Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ABSTRACT: ECOLOGICAL AND MOLECULAR ASPECTS OF LIGNOCELLULOSE DIGESTION IN NEOTROPICAL HIGHER TERMITES

PROVIDER: PRJNA735327 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR14740111_1.fastq.gz	Fastqsanger.gz
	SRR14740111_2.fastq.gz	Fastqsanger.gz
	SRR14740112_1.fastq.gz	Fastqsanger.gz
	SRR14740112_2.fastq.gz	Fastqsanger.gz
	SRR14740113_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 28

Similar Datasets

ECOLOGICAL AND MOLECULAR ASPECTS OF LIGNOCELLULOSE DIGESTION IN NEOTROPICAL HIGHER TERMITES

Project description:ECOLOGICAL AND MOLECULAR ASPECTS OF LIGNOCELLULOSE DIGESTION IN NEOTROPICAL HIGHER TERMITES

| PRJEB17080 | ENA

Project description:symbiotic prokaryotic communities of higher and lower termites

| PRJNA532793 | ENA

termite gut metagenome

Project description:Gut metagenomes from 48 lower and higher termites

| PRJNA732531 | ENA

Project description:Gut bacterial community of fungus-growing higher termites

| PRJNA689666 | ENA

Project description:Termites in a World of Climate Change: An Ecological, Functional, and Molecular Approach

| PRJNA1443299 | ENA

undefined

Project description:Lignocellulose-rich residues in anaerobic digestion

| PRJEB55850 | ENA

Venom evolution of 15 neotropical ants

Project description:To comprehend the drivers underlying venom variation in ants, we selected 15 Neotropical species and recorded a range of traits, including ecology, morphology, and venom bioactivity. Principal component analysis of both morphological and venom bioactivity traits revealed that stinging ants display two functional strategies. Additionally, phylogenetic comparative analysis indicated that venom function (predatory, defensive, or both) and mandible morphology significantly correlate with venom bioactivity and amount, while pain-inducing activity trades off with insect paralysis. Further analysis of the venom biochemistry of the 15 species revealed switches between cytotoxic and neurotoxic venom compositions in some species. This study highlights the fact that ant venoms are not homogenous, and for some species, there are major shifts in venom composition associated with the diversification of venom ecological functions.

2024-10-16 | PXD050348 | Pride

termite gut metagenome

Project description:Bacterial communities associated with hindgut compartments of higher termites Targeted Locus (Loci)

| PRJNA305127 | ENA

Venom proteome of the termite-eating spider Ammoxenus amphalodes

Project description:Venoms are complex chemical arsenals that have evolved across various animal lineages for predation, defence, and other ecological functions. In predatory species, venom composition is often shaped by diet, potentially leading to unique toxin profiles. Spiders are the most diverse group of terrestrial venomous predators, yet the venoms of most species, including highly specialized stenophagous species with narrow trophic niches, remain poorly understood. In this study, we investigated the venom of Ammoxenus amphalodes, a spider that preys exclusively on termites, to explore its molecular composition and functional adaptations. Using a proteotranscriptomic approach, we identified 116 putative toxin sequences. Half of these were cysteine-rich peptides with distinct structural motifs, most of which diverge from known spider toxins containing an inhibitor-cystine-knot (ICK) motif. The venom proteome is dominated by two ammoxotoxin families, which together account for more than half of all transcripts, supporting the hypothesis that spiders with specialized diets have lower toxin diversity. We also identified a low proportion of larger venom proteins, including cholinesterases, phospholipases, immune proteins, carbonic anhydrases, and EF-hand proteins, which may serve housekeeping functions or play auxiliary roles in prey incapacitation. Bioassays with selected lab-produced peptides revealed one prey-specific peptide, U-AXTX(9)-Aa15, a member of the waprin family, which paralyses termites but not flies. The other peptides tested showed limited prey specificity, challenging assumptions of venom specialization. These findings provide new insights into the evolution of venom in dietary specialists and broaden the search for novel bioactive compounds with potential biotechnological applications.

2026-04-27 | PXD074241 | Pride

Giant panda (Ailuropoda melanoleuca) gut microbiomes degrade bamboo in distinct patterns: heterofermentation of green leaves to ethanol, lactate and acetate, and homofermentation of yellow pith to lactate

Project description:The iconic giant panda is an endangered species known worldwide for its peculiar dietary habits. While retaining the digestive system of a carnivore, the giant panda successfully moved into a diet almost exclusively based on bamboo. Digestion of lignocellulose is believed to be conducted solely by its gut microbiome, provided that no lignocellulose-degrading enzyme was found in the giant panda’s genome. Many reports focused on which lignocellulose component feeds the giant panda, while little effort was made to link the products of bamboo fermentation to the panda’s dietary choices. In the present study, fermentation of either green leaves or yellow pith was conducted in the laboratory using gut microbiomes derived from either green or yellow stools, respectively. Green leaves were fermented to ethanol, lactate and acetate, while yellow pith to lactate resembling, respectively, hetero/homo-fermentation patterns. Several microbial pathways (assessed by metaproteomics) related to hemicellulose rather than cellulose degradation. However, alpha-amylases (E.C. 3.2.1.1) from the giant panda itself were the most predominant enzyme (up to 60% of all metaproteins), indicating that they have a primary role in bamboo digestion. The distinct fermentation profiles resulting from digestion of selected portions of bamboo may be part of the feeding strategy of giant pandas.

2020-03-02 | PXD010872 | 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