AI Article Synopsis
- - Human parainfluenza virus type 2's phosphoprotein (P) is crucial for its polymerase function and can produce both P and accessory V proteins through a unique gene editing process.
- - The P protein contains a nuclear localization signal (NLS) that helps it enter the nucleus, while a nuclear export signal (NES) allows it to exit, with specific amino acid sequences for both signals identified.
- - The study shows that the movement of P protein between the nucleus and cytoplasm is vital for its role in viral polymerase activity, further inhibited by the drug leptomycin B.
Article Abstract
Human parainfluenza virus type 2 phosphoprotein (P) is an essential component of viral polymerase. The P gene encodes both P and accessory V proteins by a specific gene editing mechanism. Therefore, the N-terminal 164 amino acids of P protein are common to V protein. Interestingly, while P protein is located in the cytoplasm, V protein is found mainly in the nucleus. Using deletion mutants, we show the presence of a nuclear localization signal (NLS) in the P/V common domain, and a nuclear export signal (NES) in the C-terminal P specific region. The NLS region makes a complex with importin α5 or 7. In the presence of leptomycin B, P protein is retained in the nucleus, indicating that it contains a CRM1-dependent NES. We identified the NLS (PVKPRRKK) and the NES (IIELLKGLDL) using β-galactosidase fusion proteins. Moreover, nucleocytoplasmic shuttling of P protein appears to be important for efficient viral polymerase activity.
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| http://dx.doi.org/10.1016/j.virol.2018.12.005 | DOI Listing |
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