Publication: C-terminal hemocyanin from hemocytes of penaeus vannamei interacts with ERK1/2 and undergoes serine phosphorylation
Issued Date
2009-05-01
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ISSN
15353893
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2-s2.0-66749123017
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Proteome Research. Vol.8, No.5 (2009), 2476-2483
Suggested Citation
Phattaraorn Havanapan, Rattiyaporn Kanlaya, Apichai Bourchookarn, Chartchai Krittanai, Visith Thongboonkerd C-terminal hemocyanin from hemocytes of penaeus vannamei interacts with ERK1/2 and undergoes serine phosphorylation. Journal of Proteome Research. Vol.8, No.5 (2009), 2476-2483. doi:10.1021/pr801067e Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/27231
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Title
C-terminal hemocyanin from hemocytes of penaeus vannamei interacts with ERK1/2 and undergoes serine phosphorylation
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Abstract
To understand molecular immune response of Penaeus vannamei during Taura syndrome virus (TSV) infection, expression and functional proteomics studies were performed on hemocyanin, which is a major abundant protein in shrimp hemocytes. Two-dimensional electrophoresis (2-DE) revealed up- regulation of several C-terminal fragments of hemocyanin, whereas the N-terminal fragments were down-regulated during TSV infection. 2-D Western blot analysis showed that the C-terminal hemocyanin fragments had more acidic isoelectric points (p/), whereas the N-terminal fragments had less acidic p/. Further analysis by NetPhos showed a greater number of serine phosphorylation sites in the C-terminal hemocyanin. Additionally, motif scan using Scansite revealed ERK D-domain, which is required for activation of ERK1/2 effector kinase, as a kinase-binding site at the 527th valine in the C-terminal hemocyanin, whereas neither motif nor functional domain was found in the N-terminus. Co- immunoprecipitation confirmed the interaction between the C-terminal hemocyanin and ERK1/2. 1-D Western blot analysis showed that ERK1/2 was also up-regulated during TSV infection. Our findings demonstrate for the first time that ERK1/2 signaling pathway may play an important role in molecular immune response of P. vannamei upon TSV infection through its interaction with the C-terminal hemocyanin. © 2009 American Chemical Society.