中国对虾精氨酸激酶与WSSV结构蛋白VP31的作用初探

摘要：精氨酸激酶（AK）通过调节无脊椎动物体内磷酸精氨酸与ATP之间平衡在能量代谢、储存和利用方面具有重要作用。前期研究发现，白斑综合征病毒（WSSV）囊膜蛋白VP31可以与中国明对虾AK（FcAK）发生结合作用。本文通过重组表达的rFcAK与rVP31的far-Western blotting分析，证实两者有结合作用。此外，rFcAK还与WSSV的VP19、VP28等6种结构蛋白有结合作用。双向电泳分析观察到，rFcAK与rVP31的磷酸化反应后，rVP31部分发生pI降低现象，提示rVP31可能发生了磷酸化。生物信息学分析表明VP31存在21个精氨酸残基，FcAK具有12个精氨酸结合位点，这可能为VP31和FcAK的结合活性提供了靶位。

Preliminary study on the function between arginine kinase of Fenneropenaeus chinensis and the structure proteins of white spot syndrome virus (WSSV)

ABSTRACT: Arginine kinase (AK) plays important roles in the metabolism, storage and utilization of energy by regulation of the balance between phosphorylation of arginine and ATP in invertebrate. Our previous study found that envelope protein VP31 of white spot syndrome virus (WSSV) is able to interact with arginine kinase of Fenneropenaeus chinensis (FcAK). The present study proved the binding activity between the recombinant FcAK (rFcAK) and VP31 (rVP31) by far-Western blotting. Furthermore, the far-Western blotting between the rFcAK and WSSV showed that rFcAK is able to bind with other 6 structural proteins of WSSV, including VP19 and VP28. Analysis of two-dimensional electrophoresis showed that part of VP31 migrated to the spot with reduced pI after the in vitro phosphorylating incubation between rFcAK and rVP31. It prompted that the rVP31 may be phosphorylated. The bioinformatics analysis showed that VP31 has 21 arginine residents and FcAK has 12 arginine binding sites. They may provide the loci for the binding activity between VP31 and FcAK.