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Review ARTICLE Provisionally accepted The full-text will be published soon. Notify me

Front. Microbiol. | doi: 10.3389/fmicb.2019.01832

The nucleoprotein and phosphoprotein of measles virus.

  • 1Université Grenoble Alpes, France
  • 2Centre National de la Recherche Scientifique, Grenoble, France
  • 3CEA Grenoble, France

Measles virus is a negative strand virus and the genomic and antigenomic RNA binds to the nucleoprotein (N), assembling into a helical nucleocapsid. The polymerase complex comprises two proteins, the Large protein (L), that both polymerizes RNA and caps the mRNA, and the phosphoprotein (P) that co-locallises with L on the nucleocapsid. This review presents recent results about N and P, in particular concerning their intrinsically disordered domains. N is a protein of 525 residues with a 120 amino acid disordered C-terminal domain, Ntail. The first 50 residues of Ntail extricate the disordered chain from the nucleocapsid, thereby loosening the otherwise rigid structure, and the C-terminus contains a linear motif that binds P. Recent results show how the 5’ end of the viral RNA binds to N within the nucleocapsid and also show that the bases at the 3’ end of the RNA are rather accessible to the viral polymerase. P is a tetramer and most of the protein is disordered; comprising 507 residues of which around 380 are disordered. The first 37 residues of P bind N, chaperoning against non-specific interaction with cellular RNA, while a second interaction site, around residue 200 also binds N. In addition, there is another interaction between C-terminal domain of P (XD) and Ntail. These results allow us to propose a new model of how the polymerase binds to the nucleocapsid and suggests a mechanism for initiation of transcription.

Keywords: Measles, nucleoprotein, Phosphoprotein, cryo-EM, NMR, X-ray crystallogaphy, RNA binding

Received: 14 Mar 2019; Accepted: 25 Jul 2019.

Edited by:

Mathilde Richard, Erasmus Medical Center, Netherlands

Reviewed by:

Sara Louise Cosby, Agri-Food and Biosciences Institute (AFBI), United Kingdom
Richard K. Plemper, Georgia State University, United States  

Copyright: © 2019 Guseva, Milles, Blackledge and Ruigrok. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence:
Dr. Martin Blackledge, CEA Grenoble, Grenoble, 38000, Rhône-Alpes, France,
Prof. Rob W. Ruigrok, Université Grenoble Alpes, Saint Martin d'Hères, France,