Monomeric Structure of Influenza A Virus NEP/NS2 Obtained With an Artificial Protein Highlights Conformational Plasticity.

Stelfox AJ, Bessonne M, Bourhis JM, Erba EB, Albanese P, Compte DP, Nevers Q, Urvoas A, Valerio-Lepiniec M, Minard P, Ruigrok RWH, Crépin T, Delmas B, Ballandras-Colas A, J Mol Biol 437(24):169511 (2025) Europe PMC

SASDYY3 – Influenza A virus Nuclear export protein NEP/NS2

Nuclear export protein
MWexperimental 15 kDa
MWexpected 14 kDa
VPorod 24 nm3
log I(s) 1.51×10-2 1.51×10-3 1.51×10-4 1.51×10-5
Nuclear export protein small angle scattering data  s, nm-1
ln I(s)
Nuclear export protein Guinier plot ln 1.51×10-2 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Nuclear export protein Kratky plot 1.104 0 √3 sRg
p(r)
Nuclear export protein pair distance distribution function Rg: 1.9 nm 0 Dmax: 6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Nuclear export protein DAMMIN model
Synchrotron SAXS data from solutions of Influenza A virus Nuclear export protein NEP/NS2 in 20 mM HEPES, 300 mM NaCl, pH 7.5 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 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 15.00 μl sample at 6 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 20°C. 400 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.

Nuclear export protein (NEP)
Mol. type   Protein
Organism   Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Olig. state   Monomer
Mon. MW   14.3 kDa
 
UniProt   Q89733
Sequence   FASTA