Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody - Archive ouverte HAL Access content directly
Journal Articles Acta crystallographica Section D : Structural biology [1993-...] Year : 2024

Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody

Abstract

Phenuiviridae nucleoprotein is the main structural and functional component of the viral cycle, protecting the viral RNA and mediating the essential replication/transcription processes. The nucleoprotein (N) binds the RNA using its globular core and polymerizes through the N-terminus, which is presented as a highly flexible arm, as demonstrated in this article. The nucleoprotein exists in an `open' or a `closed' conformation. In the case of the closed conformation the flexible N-terminal arm folds over the RNA-binding cleft, preventing RNA adsorption. In the open conformation the arm is extended in such a way that both RNA adsorption and N polymerization are possible. In this article, single-crystal X-ray diffraction and small-angle X-ray scattering were used to study the N protein of Toscana virus complexed with a single-chain camelid antibody (VHH) and it is shown that in the presence of the antibody the nucleoprotein is unable to achieve a functional assembly to form a ribonucleoprotein complex.
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hal-04416977 , version 1 (25-01-2024)

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Nicolas Papageorgiou, Amal Baklouti, Julie Lichière, Aline Desmyter, Bruno Canard, et al.. Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody. Acta crystallographica Section D : Structural biology [1993-..], 2024, 80 (2), ⟨10.1107/S2059798324000196⟩. ⟨hal-04416977⟩
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