Unraveling the molecular grammar and the structural transitions underlying the fibrillation of a viral fibrillogenic domain.

Gondelaud F, Leval J, Arora L, Walimbe A, Bignon C, Ptchelkine D, Brocca S, Mukhopadyay S, Longhi S, Protein Sci 34(3):e70068 (2025) Europe PMC

SASDVE8 – Hendra virus protein P/V/W PNT3 high-K domain

Protein W (artificial PNT3 variant - high-kappa)
MWexperimental 23 kDa
MWexpected 15 kDa
VPorod 54 nm3
log I(s) 1.10×100 1.10×10-1 1.10×10-2 1.10×10-3
Protein W (artificial PNT3 variant - high-kappa) small angle scattering data  s, nm-1
ln I(s)
Protein W (artificial PNT3 variant - high-kappa) Guinier plot ln 1.10×100 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Protein W (artificial PNT3 variant - high-kappa) Kratky plot 1.104 0 3 sRg
Dmax: 14.7 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Hendra virus protein P/V/W PNT3 high-K domain Rg histogram Rg, nm

Synchrotron SAXS data from solutions of Hendra virus protein P/V/W PNT3 high-K domain in 20 mM HEPES, 150 mM NaCl, pH 7.2 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.133 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 0.30 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 20°C. 600 successive 0.990 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

50 µl were injected on a BioSec 3-300 at 0.3 ml/min in HBS

Protein W (artificial PNT3 variant - high-kappa) (PNT3 high K)
Mol. type   Protein
Organism   Hendra virus (isolate Horse/Autralia/Hendra/1994)
Olig. state   Monomer
Mon. MW   15.2 kDa
Sequence   FASTA