Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein.

Rawlinson SM, Chakraborty S, Sethi A, David CT, Harrison AR, Bird LE, Rozario AM, Uthishtran S, Ardipradja K, Zhao T, Oksayan S, Jans DA, Ang CS, Lu ZH, Yan F, Williamson NA, Arumugam S, Sundaramoorthy V, Bell TDM, Gooley PR, Moseley GW, Nat Commun 16(1):9491 (2025) Europe PMC

SASDRB6 – Rabies CVS Phosphoprotein (P1)

Phosphoprotein
MWexperimental 65 kDa
MWexpected 67 kDa
VPorod 230 nm3
log I(s) 1.81×10-2 1.81×10-3 1.81×10-4 1.81×10-5
Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein Guinier plot ln 1.81×10-2 Rg: 4.7 nm 0 (4.7 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoprotein Kratky plot 1.104 0 3 sRg
Dmax: 25 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Rabies CVS Phosphoprotein (P1) Rg histogram Rg, nm
Phosphoprotein EOM/RANCH model
Phosphoprotein EOM/RANCH model
Phosphoprotein EOM/RANCH model
Phosphoprotein EOM/RANCH model
Phosphoprotein EOM/RANCH model
Phosphoprotein EOM/RANCH model

Synchrotron SAXS data from solutions of rabies CVS phosphoprotein (P1) in 25 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 3.3 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superose 6 5/150 column at 22°C. Twenty three 1 second frames were collected through the SEC elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Phosphoprotein (CVS P1)
Mol. type   Protein
Organism   Rabies virus (strain CVS-11)
Olig. state   Dimer
Mon. MW   33.7 kDa
 
UniProt   P22363 (1-297)
Sequence   FASTA