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Logo of bmcvetresBioMed Centralsearchsubmit a manuscriptregisterthis articleBMC Veterinary Research
BMC Vet Res. 2012; 8: 15.
Published online Feb 7, 2012. doi:  10.1186/1746-6148-8-15
PMCID: PMC3295642
Identification of the NLS and NES motifs of VP2 from chicken anemia virus and the interaction of VP2 with mini-chromosome maintenance protein 3
Jai-Hong Cheng,#1 Shyang-Chwen Sheu,#2 Yi-Yang Lien,3 Meng-Shiunn Lee,4 His-Jien Chen,5 Wen-Hong Su,1 and Meng-Shiou Leecorresponding author6
1Department of Medical Research, Chang Gung Memorial Hospital-Kaohsiung Medical Center, Chang Gung University College of Medicine, Kaohsiung, Taiwan
2Department of Food Science, National Pingtung University of Science and Technology, Pingtung, Taiwan
3Department of Veterinary Medicine, National Pingtung University of Science and Technology, Pingtung, Taiwan
4Department of Medical Research, Tung's Taichung Metro Harbor Hospital, Taichung, Taiwan
5Department of Safety, Health and Environmental Engineering, Mingchi University of Technology, Taipei, Taiwan
6School of Chinese Pharmaceutical Science and Chinese Medicine Resources, China Medical University, Taichung, Taiwan
corresponding authorCorresponding author.
#Contributed equally.
Jai-Hong Cheng: cjaiho/at/; Shyang-Chwen Sheu: ssheu/at/; Yi-Yang Lien: yylien/at/; Meng-Shiunn Lee: mengshiunn/at/; His-Jien Chen: hjchen/at/; Wen-Hong Su: superwhsu/at/; Meng-Shiou Lee: leemengshiou/at/
Received August 21, 2011; Accepted February 7, 2012.
VP2 of chicken anemia virus (CAV) is a dual-specificity phosphatase required for virus infection, assembly and replication. The functions of the nuclear localization signal (NLS) and nuclear export signal (NES) of VP2 in the cell, however, are poorly understood. Our study identified the presence of a NLS in VP2 and showed that the protein interacted significantly with mini-chromosome maintenance protein 3 (MCM3) in the cell.
An arginine-lysine rich NLS could be predicted by software and spanned from amino acids 133 to 138 of VP2. The critical amino acids residues between positions 136 and 138, and either residue 133 or 134 are important for nuclear import in mammalian cells based on systematic mutagenesis. A NES is also predicted in VP2; however the results suggest that no functional NES is present and that this protein is CRM1 independent. It was also shown that VP2 is a chromatin binding protein and, notably, using a co-immunoprecipitation assay, it was found that VP2 association with MCM3 and that this interaction does not require DSP activity.
VP2 contains a NLS that span from amino acids 133 to 138. VP2 is a CRM1 independent protein during nuclear export and associates with MCM3 in cells.
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