ICP35是在白斑综合征病毒中鉴定出的一种类TREX蛋白。
ICP35 Is a TREX-Like Protein Identified in White Spot Syndrome Virus.
作者信息
Phairoh Panapat, Suthibatpong Thana, Rattanarojpong Triwit, Jongruja Nujarin, Senapin Saengchan, Choowongkomon Kiattawee, Khunrae Pongsak
机构信息
Department of Microbiology, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
Department of Physics, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
出版信息
PLoS One. 2016 Jun 27;11(6):e0158301. doi: 10.1371/journal.pone.0158301. eCollection 2016.
ICP35 is a non-structural protein from White spot syndrome virus believed to be important in viral replication. Since ICP35 was found to localize in the host nucleus, it has been speculated that the function of ICP35 might be involved in the interaction of DNA. In this study, we overexpressed, purified and characterized ICP35. The thioredoxin-fused ICP35 (thio-ICP35) was strongly expressed in E. coli and be able to form itself into dimers. Investigation of the interaction between ICP35 and DNA revealed that ICP35 can perform DNase activity. Structural model of ICP35 was successfully built on TREX1, suggesting that ICP35 might adopt the folding similar to that of TREX1 protein. Several residues important for dimerization in TREX1 are also conserved in ICP35. Residue Asn126 and Asp132, which are seen to be in close proximity to metal ions in the ICP35 model, were shown through site-directed mutagenesis to be critical for DNase activity.
ICP35是一种来自白斑综合征病毒的非结构蛋白，据信在病毒复制中起重要作用。由于发现ICP35定位于宿主细胞核，因此推测ICP35的功能可能与DNA的相互作用有关。在本研究中，我们对ICP35进行了过表达、纯化和表征。硫氧还蛋白融合的ICP35（硫氧-ICP35）在大肠杆菌中强烈表达，并能够形成二聚体。对ICP35与DNA相互作用的研究表明，ICP35具有DNase活性。ICP35的结构模型成功构建在TREX1上，表明ICP35可能采用与TREX1蛋白相似的折叠方式。TREX1中对二聚化重要的几个残基在ICP35中也保守。通过定点诱变显示，在ICP35模型中与金属离子紧密相邻的Asn126和Asp132残基对DNase活性至关重要。
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