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The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

¹ Architecture et Fonction des Macromolé cules Biologiques (AFMB), UMR 6098 CNRS et Université s Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France
² Department Veterinary Biosciences, The Ohio State University, Columbus, Ohio 43210, USA
³ European Synchrotron Radiation Facility, BP 220, 38043 Grenoble Cedex, France

(RECEIVED February 14, 2005; FINAL REVISION May 9, 2005; ACCEPTED May 10, 2005)

Measles virus is a negative-sense, single-stranded RNA virus within theMononegavirales order,which includes several human pathogens, including rabies, Ebola, Nipah, and Hendra viruses. Themeasles virus nucleoprotein consists of a structured N-terminal domain, and of an intrinsically disordered C-terminal domain, N_TAIL (aa 401–525), which undergoes induced folding in the presence of the C-terminal domain (XD, aa 459–507) of the viral phosphoprotein. With in N_TAIL, an -helical molecular recognition element (-MoRE, aa 488–499) involved in binding to P and in induced folding was identified and then observed in the crystal structure of XD. Using small-angle X-ray scattering, we have derived a low-resolution structural model of the complex between XD and N_TAIL, which shows that most of N_TAIL remains disordered in the complex despite P-induced folding within the -MoRE. The model consists of an extended shape accommodating the multiple conformations adopted by the disordered N-terminal region of N_TAIL, and of a bulky globular region, corresponding to XD and to the C terminus of N_TAIL (aa 486–525). Using surface plasmon resonance, circular dichroism, fluorescence spectroscopy, and heteronuclear magnetic resonance, we show that N_TAIL has an additional site (aa 517–525) involved in binding to XD but not in the unstructured-to-structured transition. This work provides evidence that intrinsically disordered domains can establish complex interactions with their partners, and can contact them through multiple sites that do not all necessarily gain regular secondary structure.

Keywords: measles virus; nucleoprotein; phosphoprotein; intrinsic disorder; induced folding; NMR; CD; SAXS

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051411805.

Reprint requests to: Sonia Longhi, ESIL-CNRS-AFMB Case 925, 163, avenue de Luminy, 13288 Marseille Cedex 09, France; e-mail: longhi{at}afmb.cnrs-mrs.fr; fax: (33) 4-91-82-86-46.

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