Penaeus vannamei
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ABSTRACT:
PROVIDER: PRJNA1023052 | ENA |
REPOSITORIES: ENA
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Project description:The functional diversity of crustacean hemocyanins is broad, encompassing O2 delivery, innate immune response, metabolite storage, and osmolyte balance, all in a heterogeneous protein structure. As such, the sequence diversity of this class of proteins and its subunit composition are the focus of many studies on crustacean adaptation to environmental challenges. Recent transcriptomic and genomic sequencing on the Pacific whiteleg shrimp Litopenaeus vannamei has identified unique isoforms of hemocyanin including an ancestral β-type subunit thought to be lost in penaeid shrimp. However, it is unknown the degree to which these isoforms are translated as proteins, and whether they differ in function. The present study uses proteomic approaches to characterize the protein-level abundance and organization of these hemocyanin isoforms within their native oligomeric structures. Fractions of each hemocyanin oligomeric form were purified by size-exclusion high performance liquid chromatography for identification of subunit isoforms using tandem mass spectrometry at <1% protein false discovery rate. Relative abundances of hemocyanin oligomers and monomeric subunits from hemolymph and fractions were also quantified by polyacrylamide gel electrophoresis with and without denaturation for comparison of relative abundance. Ten hemocyanin isoforms were identified by tandem mass spectrometry in both hemocyanin oligomer fractions including a single small subunit, eight large subunits, and the first protein-level evidence of a β-type subunit in penaeid shrimp. Hemocyanin subunits were organized primarily as hexamers (95-99% relative abundance) as opposed to dodecamers. Hexamers utilized a significantly higher ratio (2.05:1) of small subunit to large subunit compared to dodecamers (1.04:1), and the relative abundances of the large subunit isoforms was dominated by HcL1 in both fractions. The ability to distinguish and quantify hemocyanin isoforms within oligomeric structures will aid future studies linking hemocyanin genes to function and physiology as well as offer insight into the evolutionary history of crustaceans.
2020-02-07 | PXD014575 | Pride
Project description:Transcriptomic profiling of shrimp hemocytes after HIF-1a interference under Vibrio parahaemolyticus stimulation
| PRJNA1427275 | ENA
Project description:Detection of Casein Kinase II mediated hemocyanin phosphorylation sites by LTQ-Orbitrap Elite
2026-03-23 | PXD032927 | Pride
Project description:A marine shrimp that is used in shrimp farming
| PRJNA12975 | ENA
Project description:Transcriptome sequencing of white pacific shrimp Litopenaeus vannamei
| PRJNA229518 | ENA
Project description:MiRNA sequencing of shrimp stimulated by Vibrio alginolyticus
| PRJNA761657 | ENA
Project description:Pacific whiteleg shrimp (Litopenaeus vannamei)
| PRJNA255337 | ENA
Project description:Hemocyanins function not only as oxygen carriers in the hemolymph of arthropods and molluscs but also as an important multifunctional immune molecule. In this study, we observed a significant increase in hemocyanin expression and a decrease in PO activity in Penaeus vannamei infected with acute hepatopancreatic necrosis disease (AHPND). Using gas chromatography-mass spectrometry (GC-MS)-based metabolomics, we found that knockdown of the hemocyanin gene (PvHMC) led to significant reductions in phenylalanine and tyrosine levels. Subsequent qPCR, PO activity assays, and LC-MS analyses revealed that PvHMC knockdown significantly elevated the transcript levels of key enzymes in the phenylalanine-tyrosine metabolic pathway, accompanied by increased L-Dopa levels and enhanced PO activity. In contrast, exogenous supplementation of phenylalanine or tyrosine downregulated these four enzymes and reduced PO activity. Furthermore, after PvHMC knockdown, inhibiting phenylalanine hydroxylase with 4-Chloro-DL-phenylalanine (PCPA) or tyrosine hydroxylase with 3-Iodo-L-tyrosine (3-IT) increased phenylalanine or tyrosine levels, decreased the expression of the corresponding enzymes, and reduced both L-Dopa content and PO activity. Collectively, these results demonstrate that during Vibrio parahaemolyticus (VpAHPND) infection, PvHMC is significantly downregulated and negatively regulates PO activity via the phenylalanine-tyrosine metabolism, thereby enhancing immune defense. This study elucidates a novel metabolic mechanism through underlying PvHMC-mediated regulation of the PO cascade regulation, providing new insights into the interplay between metabolism and immunity in shrimp.
2026-05-22 | MTBLS14563 | MetaboLights
Project description:Tissue differential expression of shrimp (PRJCA031192)
| PRJDB38453 | ENA