Department of Biotechnology, Faculty of Science and Humanities, SRM University, SRM Nagar, Kattankulathur 603 203, Chennai, Tamil Nadu, India.
Gene. 2012 Oct 25;508(2):241-9. doi: 10.1016/j.gene.2012.07.050. Epub 2012 Aug 8.
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.
伴侣蛋白（MrChap）是从淡水虾罗氏沼虾的构建转录组数据集鉴定出来的。MrChap 肽含有一个 11 到 525 之间的长伴侣超级家族结构域。MrChap 肽序列中有三个伴侣无尾复合物多肽 (TCP-1) 特征，位于 36-48、57-73 和 85-93 位。采用 qRT-PCR 法检测健康罗氏沼虾和感染传染性皮下及造血坏死病毒 (IHHNV) 的罗氏沼虾中 MrChap 的基因表达。为了了解其生物学活性，构建并在大肠杆菌 BL21 (DE3) 中表达了重组 MrChap 基因。ATPase 分析结果表明，重组 MrChap 蛋白表现出明显的 ATPase 活性。伴侣活性分析表明，重组 MrChap 蛋白是一种具有活性的伴侣。这些结果表明，MrChap 可能参与了罗氏沼虾对病毒感染的免疫反应。这些发现表明，重组 MrChap 蛋白可能用于免疫治疗方法。
