Abstract
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-localizes 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.
Highlights
Measles virus is a human virus that, the vaccine is very efficient, still kills about 100,000 people per year (Laksono et al, 2018; WHO, 2019)
The only known structure of L of the viruses of Mononegavirales order, to which paramyxoviruses belong, is the one from vesicular stomatitis virus (VSV) (Rahmeh et al, 2010; Liang et al, 2015; Qiu et al, 2016), and several reviews have used this structure as a model for the function and structure of measles virus L (Sourimant and Plemper, 2016; Fearns and Plemper, 2017)
This review describes recent results on the phosphoprotein (P) and nucleoprotein (N) of measles virus
Summary
Université Grenoble Alpes, Le Centre National de la Recherche Scientifique, Commissariatá l’Energie Atomique et aux Energies Alternatives, Institut de Biologie Structurale, Grenoble, France. 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. 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
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