title: Insights into the coiled-coil organization of the Hendra virus phosphoprotein from combined biochemical and SAXS studies.
abstract: Nipah and Hendra viruses are recently emerged paramyxoviruses belonging to the Henipavirus genus. The Henipavirus phosphoprotein (P) consists of a large intrinsically disordered domain and a C-terminal domain (PCT) containing alternating disordered and ordered regions. Among these latter is the P multimerization domain (PMD). Using biochemical, analytical ultracentrifugation and small-angle X-ray scattering (SAXS) studies, we show that Hendra virus (HeV) PMD forms an elongated coiled-coil homotrimer in solution, in agreement with our previous findings on Nipah virus (NiV) PMD. However, the orientation of the N-terminal region differs from that observed in solution for NiV PMD, consistent with the ability of this region to adopt different conformations. SAXS studies provided evidence for a trimeric organization also in the case of PCT, thus extending and strengthening our findings on PMD. The present results are discussed in light of conflicting reports in the literature pointing to a tetrameric organization of paramyxoviral P proteins.
authors: Aix-Marseille University, Architecture et Fonction des Macromolécules Biologiques (AFMB) UMR 7257, 13288 Marseille, France; CNRS, AFMB UMR 7257, 13288 Marseille, France.
authors: Matilde
authors: M
authors: Beltrandi
authors: Aix-Marseille University, Architecture et Fonction des Macromolécules Biologiques (AFMB) UMR 7257, 13288 Marseille, France; CNRS, AFMB UMR 7257, 13288 Marseille, France.
authors: David
authors: D
authors: Blocquel
authors: Aix-Marseille University, Architecture et Fonction des Macromolécules Biologiques (AFMB) UMR 7257, 13288 Marseille, France; CNRS, AFMB UMR 7257, 13288 Marseille, France.
authors: Jenny
authors: J
authors: Erales
authors: Aix-Marseille University, INSERM, CRO2 UMR_S911, Faculté de Pharmacie, 13385 Marseille, France.
authors: Pascale
authors: P
authors: Barbier
authors: Institute for Research in Biomedicine, Via Vincenzo Vela 6, 6500 Bellinzona, Switzerland; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom. Electronic address: andrea.cavalli@irb.usi.ch.
authors: Andrea
authors: A
authors: Cavalli
authors: Aix-Marseille University, Architecture et Fonction des Macromolécules Biologiques (AFMB) UMR 7257, 13288 Marseille, France; CNRS, AFMB UMR 7257, 13288 Marseille, France. Electronic address: Sonia.Longhi@afmb.univ-mrs.fr.
authors: Sonia
authors: S
authors: Longhi
mesh_terms: D045404:Hendra Virus / Q000737:chemistry* / Q000502:physiology*; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D014461:Ultracentrifugation
chemical_list: D010750:Phosphoproteins
keywords: Coiled-coil; Cross-linking; Hendra virus; Henipavirus; Homotrimer; P multimerization domain; PMD; Phosphoprotein; Small-angle X-ray scattering