| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5907140 | Gene | 2012 | 9 Pages |
Chaperonin (MrChap) was identified from a constructed transcriptome dataset of freshwater prawn Macrobrachium rosenbergii. The MrChap peptide contains a long chaperone super family domain between 11 and 525. Three chaperone tailless complex polypeptide (TCP-1) signatures are present in the MrChap peptide sequence at 36-48, 57-73 and 85-93. The gene expressions of MrChap in both healthy M. rosenbergii and those infected with infectious hypodermal and hematopoietic necrosis virus (IHHNV) were examined using qRT-PCR. To understand its biological activity, the recombinant MrChap gene was constructed and expressed in Escherichia coli BL21 (DE3). The results of ATPase assay showed that the recombinant MrChap protein exhibited apparent ATPase activity. Chaperone activity assay showed that the recombinant MrChap protein is an active chaperone. These results suggest that MrChap is potentially involved in the immune responses against viral infection in M. rosenbergii. These findings indicate that the recombinant MrChap protein may be used in immunotherapeutic approaches.
⺠Chaperonin encoding cDNA has been identified from M. rosenbergii. ⺠Three chaperone TCP-1 signatures are present in MrChap amino acid. ⺠Highest gene expression was observed in hemocyte. ⺠Recombinant MrChap is an active chaperone and exhibited ATPase activity. ⺠MrChap recombinant product may be used as immunotherapeutic agent.
