Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.

Scientific Reports
Max RennerCedric Leyrat

Abstract

The phosphoprotein (P) is the main and essential cofactor of the RNA polymerase (L) of non-segmented, negative-strand RNA viruses. P positions the viral polymerase onto its nucleoprotein-RNA template and acts as a chaperone of the nucleoprotein (N), thereby preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of human metapneumovirus (HMPV) forms homotetramers composed of a stable oligomerization domain (Pcore) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of Pcore with small angle x-ray scattering (SAXS)-based ensemble modeling of the full-length P protein and several of its fragments to provide a structural description of P that captures its dynamic character, and highlights the presence of varyingly stable structural elements within the IDRs. We discuss the implications of the structural properties of HMPV P for the assembly and functioning of the viral transcription/replication machinery.

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Citations

Apr 18, 2019·Proceedings of the National Academy of Sciences of the United States of America·Joshua A RibackTobin R Sosnick
Feb 12, 2020·Journal of Molecular Biology·Patricia L ClarkTobin R Sosnick
Apr 4, 2021·Viruses·Nicolás M S GálvezAlexis M Kalergis
Jul 17, 2021·PLoS Pathogens·De-Sheng KerAlfred A Antson

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Datasets Mentioned

BETA
AAK62966.1

Methods Mentioned

BETA
x-ray crystallography
x-ray scattering
X-ray
MDS
NMR
size exclusion chromatography
PISA

Software Mentioned

Jalview
PHASER
GROMACS
PHENIX
PRIMUS
LOMETS
PROMALS3D
flexible
CRYSOL
SCCOMP

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