Détail du document
Identifiant
oai:HAL:hal-02912888v1
Sujet
fluorescence anisotropy importin-α influenza nucleoprotein influenza-host interaction nuclear localization signal nuclear transport surface plasmon resonance [SDV.BBM.BS]Life Sciences [q-bio]/...Auteur
Donchet, Amélie Vassal-Stermann, Emilie Gérard, Francine Ruigrok, Rob W H Crépin, ThibautLangue
enEditeur
HAL CCSD;MDPI
Catégorie
sciences : sciences du vivant
Année
2020
Date de référencement
08/12/2023
Mots clés
importin-α viruses influenza importins-αRésumé
International audience; Influenza viruses are negative single-stranded RNA viruses with nuclear transcription and replication.
They enter the nucleus by using the cellular importin-α/-β 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-α identified as partners.
All interactions between NPTAILs and importins-α have high association and dissociation rates and present a distinct and specific behaviour.
D/NPTAIL interacts strongly with all importins-α while B/NPTAIL shows weak affinity for importins-α.
A/NPTAIL and C/NPTAIL present preferential importin-α partners.
Mutations in B/NPTAIL and D/NPTAIL show a loss of importin-α binding, confirming key NLS residues.
Taken together, our results provide essential highlights of this complex translocation mechanism.
Donchet, Amélie,Vassal-Stermann, Emilie,Gérard, Francine,Ruigrok, Rob W H,Crépin, Thibaut, 2020, Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-α, HAL CCSD;MDPI
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