Accéder directement au contenu Accéder directement à la navigation
Article dans une revue

Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution

Abstract : Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a significant public health problem in Southeast Asia. Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part of the heparin sulfate receptor binding region that drives the dengue virus (DENV)’s fusion with the host cell. Here, we used high-hydrostatic-pressure nuclear magnetic resonance (HHP-NMR) to obtain residue-specific information on the folding process of domain III from serotype 4 dengue virus (DEN4-ED3), which adopts the classical three-dimensional (3D) ß-sandwich structure known as the Ig-like fold. Interestingly, the folding pathway of DEN4-ED3 shares similarities with that of the Titin I27 module, which also adopts an Ig-like fold, but is functionally unrelated to ED3. For both proteins, the unfolding process starts by the disruption of the N- and C-terminal strands on one edge of the ß-sandwich, yielding a folding intermediate stable over a substantial pressure range (from 600 to 1000 bar). In contrast to this similarity, pressure-jump kinetics indicated that the folding transition state is considerably more hydrated in DEN4-ED3 than in Titin I27.
Type de document :
Article dans une revue
Liste complète des métadonnées

https://hal.umontpellier.fr/hal-03472289
Contributeur : Philippe BARTHE Connectez-vous pour contacter le contributeur
Soumis le : mardi 31 mai 2022 - 13:56:40
Dernière modification le : jeudi 9 juin 2022 - 15:35:57

Fichier

biomolecules-09-00309.pdf
Fichiers éditeurs autorisés sur une archive ouverte

Licence


Distributed under a Creative Commons Paternité 4.0 International License

Identifiants

Collections

Citation

Tomonori Saotome, Maxime Doret, Manjiri Kulkarni, yin-Shan yang, Philippe Barthe, et al.. Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution. Biomolecules, MDPI, 2019, 9 (8), pp.309. ⟨10.3390/biom9080309⟩. ⟨hal-03472289⟩

Partager

Métriques

Consultations de la notice

0

Téléchargements de fichiers

0