Ontology highlight
ABSTRACT:
PROVIDER: PRJNA587301 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR10414000_1.fastq.gz | Fastqsanger.gz | |||
| SRR10414000_2.fastq.gz | Fastqsanger.gz | |||
| SRR10414001_1.fastq.gz | Fastqsanger.gz | |||
| SRR10414001_2.fastq.gz | Fastqsanger.gz | |||
| SRR10414002_1.fastq.gz | Fastqsanger.gz |
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Project description:Spiders are a highly diverse group of arthropods that occur in most habitats on land. Notably, spiders have significant ecological impact as predators because of their extraordinary prey capture adaptations, venom and silk. Spider venom is among the most heterogeneous animal venoms and has pharmacological applications, while spider silk is characterized by great toughness with potential for biomaterial application. We describe the genome sequences of two spiders representing two major taxonomic groups, the social velvet spider Stegodyphus mimosarum (Araneomorphae), and the Brazilian white-knee tarantula Acanthoscurria geniculata (Mygalomorphae). We annotate genes using a combination of transcriptomic and in-depth proteomic analyses. The genomes are large (2.6 Gb and 6 Gb, respectively) with short exons and long introns and approximately 50% repeats, reminiscent of typical mammalian genomes. Phylogenetic analyses show that spiders and ticks are sister groups outgrouped by mites, and phylogenetic dating using a molecular clock dates separation of velvet spider and tarantula at 270 my. Based on the genomes and proteomes, we characterize the genetic basis of venom and silk production of both species in detail. Venom protein composition differs markedly between the two spiders, with lipases as the most abundant protein in the velvet spider and present only at low concentration in tarantula. Venom in both spiders contains proteolytic enzymes, and our analyses suggest that these enzymes target and process precursor peptides that subsequently mediate the toxic effects of venom. Complete analysis of silk genes reveal a diverse suite of silk proteins in the velvet spider including novel types of spidroins, and dynamic evolution of major ampullate spidroin genes, whereas silk protein diversity in tarantula is far less complex. The difference in silk proteins between species is consistent with a more complex silk gland morpholgy and use of three-dimentional capture webs consisting of multiple silk types in aranomorph spiders.
2014-05-01 | PXD000318 | Pride
Project description:Spiders are renowned for their efficient capture of flying insects using intricate aerial webs. How the spider nervous systems evolved to cope with this specialized hunting strategy and various environmental clues in an aerial space remains unknown. Here, we report a brain cell atlas of >30,000 single-cell transcriptomes from a web-building spider (Hylyphantes graminicola). Our analysis revealed the preservation of ancestral neuron types in spiders, including the potential coexistence of noradrenergic and octopaminergic neurons, and many peptidergic neuronal types that are lost in insects. By comparing the genome of two newly sequenced plesiomorphic burrowing spiders with three aerial web-building spiders, we found that the positively selected genes in the ancestral branch of web-building spiders were preferentially expressed (42%) in the brain, especially in the three mushroom body-like neuronal types. By gene enrichment analysis and RNAi experiments, these genes were suggested to be involved in the learning and memory pathway and may influence the spiders’ web-building and hunting behavior. Our results provide key sources for understanding the evolution of behavior in spiders and reveal how molecular evolution drives neuron innovation and the diversification of associated complex behaviors.
2023-10-24 | GSE241696 | GEO
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
Project description:Spiders have distinct capture prey behaviors selected along Araneae´s evolutive history, but mainly based on the use of venom for prey paralysis. Uloboridae spiders lost the venom glands secondarily in evolution. Due to that they extensively wrap prey with silk to paralyze and begin digestion. During the extra-oral digestion, the digestive fluid very efficiently performs the liquefaction of both the prey and the AcSp2 spidroins from the web fibers. Despite the efficiency of this process, the cocktail of enzymes involved in digestion in Uloboridae spiders is unknown. In this study, we evaluated the protein content in the midgut of Uloborus sp. using enzymatic, proteomic, and phylogenetic analysis approaches. Hydrolases as peptidases (endo and exopeptidases: cysteine, serine and metallopeptidases), carbohydrases (alpha-amylase, chitinase, alpha-mannosidase), and lipases were biochemically assayed; 50 proteins, annotated as enzymes, structural proteins, and toxins, were identified. This is the first characterization of the molecules involved in the digestive process and the midgut protein content of a nonvenomous spider.
2023-03-11 | PXD037345 | 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: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).
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Project description:Arboreal adaptation and venom evolution in Australian funnel-web spiders
| PRJEB14965 | ENA
Project description:Arboreal adaptation and venom evolution in Australian funnel-web spiders
| PRJEB14734 | ENA
Project description:Venoms and the toxins they contain represent molecular adaptations that have evolved on numerous occasions throughout the animal kingdom. However, the processes that shape venom protein evolution are poorly understood because of the scarcity of whole genome data available for comparative analyses of venomous species. Here, we perform a broad comparative toxicogenomic analysis to gain insight into the genomic mechanisms of venom evolution in robber flies (Asilidae). We first sequenced a high-quality draft genome of the hymenopteran hunting robber fly Dasypogon diadema, and analysed its venom by a combined proteotranscriptomic approach, and compared our results to recently described robber fly venoms to assess the general composition and major components of asilid venom. We then applied a comparative genomics approach, based on one additional asilid genome, ten high-quality dipteran genomes, and two lepidopteran outgroup-genomes, to reveal the evolutionary mechanisms and origins of identified venom proteins in robber flies. While some venom proteins were identified in the non-asilid genomes, several of the identified highly expressed venom proteins appear to be unique to robber flies. Our results reveal that the venom of D. diadema likely evolves in a multimodal fashion comprising 1) neofunctionalization after gene duplication, 2) expression-dependent co-option of proteins and 3) asilid lineage-specific orphan genes with enigmatic origin. The role of such orphan genes is currently being disputed in evolutionary genomics, but has not yet discussed in the context of toxin evolution. Our results display an unexpected dynamic venom evolution in asilid insects, which contrasts the findings of the only other insect toxicogenomic evolutionary analysis, in parasitoid wasps (Hymenoptera), were toxin evolution is dominated by single gene co-option.
2019-06-13 | PXD013358 | Pride