A clip-domain serine proteinase homolog (SPH) in oriental river prawn, Macrobrachium nipponense provides insights into its role in innate immune response

Zhili Ding, Youqin Kong, liqiao Chen, Jianguang Qin, Shengming Sun, Ming Li, Zhenyu Du, Jinyun Ye

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    Abstract

    In this study, a clip-domain serine proteinase homolog designated as MnSPH was cloned and characterized from a freshwater prawn Macrobrachium nipponense. The full-length cDNA of MnSPH was 1897bp and contained a 1701bp open reading frame (ORF) encoding a protein of 566 amino acids, a 103bp 5'-untranslated region, and a 93bp 3'-untranslated region. Sequence comparison showed that the deduced amino acids of MnSPH shared 30-59% identity with sequences reported in other animals. Tissue distribution analysis indicated that the MnSPH transcripts were present in all detected tissues with highest in the hepatopancreas and ovary. The MnSPH mRNA levels in the developing ovary were stable at the initial three developmental stages, then increased gradually from stage IV (later vitellogenesis), and reached a maximum at stage VI (paracmasis). Furthermore, the expression of MnSPH mRNA in hemocytes was significantly up-regulated at 1.5h, 6h, 12h and 48h post Aeromonas hydrophila injection. The increased phenoloxidase activity also demonstrated a clear time-dependent pattern after A.hydrophila challenge. These results suggest that MnSPH participates in resisting to pathogenic microorganisms and plays a pivotal role in host defense against microbe invasion in M.nipponense.

    Original languageEnglish
    Pages (from-to)336-342
    Number of pages7
    JournalFish and Shellfish Immunology
    Volume39
    Issue number2
    DOIs
    Publication statusPublished - Aug 2014

    Keywords

    • Innate immune
    • Macrobrachium nipponense
    • MRNA expression
    • Serine protease homolog

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