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Default Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.

Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.

Related Articles Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.

Angew Chem Int Ed Engl. 2020 Nov 18;:

Authors: Jirasko V, Lends A, Lakomek NA, Fogeron ML, Weber M, Malär A, Penzel S, Bartenschlager R, Meier BH, Böckmann A

Abstract
The Hepatitis C virus nonstructural protein 5A (NS5A) is a membrane-associated protein involved in multiple steps of the viral life cycle. Direct-acting antivirals (DAAs) targeting NS5A are a cornerstone of antiviral therapy, but the mode-of-action of these drugs is poorly understood. This is due to the lack of information on the membrane-bound NS5A structure. Here we present the structural model of an NS5A AH-linker-D1 protein reconstituted as proteoliposomes. We use highly sensitive proton-detected solid-state NMR methods suitable to study samples generated*via*synthetic biology approaches. Spectra analyses disclose that both the AH membrane anchor and the linker are highly flexible. Paramagnetic relaxation enhancements (PRE) reveal that the dimer organization in lipids requires a new type of NS5A self-interaction not reflected in previous crystal structures. In conclusion, we provide the*first characterization*of NS5A AH-linker-D1 in a lipidic environment shedding light onto the mode-of-action of clinically used NS5A inhibitors.


PMID: 33205864 [PubMed - as supplied by publisher]



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