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Open Access Highly Accessed Research article

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 Cheng1, Shyang-Chwen Sheu2, Yi-Yang Lien3, Meng-Shiunn Lee4, His-Jien Chen5, Wen-Hong Su1 and Meng-Shiou Lee6*

Author Affiliations

1 Department of Medical Research, Chang Gung Memorial Hospital-Kaohsiung Medical Center, Chang Gung University College of Medicine, Kaohsiung, Taiwan

2 Department of Food Science, National Pingtung University of Science and Technology, Pingtung, Taiwan

3 Department of Veterinary Medicine, National Pingtung University of Science and Technology, Pingtung, Taiwan

4 Department of Medical Research, Tung's Taichung Metro Harbor Hospital, Taichung, Taiwan

5 Department of Safety, Health and Environmental Engineering, Mingchi University of Technology, Taipei, Taiwan

6 School of Chinese Pharmaceutical Science and Chinese Medicine Resources, China Medical University, Taichung, Taiwan

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BMC Veterinary Research 2012, 8:15  doi:10.1186/1746-6148-8-15

Published: 7 February 2012

Abstract

Background

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.

Results

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.

Conclusions

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.