Details

Autor(en) / Beteiligte

• Papageorgiou, Nicolas
• Baklouti, Amal
• Lichière, Julie
• Desmyter, Aline
• Canard, Bruno
• Coutard, Bruno
• Ferron, François

Titel

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

Ist Teil von

• Acta crystallographica. Section D, Biological crystallography., 2024-02, Vol.80 (2), p.113-122

Ort / Verlag

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

Erscheinungsjahr

2024

Quelle

Wiley Online Library - AutoHoldings Journals

Beschreibungen/Notizen

• 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. Structural rearrangement of the Toscana virus nucleoprotein is induced by a single‐chain camelid antibody.