Shrimp arginine kinase being a binding protein of WSSV envelope protein VP31

文献类型： 外文期刊

第一作者： Ma Cuiyan

作者： Ma Cuiyan;Gao Qiang;Liang Yan;Li Chen;Liu Chao;Huang Jie;Ma Cuiyan;Gao Qiang;Liang Yan;Li Chen;Liu Chao;Huang Jie

作者机构：

关键词： white spot syndrome virus (WSSV); VP31; arginine kinase; shrimp; binding protein

期刊名称：CHINESE JOURNAL OF OCEANOLOGY AND LIMNOLOGY （ 影响因子：1.068； 五年影响因子：0.983 ）

ISSN： 0254-4059

年卷期： 2016 年 34 卷 6 期

页码：

收录情况： SCI

摘要： Viral entry into the host is the earliest stage of infection in the viral life cycle in which attachment proteins play a key role. VP31 (WSV340/WSSV396), an envelope protein of white spot syndrome virus (WSSV), contains an Arg-Gly-Asp (RGD) peptide domain known as a cellular attachment site. At present, the process of VP31 interacting with shrimp host cells has not been explored. Therefore, the VP31 gene was cloned into pET30a (+), expressed in Escherichia coli strain BL21 and purified with immobilized metal ion affinity chromatography. Four gill cellular proteins of shrimp (Fenneropenaeus chinensis) were pulled down by an affinity column coupled with recombinant VP31 (rVP31), and the amino acid sequences were identified with MALDI-TOF/TOF mass spectrometry. Hemocyanin, beta-actin, arginine kinase (AK), and an unknown protein were suggested as the putative VP31 receptor proteins. SDS-PAGE showed that AK is the predominant binding protein of VP31. An i n vitro binding activity experiment indicated that recombinant AK's (rAK) binding activity with rVP31 is comparable to that with the same amount of WSSV. These results suggested that AK, as a member of the phosphagen kinase family, plays a role in WSSV infection. This is the first evidence showing that AK is a binding protein of VP31. Further studies on this topic will elucidate WSSV infection mechanism in the future.

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