Ontology highlight
ABSTRACT:
PROVIDER: PRJNA554402 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR9687566.fastq.gz | Fastqsanger.gz |
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Project description:P. yezoensis is an economically important marine crop and highly used seafood in China containing a high number of proteiP. yezoensis is an economically important marine crop and highly used seafood in China containing a high number of proteins. An oomycete, known as Pythium porphyrae, causes the red rot disease that seriously damages Pyropia farms every year in China, Korea, and Japan. To investigate the pathogen responsive proteins after the artificial infection of Pyropia with (P. porphyrae) oomycetes spores, an iTRAQ-based proteomic analysis was performed. A total of 762 differentially expressed proteins (DEP’s) were identified from which 378 proteins were highly expressed and 284 proteins were found to be low expressed. A large number of differentially expressed proteins were identified, which are involved in disease stress, carbohydrate metabolism, photosynthetic activity, and amino acid pathways as annotated in the Kyoto Encyclopedia of Genes and Genomes KEGG database. Our results showed that Pyropia resisted infection by inhibiting photosynthesis, energy and carbohydrate metabolism pathways, as supported by the change in the expression level of related proteins. Thus, the current research data provide an overall summary of the red algae response to pathogen infection. The present study could assist in a better understanding of the mechanisms behind infection resistance in P. yezoensis as well as improve the breeding of Pythium infection tolerant macroalgaens. An oomycete, known as Pythium porphyrae, causes the red rot disease that seriously damages Pyropia farms every year in China, Korea, and Japan. To investigate the pathogen responsive proteins after the artificial infection of Pyropia with (P. porphyrae) oomycetes spores, an iTRAQ-based proteomic analysis was performed. A total of 762 differentially expressed proteins (DEP’s) were identified from which 378 proteins were highly expressed and 284 proteins were found to be low expressed. A large number of differentially expressed proteins were identified, which are involved in disease stress, carbohydrate metabolism, photosynthetic activity, and amino acid pathways as annotated in the Kyoto Encyclopedia of Genes and Genomes KEGG database. Our results showed that Pyropia resisted infection by inhibiting photosynthesis, energy and carbohydrate metabolism pathways, as supported by the change in the expression level of related proteins. Thus, the current research data provide an overall summary of the red algae response to pathogen infection. The present study could assist in a better understanding of the mechanisms behind infection resistance in P. yezoensis as well as improve the breeding of Pythium infection tolerant macroalgae
2018-12-03 | PXD009363 | Pride
Project description:Pyropia yezoensis Transcriptome
| PRJNA182064 | ENA
Project description:Porphyra/Pyropia seaweeds are promising sources for functional foods development, offering a rich macro- and micronutrient profiles. In New Zealand (NZ), endemic Porphyra/Pyropia species (karengo), exhibit considerable variability driven by geography, seasonality, and climate, which may influence their nutritional quality. Despite their use as traditional foods, the NZ Porphyra/Pyropia remain underutilized commercially, in part due to the lack of biomolecular characterisation, particularly their bioactive protein components, hindering evidence-based species selection for seaweed farming commercialisation and functional food development. This study presents the first proteomic characterization of three NZ Porphyra/Pyropia species: Pyropia virididentata, Pyropia cinnamomea, and Porphyra GRB complex. Mass spectrometry-based proteomics analysis identified differences in the phycobiliprotein composition among the species, with the Porphyra GRB complex containing higher levels of phycocyanin. Using the protein sequence information, in silico gastrointestinal digestion analysis predicted that phycobiliproteins from NZ Porphyra/Pyropia seaweeds can potentially release bioactive peptides capable of inhibiting angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) activities. Sequence-based allergenicity prediction indicated possible cross-reactivity between NZ Porphyra/Pyropia β-phycoerythrin and β-phycocyanin against the β-phycocyanin allergen from spirulina, which is associated with a low incidence of allergy. Proximate analysis revealed that NZ Porphyra/Pyropia seaweeds have high protein (26–30.2 %) and carbohydrate (48.3–50.9 %) contents, and low fat and free sugar levels. Amino acid profiling further showed that NZ Porphyra/Pyropia seaweeds are relatively rich in sulphur-containing amino acids and umami-associated amino acids. Overall, these findings highlight the potential of NZ Porphyra/Pyropia seaweeds as a novel plant-based protein source for functional food applications.
2026-02-09 | PXD069102 | Pride