Article
Ebola Virus Delta Peptide is a Viroporin
Journal of Virology
(2017)
Abstract
The Ebola virus (EBOV) genome encodes a partly conserved 40-residue nonstructural polypeptide, called the delta peptide, that is produced in abundance during Ebola virus disease (EVD). The function of the delta peptide is unknown, but sequence analysis has suggested that delta peptide could be a viroporin, belonging to a diverse family of membrane-permeabilizing small polypeptides involved in replication and pathogenesis of numerous viruses. Full-length and conserved C-terminal delta peptide fragments permeabilize the plasma membranes of nucleated cells of rodent, dog, monkey, and human origin; increase ion permeability across confluent cell monolayers; and permeabilize synthetic lipid bilayers. Permeabilization activity is completely dependent on the disulfide bond between the two conserved cysteines. The conserved C-terminal portion of the peptide is biochemically stable in human serum, and most serum-stable fragments have full activity. Taken together, the evidence strongly suggests that Ebola virus delta peptide is a viroporin and that it may be a novel, targetable aspect of Ebola virus disease pathology.
Keywords
- delta peptide,
- Ebola virus,
- enterotoxins,
- permeabilization,
- viroporin
Publication Date
August 15, 2017
DOI
10.1128/JVI.00438-17
Citation Information
Jing He, Lilia I. Melnik, Alexander Komin, Gregory Wiedman, et al.. "Ebola Virus Delta Peptide is a Viroporin" Journal of Virology Vol. 91 Iss. 16 (2017) ISSN: 1098-5514 Available at: http://works.bepress.com/gregory-wiedman/27/