Panapat PhairohThana SuthibatpongTriwit RattanarojpongNujarin JongrujaSaengchan SenapinKiattawee ChoowongkomonPongsak KhunraeKing Mongkut s University of Technology ThonburiThailand National Center for Genetic Engineering and BiotechnologyMahidol UniversityKasetsart University2018-12-112019-03-142018-12-112019-03-142016-06-01PLoS ONE. Vol.11, No.6 (2016)193262032-s2.0-84977103176https://repository.li.mahidol.ac.th/handle/20.500.14594/41514© 2016 Phairoh et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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.Mahidol UniversityAgricultural and Biological SciencesBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1371/journal.pone.0158301