Back to Search
Start Over
Identification of nuclear localization signal and nuclear export signal of VP1 from the chicken anemia virus and effects on VP2 shuttling in cells
- Source :
- Virology Journal, Vol 16, Iss 1, Pp 1-9 (2019), Virology Journal
- Publication Year :
- 2019
- Publisher :
- Springer Science and Business Media LLC, 2019.
-
Abstract
- Background VP1 of the chicken anemia virus (CAV) is a structural protein that is required for virus encapsulation. VP1 proteins are present both in the nucleus and cytoplasm; however, the functional nuclear localization signal (NLS) and nuclear export signal (NES) of VP1 are still unknown. This study aimed to characterize the NLS and NES motifs of VP1 using bioinformatics methods and multiple-site fragment deletions, and investigate shuttling of VP2 from nucleus to cytoplasm by co-transfection with VP1. Methods Two putative NLS motifs were predicted by the WoLF PSORT and NLStradamus programs from the amino acid sequence of VP1. Three NES motifs of VP1 were predicted by the NetNES 1.1 Server and ELM server programs. All mutants were created by multiple-site fragment deletion mutagenesis. VP1 and VP2 were co-expressed in cells using plasmid transfection. Results A functional NLS motif was identified at amino acid residues 3 to 10 (RRARRPRG) of VP1. Critical amino acids 3 to 10 were significantly involved in nuclear import in cells and were evaluated using systematic deletion mutagenesis. Three NES motifs of VP1 were predicted by the NetNES 1.1 Server and ELM server programs. A functional NES was identified at amino acid residues 375 to 388 (ELDTNFFTLYVAQ). Leptomycin B (LMB) treatment demonstrated that VP1 export from nucleus to cytoplasm occurred through a chromosome region maintenance 1 (CRM1)-dependent pathway. With co-expression of VP1 and VP2 in cells, we observed that VP1 may transport VP2 from nucleus to cytoplasm. Conclusion Our data showed that VP1 of CAV contained functional NLS and NES motifs that modulated nuclear import and export through a CRM1-dependent pathway. Further, VP1 may play a role in the transport of VP2 from nucleus to cytoplasm.
- Subjects :
- 0301 basic medicine
Cytoplasm
viruses
Amino Acid Motifs
Nuclear Localization Signals
Receptors, Cytoplasmic and Nuclear
environment and public health
0302 clinical medicine
Peptide sequence
chemistry.chemical_classification
virus diseases
VP1
VP2
Cell biology
Amino acid
Protein Transport
Infectious Diseases
Fatty Acids, Unsaturated
030211 gastroenterology & hepatology
Protein Binding
Active Transport, Cell Nucleus
CHO Cells
Karyopherins
Biology
Transfection
lcsh:Infectious and parasitic diseases
03 medical and health sciences
Cricetulus
Nuclear localization signal
Virology
Animals
NLS
lcsh:RC109-216
Nuclear export signal
Cell Nucleus
Nuclear Export Signals
Research
CRM1-dependent pathway
Computational Biology
biochemical phenomena, metabolism, and nutrition
030104 developmental biology
chemistry
Mutagenesis
Capsid Proteins
Nuclear transport
Chicken anemia virus
PSORT
Nuclear localization sequence
Subjects
Details
- ISSN :
- 1743422X
- Volume :
- 16
- Database :
- OpenAIRE
- Journal :
- Virology Journal
- Accession number :
- edsair.doi.dedup.....6f611d6a20a780933f7ba986f2f1d2af