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Updated: May 31, 2026

Assembly and Purification of Prototype Foamy Virus Intasomes
Published on: March 19, 2018
Minimal size of prototype foamy virus integrase for nuclear localization
1Department of Biotechnology, Chung-Ang University, Ansung 456-756, South Korea.
Prototype foamy virus (PFV) integrase (IN) nuclear localization signals (NLS) were further analyzed. A larger 64 amino acid region (aa 289-352) in the C-terminal domain, with specific arginines and lysines, shows maximum karyophilicity.
Area of Science:
- Molecular Biology
- Virology
- Cell Biology
Background:
- Prototype foamy virus (PFV) integrase (IN) possesses a nuclear localization signal (NLS) within its C-terminal domain.
- Previous studies identified a 29 amino acid region (aa 306-334) containing basic residues as crucial for IN nuclear import.
Purpose of the Study:
- To further delineate the karyophilic determinants within the C-terminal domain of PFV integrase.
- To identify specific amino acid residues critical for nuclear localization.
Main Methods:
- Construction and transfection of plasmids expressing various mutants of the PFV IN C-terminal domain fused to MBP and EGFP.
- Subcellular localization analysis of fusion proteins in COS-1 cells using fluorescent microscopy.
Main Results:
- A 64 amino acid region (aa 289-352) demonstrated maximal karyophilicity, exceeding the previously identified 29 amino acid region.
- Specific residues, Arginine 341 and Lysine 349, were identified as critical determinants for this enhanced nuclear localization.
Conclusions:
- The C-terminal domain of PFV integrase contains a broader region responsible for nuclear import than previously defined.
- Key arginine and lysine residues within this extended region are essential for efficient nuclear localization of PFV integrase.
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