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

SASDVD8 – Hendra virus protein P/V/W PNT3 low-K domain

Protein W (artificial PNT3 variant - low-kappa)
MWexperimental 19 kDa
MWexpected 15 kDa
VPorod 48 nm3
log I(s) 2.80×10-2 2.80×10-3 2.80×10-4 2.80×10-5
Protein W (artificial PNT3 variant - low-kappa) small angle scattering data  s, nm-1
ln I(s)
Protein W (artificial PNT3 variant - low-kappa) Guinier plot ln 2.80×10-2 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Protein W (artificial PNT3 variant - low-kappa) Kratky plot 1.104 0 3 sRg
Dmax: 18 nm

Data validation


Fits and models


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

Synchrotron SAXS data from solutions of Hendra virus protein P/V/W PNT3 low-K domain in 20 mM HEPES, 150 mM NaCl, pH 7.2 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.0992 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 45.00 μl sample at 5 mg/ml was injected at a 0.30 ml/min flow rate onto a Agilent AdvanceBio SEC 2.7 µm - 130 Å column at 20°C. 600 successive 1 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.

45 µl were injected on a BioSec 3-300 at a flow rate of 0.3 ml/min in HBS

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