Amphibalanus amphitrite
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA79921 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR094476.fastq.gz | Fastqsanger.gz | |||
| SRR094478.fastq.gz | Fastqsanger.gz | |||
| SRR094479.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 3 of 3 |
Similar Datasets
Project description:Settlement-inducing protein complex (SIPC) is a protein that acts as a phoromone cue to attract conspecific of the barnacle Amphibalanus amphitrite to settle on a substrate. Recombinant settlement-inducing protein complex was expressed in insect Sf9 cells through a baculovirus overexpression system, purified and analysed by mass spectrometry to confirm its identity.
2019-01-07 | PXD006858 | Pride
Project description:Balanus amphitrite is a small striped barnacle
| PRJNA43199 | ENA
Project description:A complete understanding of barnacle adhesion remains elusive as the process occurs within and beneath the confines of a rigid calcified shell. Barnacle cement is mainly proteinaceous and several individual proteins have been identified in the hardened cement at the barnacle-substrate interface.We report the discovery of a novel 114kD cement protein, which is identified in material secreted onto various surfaces by adult barnacles and with the encoding gene highly expressed in the sub-mantle tissue.
2015-10-20 | PXD001982 | Pride
Project description:Transcriptome sequencing of naupliar- cyprid- and adult-specific normalised ESTs libraries of the acorn barnacle Balanus amphitrite.
| PRJNA79891 | ENA
Project description:The base of the barnacle Amphibalanus amphitrite has a layer of protein and cuticle that adheres the barnacle to the surface. The proteins in the adhesive have been characterized, but it is unknown whether the adhesive proteins are associated with the cuticle. To address this possibility, we examined the proteins associated with the molt (exuviae) from the main body, which is also composed of cuticle.
2021-09-08 | PXD013036 | Pride
Project description:Background: Marine biofouling negatively impacts industries reliant upon submerged stationary surfaces. The acorn barnacle Amphibalanus amphitrite is a major biofouler that permanently attaches to a wide array of substrates by producing a proteinaceous adhesive at the surface interface. These interface proteins are difficult to solubilize, and the understanding of what proteins exist in the adhesive has only been expanded with the use of the strong polar solvent hexafluoroisopropanol in combination with standard gel-based sample processing methods for proteomics analysis. Although effective, existing sample processing methods are labor and time intensive, hindering progress in this field. Results: We have developed a more efficient sample processing method by exploiting pressure cycling technology, which aids in protein extraction and digestion for proteomics analysis, and explored the efficacy of multiple solvents in combination with pressure on protein identification. We found that barnacle adhesive proteins can be extracted and digested in the same tube using pressure cycling technology, minimizing sample loss, increasing throughput to 16 concurrently processed samples, and decreasing sample processing time to under 8 hours. Pressure cycling technology methods produced similar proteomes in comparison to previous methods. Two solvents which were ineffective at extracting proteins from the adhesive at ambient pressure (urea and methanol) produced more protein identifications under pressure than hexafluoroisopropanol, leading to the identification and our description of >40 novel proteins at the interface. Many A. amphitrite adhesive proteins have no sequence similarity to publically available proteins, highlighting the unique adherent processes evolved by barnacles. Conclusion: Using pressure cycling technology, we describe methods that produce robust and consistent protein identifications from barnacle adhesive. These methods can be used to examine changes in barnacle adhesive, enabling future research on the effects of environmental and surface substrate composition on barnacle cement, a critical step for both broadening the understanding of barnacle adhesion and the development of new coatings for submerged surfaces to combat hard biofoulants.
2019-07-04 | PXD012730 | Pride
Project description:ABSTRACT: Acorn barnacles are efficient colonizers on a wide variety of marine surfaces. As they proliferate on critical infrastructure, their settlement and growth have deleterious effects on performance. To address acorn barnacle biofouling, research has focused on the settlement and adhesion processes with the goal of informing the development of novel coatings. This effort has resulted in the discovery and characterization of several proteins found at the adhesive substrate interface, i.e. cement proteins, and a deepened understanding of the function and composition of the biomaterials within this region. While the adhesive properties at the interface are affected by the interaction between the proteins, substrate, and mechanics of the calcified base plate, little attention has been given to the interaction between the proteins and the cuticular material present at the substrate interface. Here, the proteome of the organic matrix isolated from the base plate of the acorn barnacle Amphibalanus amphitrite is compared with the chitinous and proteinaceous matrix embedded within A. amphitrite parietal plates. The objective was to gain an understanding of how the basal organic matrix may be specialized for adhesion via an in-depth comparative proteome analysis. In general, the majority of proteins identified in the parietal matrix were also found in the basal organic matrix, including nearly all those grouped in classes of cement proteins, enzymes and pheromones. However, the parietal organic matrix was enriched with cuticle-associated proteins, of which ~30% of those identified were unique to the parietal region. In contrast, ~30-40% of the protease inhibitors, enzymes, and pheromones identified in the basal organic matrix were unique to this region. Not unexpectedly, nearly 50% of the cement proteins identified in the basal region were significantly distinct from those found in the parietal region. The wider variety of identified proteins in the basal organic matrix indicates a greater diversity of biological function in the vicinity of the substrate interface where several processes related to adhesion, cuticle formation, and expansion of the base synchronize to play a key role in organism survival.
2023-12-12 | MSV000093654 | MassIVE
Project description:Amphibalanus amphitrite Raw sequence reads
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Project description:Amphibalanus amphitrite Genome sequencing and assembly
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Project description:Amphibalanus amphitrite Transcriptome or Gene expression
| PRJNA271096 | ENA