新近出版的普通病毒学杂志《普通病毒学杂志》(Journal of General Virology，August 2008; Volume 89, Part 8)刊登了中科院水生所赵哲博士为第一作者的封面文章“Identification and characterization of a novel envelope protein in Rana grylio virus” （Journal of General Virology，2008 89: 1866-1872），该项研究结果由张奇亚研究员负责的水生病毒学科组和桂建芳研究员负责的发育遗传学学科组合作完成。
论文报道了一个新发现的蛙虹彩病毒RGV囊膜蛋白基因及功能特征。该RGV 53R 基因的ORF长1569bp，编码一个长为522aa、分子量大小约为54.7kDa的蛋白，具有两次跨膜结构域、N末端十四烷基化位点和两个不变的半胱氨酸残基这样三个结构特征。在病毒感染细胞后12h才开始转录和表达，且能被AraC所抑制，为RGV晚期表达基因。免疫荧光定位显示其表达产物较早时候在细胞质中呈颗粒状分布，定位于内质网上，而晚期则定位于病毒加工厂。抗体中和实验进一步显示53R抗体能明显降低或延迟RGV的感染，证实这是一个在病毒装配和感染过程中发挥重要作用的虹彩病毒囊膜蛋白。Bioon
中科院水生所近两年在水生病毒学领域取得一系列进展，有关研究结果已在国际系列病毒学及相关学科期刊上发表[Journal of Virology, 2008，82: 6889-6901; Virology, 2008, 372:118-126; Journal of General Virology, 2008, 89:1866-1872; Virus Research, 2007,123:128–137; 2008, 132:86–96; Apoptosis, 2007, 12(9):1569-1577; Journal of Virological Methods.2008. 148: 205–210; Viral Immunology, 2006,19(4):637-645; 2007, 20(1): 150-159; Archives Virology, 2008, 153: 1143–1148]，并受到国际同行关注。如揭示蛙虹彩病毒装配过程、以及发现RGV尿嘧啶脱氧核糖核苷三磷酸酶dUTPase基因在病毒复制中有重要作用的论文发表后，被英国学者在长篇综述中(Netherton et al, Adv Virus Res. 2007 ;70C :101-182)作为虹彩病毒细胞质病毒加工厂的典型事例所引用。（生物谷Bioon.com）
生物谷推荐原始出处：
Journal of General Virology，89 (2008), 1866-1872，Jian-Fang Gui，Qi-Ya Zhang
Identification and characterization of a novel envelope protein in Rana grylio virus
Zhe Zhao, Fei Ke, You-Hua Huang, Jiu-Gang Zhao, Jian-Fang Gui and Qi-Ya Zhang
State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Graduate School of Chinese Academy of Sciences, Wuhan 430072, PR China
Correspondence
Qi-Ya Zhang
zhangqy@ihb.ac.cn
Viral envelope proteins have been proposed to play significant roles in virus infection and assembly. In this study, an envelope protein gene, 53R, was cloned and characterized from Rana grylio virus (RGV), a member of the family Iridoviridae. Database searches found its homologues in all sequenced iridoviruses, and sequence alignment revealed several conserved structural features shared by virus capsid or envelope proteins: a myristoylation site, two predicted transmembrane domains and two invariant cysteine residues. Subsequently, RT-PCR and Western blot detection revealed that the transcripts encoding RGV 53R and the protein itself appeared late during infection of fathead minnow cells and that their appearance was blocked by viral DNA replication inhibitor, indicating that RGV 53R is a late expression gene. Moreover, immunofluorescence localization found an association of 53R with virus factories in RGV-infected cells, and this association was further confirmed by expressing a 53R–GFP fusion protein in pEGFP-N3/53R-transfected cells. Furthermore, detergent extraction and Western blot detection confirmed that RGV 53R was associated with virion membrane. Therefore, the current data suggest that RGV 53R is a novel viral envelope protein and that it may play an important role in virus assembly. This is thought to be the first report on a viral envelope protein that is conserved in all sequenced iridoviruses.
