Trimeresurus trigonocephalus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1198950 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR31742165_1.fastq.gz | Fastqsanger.gz | |||
| SRR31742165_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 2 of 2 |
Similar Datasets
Project description:Trimeresurus albolabris Genome sequencing and assembly
| PRJNA947331 | ENA
Project description:This project mainly aims to characterize the complex toxic components present in the venom of Trimeresurus malabaricus (Malabar pit viper). Since Trimeresurus malabaricus (Malabar pit viper) species are mainly inhabited to plantation crop areas, its envenomation is a serious threat to the human population thriving in these zones, especially to the plantation workers. Therefore, exploring the venom proteome of Malabar pit viper is decisive to develop and design new antivenom and therapeutics against its envenomation. As described in this study, applying various orthogonal separation strategies helped in dissecting venom constituents of Trimeresurus malabaricus and is the first comprehensive attempt in revealing the complex venom profile of Malabar pit viper through proteomics approaches incorporating multiple database searches. In order to achieve this the crude venom components were resolved on a 12% SDS page. Further each of the bands were subjected to in-gel trypsin digestion. The crude venom was also subjected to ion-exchange chromatography separation. The obtained fractions were subjected to in-solution trypsin digestion. All the digested peptides were then subjected to Q-TOF LC-MS/MS analysis.
2020-01-24 | PXD011673 | Pride
Project description:RADseq loci of mangrove pit vipers of the Trimeresurus purpureomaculatus complex
| PRJNA935910 | ENA
Project description:BackgroundThe venom of bamboo vipers (Trimeresurus stejnegeri - TS), commonly found in Taiwan, contains deadly hemotoxins that cause severe envenomation. Equine-derived antivenom is a specific treatment against snakebites, but its production costs are high and there are some inevitable side effects. The aim of the present work is to help in the development of an affordable and more endurable therapeutic strategy for snakebites.MethodsT. stejnegeri venom proteins were inactivated by glutaraldehyde in order to immunize hens for polyclonal immunoglobulin (IgY) antibodies production. After IgY binding assays, two antibody libraries were constructed expressing single-chain variable fragment (scFv) antibodies joined by the short or long linker for use in phage display antibody technology. Four rounds of biopanning were carried out. The selected scFv antibodies were then further tested for their binding activities and neutralization assays to TS proteins.ResultsPurified IgY from egg yolk showed the specific binding ability to TS proteins. The dimensions of these two libraries contain 2.4 × 107 and 6.8 × 107 antibody clones, respectively. An increase in the titers of eluted phage indicated anti-TS clones remarkably enriched after 2nd panning. The analysis based on the nucleotide sequences of selected scFv clones indicated that seven groups of short linkers and four groups of long linkers were identified. The recombinant scFvs showed significant reactivity to TS venom proteins and a cross-reaction to Trimeresurus mucrosquamatus venom proteins. In in vivo studies, the data demonstrated that anti-TS IgY provided 100% protective effects while combined scFvs augmented partial survival time of mice injected with a lethal amount of TS proteins.ConclusionChickens were excellent hosts for the production of neutralization antibodies at low cost. Phage display technology is available for generation of monoclonal antibodies against snake venom proteins. These antibodies could be applied in the development of diagnostic kits or as an alternative for snakebite envenomation treatment in the near future.
| S-EPMC7682652 | biostudies-literature
Project description:The two venomous pit vipers, Trimeresurus macrops and T. hageni, are distributed throughout Thailand, although their abundance varies among different areas. No species-specific antivenom is available for their bite victims, and the only recorded treatment method is a horse antivenom raised against T. albolabris crude venom. To facilitate assessment of the cross-reactivity of heterologous antivenoms, protein profiles of T. macrops and T. hageni venoms were explored using mass-spectrometry-based proteomics. The results show that 185 and 216 proteins were identified from T. macrops and T. hageni venoms, respectively. Two major protein components in T. macrops and T. hageni venoms were snake venom serine protease and metalloproteinase. The toxicity of the venoms on human monocytes and skin fibroblasts was analyzed, and both showed a greater cytotoxic effect on fibroblasts than monocytic cells, with toxicity occurring in a dose-dependent rather than a time-dependent manner. Exploring the protein composition of snake venom leads to a better understanding of the envenoming of prey. Moreover, knowledge of pit viper venomics facilitates the selection of the optimum heterologous antivenoms for treating bite victims.
| S-EPMC7020458 | biostudies-literature
Project description:Trimeresurus albolabris, also known as the white-lipped pit viper or white-lipped tree viper, is a highly venomous snake distributed across Southeast Asia and the cause of many snakebite cases. In this study, we report the first whole genome assembly of T. albolabris obtained with next-generation sequencing from a specimen collected in Mengzi, Yunnan, China. After genome sequencing and assembly, the genome of this male T. albolabris individual was 1.51 Gb in length and included 38.42% repeat-element content. Using this genome, 21,695 genes were identified, and 99.17% of genes could be annotated using gene functional databases. Our genome assembly and annotation process was validated using a phylogenetic tree, which included six species and focused on single-copy genes of nuclear genomes. This research will contribute to future studies on Trimeresurus biology and the genetic basis of snake venom.
| S-EPMC10836062 | biostudies-literature