Distribution of Hydrophobic Residues Is Crucial for the Fusogenic Properties of the Ebola Virus GP2 Fusion Peptide
AUTOR(ES)
Adam, B.
FONTE
American Society for Microbiology
RESUMO
The lipid-destabilizing properties of the N-terminal domain of the GP2 of Ebola virus were investigated. Our results suggest that the domain of Ebola virus needed for fusion is shorter than that previously reported. The fusogenic properties of this domain are related to its oblique orientation at the lipid/water interface owing to an asymmetric distribution of the hydrophobic residues when helical.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=369453Documentos Relacionados
- Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-Å resolution
- Phosphatidylinositol-Dependent Membrane Fusion Induced by a Putative Fusogenic Sequence of Ebola Virus
- Cloning and identification of bacteriophage T4 gene 2 product gp2 and action of gp2 on infecting DNA in vivo.
- The highly O-glycosylated glycoprotein gp2 of equine herpesvirus 1 is encoded by gene 71.
- Ectodomain shedding of the glycoprotein GP of Ebola virus