Ebola virus delta peptide is a viroporin

Jing He, Lilia I. Melnik, Alexander Komin, Gregory Wiedman, Taylor Fuselier, Cameron F. Morris, Charles G. Starr, Peter C. Searson, William R. Gallaher, Kalina Hristova, Robert F. Garry, William C. Wimley

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


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.

Original languageEnglish (US)
Article numbere00438-17
JournalJournal of virology
Issue number16
StatePublished - Aug 1 2017


  • Delta peptide
  • Ebola virus
  • Enterotoxins
  • Permeabilization
  • Viroporin

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology


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