Ebola Virus Delta Peptide Is a Viroporin
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Aug 15, 2017
- Source ID
- 10.1128/jvi.00438-17
Entities
People
- Alexander Komin
- Cameron F. Morris
- Charles G. Starr
- Gregory Wiedman
- Jing He
- Kalina Hristova
- Lilia I. Melnik
- Peter C. Searson
- Robert F. Garry
- Taylor Fuselier
- William C. Wimley
- William R. Gallaher
Organizations
- Defense Threat Reduction Agency
- Johns Hopkins University
- LSU Health Sciences Center New Orleans
- National Institutes of Health
- National Science Foundation
- Tulane University of Louisiana