The non-structural NS1 protein unique to respiratory syncytial virus: a two-state folding monomer in quasi-equilibrium with a stable spherical oligomer.

ABSTRACT: Human respiratory syncytial virus (hRSV) is a major infectious agent that cause pediatric respiratory disease worldwide. Considered one of the main virulence factors of hRSV, NS1 is known to suppress type I interferon response and signaling, thus favoring immune evasion. This, together with the fact that NS1 is unique to hRSV among paramyxoviruses, and that has no homology within databases, prompted us to investigate its conformational stability, equilibria and folding. Temperature cooperatively induces conformational changes leading to soluble spherical oligomers (NS1SOs) with amyloid-like or repetitive ß-sheet structures. The onset of the thermal transition is 45°C, and the oligomerization rate is increased by 25-fold from 40 to 46°C. Conformational stability analyzed by chemical perturb

SUBMITTER: Pretel E 

PROVIDER: S-EPMC3769240 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature