Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Scolopendra viridis venom MS - Venom-gland transcriptomics and venom proteomics of the giant Florida blue centipede, Scolopendra viridis

ABSTRACT: MS analysis of tryptic digests of whole venoms from two individual of the centipede Scolopendra viridis from Florida, USA.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Scolopendra Viridis

TISSUE(S): Venom Gland

SUBMITTER: Darin Rokyta

LAB HEAD: Darin R. Rokyta

PROVIDER: PXD009665 | Pride | 2018-07-26

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	02172016_MW23_CV0559_Run1.mzid.gz	Mzid
	02172016_MW23_CV0559_Run1.mzid_02172016_MW23_CV0559_Run1.MGF	Mzid
	02172016_MW23_CV0559_Run1.mzid_02172016_MW23_CV0559_Run1.pride.mgf.gz	Mzid
	02172016_MW23_CV0559_Run1.pride.mztab.gz	Mztab
	02172016_MW23_CV0559_Run1.raw	Raw

Items per page:

1 - 5 of 30

Publications

Venom-gland transcriptomics and venom proteomics of the giant Florida blue centipede, Scolopendra viridis.

Ward Micaiah J MJ Rokyta Darin R DR

Toxicon : official journal of the International Society on Toxinology 20180804

The limited number of centipede venom characterizations have revealed a rich diversity of toxins, and recent work has suggested centipede toxins may be more rapidly diversifying than previously considered. Additionally, many identified challenges in venomics research, including assembly and annotation methods, toxin quantification, and the ability to provide biological or technical replicates, have yet to be addressed in centipede venom characterizations. We performed high-throughput, quantifiab ...[more]

PMID: 30086358

Similar Datasets

Hemiscolopendra marginata venom MS

Project description:MS analysis of tryptic digests of whole venoms from two individual of the centipede Hemiscolopendra marginata from Florida, USA.

2019-08-27 | PXD011712 | Pride

Scolopendromorpha venom Mass Spectrometry

Project description:MS analysis of tryptic digests of whole venoms from 26 individuals of the centipede order Scolopendromorpha from the United States.

2024-07-25 | PXD048308 | Pride

Centruroides henzti venom - Venom-gland transcriptomics and venom proteomics of the Hentz striped scorpion (Centruroides hentzi; Buthidae) reveal high toxin diversity in a harmless member of a lethal family

Project description:Venom proteomics for the scorpion Centruroides hentzi

2017-12-19 | PXD007788 | Pride

Hadrurus spadix venom - Venom-gland transcriptomics and venom proteomics of the black-back scorpion (Hadrurus spadix) reveal detectability challenges and an unexplored realm of animal toxin diversity

Project description:We used a combined transcriptomic and proteomic approach to characterize the venom of a male and female of the black-back scorpion (Hadrurus spadix).

2017-01-30 | PXD005009 | Pride

Scolopocryptops sexspinosus venom MS

Project description:MS analysis of tryptic digests of whole venoms from two individual of the centipede Scolopecryptops sexspinosus from Florida, USA.

2019-06-26 | PXD011714 | Pride

De Novo Transcriptome Sequencing for Tetramorium bicarinatum: The first comprehensive venom gland transcriptome analysis from an ant species.

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

Naja ashei venom fractionation using IEX chromatography

Project description:Identification of protein composition of Naja ashei fractions obtained using IEX chromatography

2020-01-21 | PXD015814 | Pride

Proteomic analysis of Heloderma horridum horridum venom

Project description:Heloderma horridum horridum commonly known as the scorpion lizard, Mexican scorpion, and beaded lizard, is a venomous reptile native of America. The venom derived from this lizard has potential applications, particularly in treatment of type II diabetes through the peptide Exendin. In this work, H. h. horridum venom was extracted from adult specimens and lyophilized. To characterize the venom, enzymatic assays, including hyaluronidase, phospholipase A2, and proteolytic activity were conducted. A proteomic analysis of the venom was also performed employing bottom-up/shotgun approaches from SDS-PAGE and High pH Reversed-Phase chromatography., besides fractionation of tryptic peptides using a nano-LC-MS/MS. These approaches involved massive sequencing to enhancing the likelihood of detecting an extensive range of venom proteins. The proteins and peptides found in H. h. horridum venom are reviewed according to the classification of the transcriptome previously reported.

2024-08-10 | PXD052417 | Pride

Qualitative and quantitative analysis of Bothrops jararaca venom gland proteome

Project description:While cellular transcripts encode rich information that provide key features to understand the molecular basis of snake venom variation, their presence/ abundance does not necessary imply/correlate in the translation of a functional (protein) product. In this study we carried out an analysis of the venom gland proteome of Bothrops jararaca taking into account two distinct phases of its ontogenetic development (i.e. newborn and adult specimens) and the marked sexual dimorphism recently reported on its venom proteome. Proteomic data analysis showed wider dynamic range for toxins when comparing to non-toxins and a dynamic proteome rearrangement in cellular proteins upon B. jararaca development. Differentially expressed proteins covered a number of biological pathways related to protein synthesis, including proteins related to transcription and translation, which were found to be significantly higher expressed in the newborn venom gland. Our results showed that the variation in the expression levels of cellular proteins gives rise to an even higher variation in the dynamic range of the expressed toxins. Upon ageing, the molecular constraints related to protein synthesis together with ecological traits would likely have an impact on the toxin repertoire, which, in the case of B. jararaca species, would enable the species to deal with different prey types during its lifespan.

2016-09-28 | PXD004186 | Pride

Snake Venom LC/MSE - Post-transcriptional Mechanisms Contribute Little to Phenotypic Variation in Snake Venoms

Project description:Protein expression is a major link in the genotype-phenotype relationship, and processes affecting protein abundances, such as rates of transcription and translation, could contribute to phenotypic evolution if they generate heritable variation. Recent work has suggested that mRNA abundances do not accurately predict final protein abundances, which would imply that post-transcriptional regulatory processes contribute significantly to phenotypes. Post-transcriptional processes also appear to buffer changes in transcriptional patterns as species diverge, suggesting that the transcriptional changes have little or no effect on the phenotypes under study. We tested for concordance between mRNA and protein expression levels in snake venoms by means of mRNA-seq and quantitative mass spectrometry for 11 snakes representing 10 species, six genera, and three families. In contrast to most previous work, we found high correlations between venom-gland transcriptomes and venom proteomes for ten of our 11 comparisons. We tested for protein-level buffering of transcriptional changes during species divergence by comparing the difference between transcript abundance and protein abundance for three pairs of species and one intraspecific pair. We found no evidence for buffering during divergence of our three species pairs but did find evidence for protein-level buffering for our single intraspecific comparison, suggesting that buffering, if present, was a transient phenomenon in venom divergence. Our results demonstrated that post-transcriptional mechanisms did not contribute significantly to phenotypic evolution in venoms and suggest a more prominent and direct role for cis-regulatory evolution in phenotypic variation, particularly for snake venoms.

2015-11-09 | PXD002837 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data