Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Disclosing the venom peptidome of the Amazonian spider Acanthoscurria juruenicola

ABSTRACT: Acanthoscurria juruenicola is an Amazonian tarantula spider described for the first time a century ago. Specimens of both genders are similar in size and in most morphological aspects, but ecological behavior and their venom composition remained unknown to date. Here we present the peptidomics characterization of the spider venom by a combination of mass spectrometric analysis of both native and digested peptides, venom gland transcriptomics and bioinformatics. A total of 367 native features were observed in the venom peptidome. Seventeen cysteine-rich peptides were simultaneously observed in the transcriptome and in the mass spectrometric experiments, from which fourteen were completely sequenced in the mature forms. The mature peptides have 3-5 disulfide bonds and cover the 3.7-8.6 kDa mass range. Moreover, in vivo paralytic activities of the whole venom were observed in crickets. In silico analysis indicated that all mature peptides are potentially antimicrobial and two may be potential anticancer agents. The antimicrobial activity was experimentally confirmed for the peptide Ap1a against Micrococcus luteus, Pseudomonas aeruginosa and Candida albicans.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Acanthoscurria

TISSUE(S): Venom

SUBMITTER: Alexandre Keiji Tashima

LAB HEAD: Alexandre Keij Tashima

PROVIDER: PXD013149 | Pride | 2022-10-20

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Peptidomics of Acanthoscurria gomesiana spider venom reveals new toxins with potential antimicrobial activity

Project description:Acanthoscurria gomesiana is a Brazilian spider from the Theraphosidae family inhabiting regions of Southeastern Brazil. Potent antimicrobial peptides as gomesin and acanthoscurrin have been discovered from the spider hemolymph in previous works. Spider venoms are also recognized as sources of biologically active peptides, however the venom peptidome of A. gomesiana remained unexplored to date. In this work, a MS-based workflow was applied to the investigation of the spider venom peptidome. Data-independent and data-dependent LC-MS/MS acquisitions of intact peptides and of peptides submitted to multiple enzyme digestions, followed by automated chromatographic alignment, de novo analysis, database and homology searches with manual validations showed that the venom is composed by less than 165 features, with masses ranging from 0.4-15.8 kDa. A total of 135 peptides from 17 proteins were identified, including three new mature peptides: U1-TRTX-Agm1a, U1-TRTX-Agm2a and U1-TRTX-Agm3a, containing 3, 4 and 3 disulfide bonds, respectively. U1-TRTX-Agm1a differed by only one amino acid from U1-TRTX-Ap1a from A. paulensis and U1-TRTX-Agm2a was derived from the genicutoxin-D1 precursor from A. geniculata. These toxins have potential applications as antimicrobial agents, as the peptide fraction of A. gomesiana showed activity against Escherichia coli strains.

2016-08-02 | PXD003884 | Pride

A multi-omics approach unravels new toxins with potential antimicrobial, antiviral and antitumoral activities in the venom of Acanthoscurria rondoniae

Project description:The Araneae order is considered one of the most successful group among venomous animals in the world. An important factor for this success is the production of venoms, a refined biological fluid rich in proteins, short peptides and cysteine-rich peptides (CRPs). These toxins may present pharmacologically relevant biological actions, as antimicrobial, antiviral and anticancer activities, for instance. Therefore, there is an increasing interest in the exploration of venom toxins for therapeutic reasons, such as drug development. However, the process of peptide sequencing and mainly the evaluation of potential biological activities of these peptides is laborious, considering the low yield of venom extraction and the high variability of toxins present in spider venoms. Here we show a robust methodology for identification, sequencing, and initial screening of potential bioactive peptides found in the venom of Acanthoscurria rondoniae. This methodology consists in a multi-omics approach involving proteomics, peptidomics and transcriptomics analyses allied to in silico predictions of antibacterial, antifungal, antiviral and anticancer activities. Through the application of this strategy, a total of 92,889 venom gland transcripts were assembled and 84 novel toxins were identified at the protein level, including 7 short peptides and 10 fully sequenced CRPs (belonging to 7 toxin families). In silico analysis revealed that 7 CRPs families have potential antimicrobial or antiviral activities, while 2 CRPs and four short peptides are potentially anticancer. Taken together, our results demonstrate an effective multi-omics strategy for the discovery of new toxins and in silico screening of potential bioactivities. This strategy may be useful in toxin discovery, as well as in the screening of activities for the vast diversity of molecules produced by venomous animals.

2020-07-20 | PXD019343 | 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

Taxon-specific toxicity and composition of venom produced by araneophagous white-tailed spiders (Lamponidae: Lampona sp.)

Project description:Prey-specialised spiders are adapted to capture specific prey items, including dangerous prey such as ants, termites or other spiders. It has been observed that the venoms of specialists are often prey-specific and less complex than those of generalists, but venom composition has not been studied in detail in prey-specialised spiders. Here, we investigated the venom of the prey-specialised white-tailed spider (Lamponidae: Lampona sp.), which utilises specialised morphological and behavioural adaptations to capture spider prey. We hypothesised Lampona spiders also possess venomic adaptations, specifically, its venom is more effective to focal spider prey due to the presence of prey-specific toxins. We analysed the venom composition using proteo-transcriptomics and taxon-specific toxicity using venom bioassays. Our analysis identified 208 putative toxin sequences, comprising 103 peptides <10 kDa and 105 proteins >10 kDa. Most peptides belonged to one of two families characterised by scaffolds containing eight or ten cysteine residues. Protein toxins showed similarity to galectins, leucine-rich repeat proteins, trypsins and neprilysins. The venom of Lampona was shown to be spider-specific, as it was more potent against the preferred spider prey than against alternative prey represented by a cricket. In contrast, the venom of a related generalist (Gnaphosidae: Gnaphosa sp.) was similarly potent against both prey types. Prey-specific Lampona toxins were found to form part of the protein (>10 kDa) fraction of the venom. These data provide insights into the molecular adaptations of venoms produced by prey-specialised spiders.

2023-02-08 | PXD033502 | Pride

Tetraponera aethiops venom peptidome

Project description:In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and causing intense pain to browsing mammals. Using integrated transcriptomic and proteomic approaches, we identified the venom peptidome of the plant-ant Tetraponera aethiops (Pseudomyrmecinae). The transcriptomic analysis of its venom glands revealed that 40 % of the assembled contigs encoded only seven peptide precursors related to the ant venom peptides from the A-superfamily. Among the 12 peptide masses detected by liquid chromatography-mass spectrometry (LC-MS), nine mature peptide sequences were characterized and confirmed through proteomic analysis. These venom peptides, called pseudomyrmecitoxins (PSDTX), share amino acid sequence homologies with myrmeciitoxins known for their dual offensive and defensive functions on both insects and mammals. Furthermore, we demonstrated through reduction/alkylation of the crude venom that four PSDTXs were homo- and heterodimeric. Thus, we provide the first indication that the defensive venom composition of the ant genus Tetraponera is a streamlined peptidome. We provide the first insights into the defensive venom composition of the ant genus Tetraponera indicative of a streamlined peptidome.

2020-01-10 | PXD016337 | Pride

A snapshot of Bothrops jararaca snake venom gland subcellular proteome

Project description:The synthesis of snake venom proteins is subjected to finely regulated processes in the specialized secretory epithelium within the venom gland. Such processes occur within a defined time frame in the cell and at specific cellular locations. Thus, the determination of subcellular proteomes allows the characterization of protein groups for which the site may be relevant to their biological roles, thereby allowing the deconvolution of complex biological circuits into functional information. In the case of snake venom glands, subcellular proteome analysis could help understand the molecular basis of venom variability. Consequently, knowing the functional implications of such phenotypic plasticity could prove relevant in envenoming treatment and biological research. In this regard, we performed subcellular fractionation of proteins from B. jararaca snake venom gland, focusing on nuclear proteins since this cellular compartment comprises key effectors that shape gene expression. Our results provided a snapshot of B. jararaca's subcellular venom gland proteome. They pointed to a 'conserved' proteome core among different life stages (newborn and adult) and between genders (adult male and female).

2023-09-30 | PXD040239 | Pride

Characterization of the gila monster (Heloderma suspectum suspectum) venom proteome

Project description:The archetypical venomous lizard species are the helodermatids, the Gila Monster (Heloderma suspectum) and the Beaded Lizards (Heloderma horridum). In the present study, the gila monster venom proteome was characterized using 2D-gel electrophoresis and tandem mass spectrometry-based de novo peptide sequencing followed by protein identification based on sequence homology. A total of 39 different proteins were identified out of the 58 selected spots that represent the major constituents of venom. Of these proteins, 19 have not previously been identified in helodermatid venom. The data showed that helodermatid venom is complex and that this complexity is caused by genetic isoforms and post-translational modifications including proteolytic processing. In addition, the venom proteome analysis revealed that the major constituents of the gila monster venom are kallikrein-like serine proteinases (EC 3.4.21) and phospholipase A2 (type III) enzymes (EC 3.1.1.4). A neuroendocrine convertase 1 homolog that most likely converts the proforms of the previously identified bioactive exendins into the mature and active forms was identified suggesting that these peptide toxins are secreted as proforms that are activated by proteolytic cleavage following secretion as opposed to being activated intracellularly. The presented global protein identification-analysis provides the first overview of the helodermatid venom composition.

2015-01-26 | PXD001343 | Pride

Venom proteomics of Indonesian king cobra

Project description:Complementary bottom-up MS/MS analyses contributed to complete a locus-resolved venom phenotype map for O. hannah, the world's longest venomous snake and a species of medical concern across its wide distribution range in forests from India through Southeast Asia. Its venom composition convincingly explains the main neurotoxic effects of human envenoming caused by king cobra bite. The integration of efficient chromatographic separation of the venom components, and locus-resolved toxin identification through top-down and bottom-up MS/MS-based species-specific database searching, promises a bright future to the field of venom research.

2015-08-20 | PXD001726 | Pride

Mass spectrometry of Manica rubida venom

Project description:In the present study, the venom peptidome of the red ant, Manica rubida, was characterized using an integrated transcriptomic and proteomic approach. In addition, insecticidal assays on C18 reversed-phase HPLC venom fractions were conducted on Lucilia caesar blowflies to identify neurotoxic peptides.

2020-03-20 | PXD015675 | Pride

Comparative gender peptidomics of Bothrops atrox venoms: new peptides and evidences of increased disintegrins levels in the venoms of females

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

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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