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

SASDVC8 – Hendra virus protein P/V/W PNT3 domain

Protein W
MWexperimental 21 kDa
MWexpected 15 kDa
VPorod 42 nm3
log I(s) 1.95×101 1.95×100 1.95×10-1 1.95×10-2
Protein W small angle scattering data  s, nm-1
ln I(s)
Protein W Guinier plot ln 1.95×101 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Protein W Kratky plot 1.104 0 √3 sRg
Dmax: 13.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Hendra virus protein P/V/W PNT3 domain Rg histogram Rg, nm
Synchrotron SAXS data from solutions of Hendra virus protein P/V/W PNT3 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 = 0.099 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.

Protein W (PNT3)
Mol. type   Protein
Organism   Hendra virus (isolate Horse/Autralia/Hendra/1994)
Olig. state   Monomer
Mon. MW   15.2 kDa
 
UniProt   P0C1C6 (200-310)
Sequence   FASTA