Dataset Information

Identification of Phosphorylation Sites of Hemocyanin in Penaeus Vannamei Mediated by Casein Kinase II

ABSTRACT: Detection of Casein Kinase II mediated hemocyanin phosphorylation sites by LTQ-Orbitrap Elite

INSTRUMENT(S):

ORGANISM(S): Penaeus Vannamei

TISSUE(S): Blood Plasma

SUBMITTER: Feng Qian

LAB HEAD: Qian Feng

PROVIDER: PXD032927 | Pride | 2026-03-23

REPOSITORIES: Pride

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Dephosphorylation at Ser548 regulates hemocyanin-derived antibacterial peptides and immune defense in Penaeus vannamei.

Feng Qian Q Fu Maoshuai M Zhao Xianliang X Zhao Yongzhen Y Liu Qingyun Q Aweya Jude Juventus JJ Zhang Yueling Y

iScience 20260221 3

Phosphorylation plays a critical role in regulating immune responses in invertebrates. In Penaeus vannamei, hemocyanin, a multifunctional immune protein, is cleaved to produce antimicrobial peptides (AMPs) essential for pathogen defense. This study identifies Ser548 phosphorylation of the hemocyanin small subunit (PvHMCs) as a key regulator of trypsin-mediated hemocyanin degradation and antimicrobial peptides production. Dephosphorylation of Ser548, controlled by PvCK2α kina ...[more]

PMID: 41852743

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Project description:Albeit much less abundant than Ser/Thr phosphorylation (pSer/pThr), Tyr phosphorylation (pTyr) is considered a hallmark in cellular signal transduction. However, its analysis remains a challenge. The conventional immunopurification (IP) approach using antibodies pan-specific to pTyr sites is known to have low sensitivity, poor reproducibility and high cost. SH2 domain-derived pTyr-superbinder is a good replacement of pTyr antibody for the specific enrichment of pTyr peptides for phosphoproteomics analysis. In this study, we aim to optimize the approach using SH2 superbinder for tyrosine phosphoproteome analysis. The present work covalently immobilized SH2 superbinders to agrose beads, designed and evaluated four different SH2 superbinder based experimental workflows for phosphotyrosine analysis. After made a head to head comparison of them, we observed that the combined strategy employing Ti4+-IMAC and covalently immobilized SH2 superbinder enrichment in sequence generated the largest pTyr peptide dataset (3519) with the best selectivity (90%). Next the optimal method was applied for pTyr profiling from normal mouse tissues, and resulted in the identification of 197 pTyr sites (of which 73 were novel) from 5 mg protein digests, which validated its high sensitivity. An comparison with antibody 4G10 by isolating pTyr peptides from 5 mg unstimulated Jurkat cell digests were made, our optimal strategy identified 343 while the antibody 4G10 based method identified 242 pTyr sites, respectively, further confirmed the robustness of the method. Finally, the optimal strategy was applied for quantitative pTyr phosphorylation analysis of EGF stimulated/unstimulated HeLa cells, 261 pTyr sites were successfully quantified from 5 mg stable-isotope dimethyl labling protein digests. In general, the combination of Ti4+-IMAC and SH2 superbinder enrichment in sequence generated a facial and robust strategy for qualitative and quantitative analysis of pTyr proteome.

Project description:Background: Baylisascaris procyonis is an intestinal ascarid worm that parasitizes in raccoons and causes fatal neural, visceral, and ocular larva migrans in humans. Phosphorylated proteins and protein kinases have been studied as vaccine and drug target candidates against parasitic infections. However, no data are available on protein phosphorylation in the raccoon roundworm. Methods: In this study, the entire proteome of adult B. procyonis was enzymatically digested. Then, phosphopeptides were enriched using immobilized metal affinity chromatography (IMAC) and analyzed by liquid chromatography-mass spectrometry (LC-MS/MS). Results: Our phosphoproteome analysis displayed 854 unique phosphorylation sites mapped to 450 proteins in B. procyonis (3,308 phosphopeptides total). The annotated phosphoproteins were associated with various biological processes, including cytoskeletal remodeling, supramolecular complex assembly, and developmental regulation. The phosphopeptide functional enrichment revealed that B. procyonis phosphoproteins were mostly involved in the cytoskeleton cellular compartment, protein binding molecular function, and multiple biological processes, including regulating supramolecular fiber and cytoskeleton organization, and assembling cellular protein-containing complexes and organelles. The significantly enriched pathways of phosphoproteins included the insulin signaling pathway, tight junction, endocytosis, longevity-regulating, glycolysis/gluconeogenesis, and apelin signaling pathways. Domain analysis revealed that the Src homology 3 domain was significantly enriched. Conclusions: This study presents the first phosphoproteomic landscape of B. procyonis, elucidating phosphorylation-mediated regulation of cytoskeletal dynamics, host interaction pathways, and metabolic adaptations. The identified 450 phosphoproteins and enriched functional domains establish a foundation for targeting conserved mechanisms critical to B. procyonis survival.

			Action	DRS
	HMC_NC_CID.msf	Msf
	HMC_NC_CID.pdResult	Other
	HMC_NC_CID.raw	Raw
	HMC_NC_HCD.msf	Msf
	HMC_NC_HCD.pdResult	Other

Dataset Information

Identification of Phosphorylation Sites of Hemocyanin in Penaeus Vannamei Mediated by Casein Kinase II

Dataset's files

Publications

Dephosphorylation at Ser548 regulates hemocyanin-derived antibacterial peptides and immune defense in <i>Penaeus vannamei</i>.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Identification of Phosphorylation Sites of Hemocyanin in Penaeus Vannamei Mediated by Casein Kinase II

Dataset's files

Publications

Dephosphorylation at Ser548 regulates hemocyanin-derived antibacterial peptides and immune defense in &lt;i&gt;Penaeus vannamei&lt;/i&gt;.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dephosphorylation at Ser548 regulates hemocyanin-derived antibacterial peptides and immune defense in <i>Penaeus vannamei</i>.