Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-?.

ABSTRACT: Influenza viruses are negative single-stranded RNA viruses with nuclear transcription and replication. They enter the nucleus by using the cellular importin-?/-? nuclear import machinery. Influenza nucleoproteins from influenza A, B, C and D viruses possess a nuclear localization signal (NLS) localized on an intrinsically disordered extremity (NPTAIL). In this paper, using size exclusion chromatography (SEC), SEC-multi-angle laser light scattering (SEC-MALLS) analysis, surface plasmon resonance (SPR) and fluorescence anisotropy, we provide the first comparative study designed to dissect the interaction between the four NPTAILs and four importins-? identified as partners. All interactions between NPTAILs and importins-? have high association and dissociation rates and present a distinct and specific behaviour. D/NPTAIL interacts strongly with all importins-? while B/NPTAIL shows weak affinity for importins-?. A/NPTAIL and C/NPTAIL present preferential importin-? partners. Mutations in B/NPTAIL and D/NPTAIL show a loss of importin-? binding, confirming key NLS residues. Taken together, our results provide essential highlights of this complex translocation mechanism.

SUBMITTER: Donchet A 

PROVIDER: S-EPMC7472415 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature