Regulation of measles virus gene expression by P protein coiled-coil properties

Louis Marie Bloyet, Antoine Schramm, Carine Lazert, Bertrand Raynal, Maggy Hologne, Olivier Walker, Sonia Longhi, Denis Gerlier

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25 Scopus citations


The polymerase of negative-stranded RNA viruses consists of the large protein (L) and the phosphoprotein (P), the latter serving both as a chaperon and a cofactor for L. We mapped within measles virus (MeV) P the regions responsible for binding and stabilizing L and showed that the coiled-coil multimerization domain (MD) of P is required for gene expression. MeV MD is kinked as a result of the presence of a stammer. Both restoration of the heptad regularity and displacement of the stammer strongly decrease or abrogate activity in a minigenome assay. By contrast, P activity is rather tolerant of substitutions within the stammer. Single substitutions at the "a" or "d" hydrophobic anchor positions with residues of variable hydrophobicity revealed that P functionality requires a narrow range of cohesiveness of its MD. Results collectively indicate that, beyond merely ensuring P oligomerization, the MD finely tunes viral gene expression through its cohesiveness.

Original languageEnglish
Article numbereaaw3702
JournalScience Advances
Issue number5
StatePublished - 2019


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