the mass range of 0.4 to 13.9 kDa. Quantitative analysis showed that Phospholipase A2 and Bradykinin Potentiating Peptides were the most abundant peptide families in both genders, but the disintegrins levels were significantly increased in the venoms of females. Known peptides processed at non-canonical sites and new peptides were also revealed in this work. Conclusion: The venom peptidomes of male and female specimens of B. atrox were analyzed by mass spectrometry-based approaches in this work. The study points to differences in the disintegrin levels in the venoms of females that may result in distinct pathophysiology in envenomation. Further research is needed to explore its biological implications.
2020-10-13 | PXD018632 | Pride
Project description:Snakebite is a major public health concern in many parts of the world, including India, where over 58,000 deaths occur annually due to this highly neglected tropical disease. The common krait (Bungarus caeruleus), one of the ‘big four’ Indian snakes, is responsible for the second-highest number of snakebite-related deaths in the country. The venom protein composition of common krait venoms from different locations were investigated. Venoms were pre-fractionated using RP-HPLC and SDS-PAGE, and subjected to mass spectromentry analysis. The relative abundance of each toxin family was estimated and compared across different locations.
2024-11-02 | PXD052611 | Pride
Project description:The socioeconomic burden of snakebite in India is largely attributed to the ‘big four’ snakes, completely neglecting the considerable impact of envenoming by many other snake species. Bites from the so-called ‘neglected many’ are often treated with a polyvalent antivenom that is manufactured against the ‘big four’ snakes - a strategy that has been widely documented to fail. Yet, specific antivenoms are not commercially manufactured against these snakes. While the medical importance of various species of cobras, saw-scaled vipers, and kraits is very well-known, the clinical impact of pit vipers from the rainforests of the Western Ghats, northeastern India, and Andaman and Nicobar islands has remained elusive. Amongst the 90+ species of snakes found in the Western Ghats, the hump-nosed (Hypnale hypnale), Malabar (Craspedocephalus malabaricus) and bamboo (Craspedocephalus gramineus) pit vipers can potentially inflict clinically severe envenoming in humans. To evaluate the severity of toxicity inflicted by these snakes, we characterised their venom composition, biochemical and pharmacological activities, and toxicity- and morbidity-inducing potentials. Our findings highlight the therapeutic inadequacies of the generic Indian and Hypnale-specific Sri Lankan polyvalent antivenoms in neutralising morbidity and mortality resulting from pit viper envenomings and underscore the need for a regional antivenom therapy in India.
2023-07-20 | PXD039139 | 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 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.
2019-09-26 | PXD012585 | 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).
2015-01-08 | GSE53988 | GEO
Project description:True cobras of the genus Naja are venomous snakes with particular medical importance in Africa and Asia. The Cape cobra Naja nivea is one of the most toxic of the African true cobras, but the composition of its venom has rarely been investigated using proteomics methods.
2024-10-08 | PXD036965 | Pride