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Viruses 2015, 7(1), 285-305; doi:10.3390/v7010285

Modeling of the Ebola Virus Delta Peptide Reveals a Potential Lytic Sequence Motif

1
Mockingbird Nature Research Group, PO Box 568, Pearl River, LA 70452, USA
2
Department of Microbiology, Immunology & Parasitology, Louisiana State University Health Sciences Center, 1901 Perdido Street, New Orleans, LA 70112, USA
3
Department of Microbiology and Immunology, Tulane University Medical Center, 1430 Tulane Avenue, New Orleans, LA 70112, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Jens H. Kuhn
Received: 1 December 2014 / Revised: 12 January 2015 / Accepted: 16 January 2015 / Published: 20 January 2015
(This article belongs to the Collection Advances in Ebolavirus, Marburgvirus, and Cuevavirus Research)
View Full-Text   |   Download PDF [1198 KB, uploaded 12 May 2015]   |  

Abstract

Filoviruses, such as Ebola and Marburg viruses, cause severe outbreaks of human infection, including the extensive epidemic of Ebola virus disease (EVD) in West Africa in 2014. In the course of examining mutations in the glycoprotein gene associated with 2014 Ebola virus (EBOV) sequences, a differential level of conservation was noted between the soluble form of glycoprotein (sGP) and the full length glycoprotein (GP), which are both encoded by the GP gene via RNA editing. In the region of the proteins encoded after the RNA editing site sGP was more conserved than the overlapping region of GP when compared to a distant outlier species, Tai Forest ebolavirus. Half of the amino acids comprising the “delta peptide”, a 40 amino acid carboxy-terminal fragment of sGP, were identical between otherwise widely divergent species. A lysine-rich amphipathic peptide motif was noted at the carboxyl terminus of delta peptide with high structural relatedness to the cytolytic peptide of the non-structural protein 4 (NSP4) of rotavirus. EBOV delta peptide is a candidate viroporin, a cationic pore-forming peptide, and may contribute to EBOV pathogenesis. View Full-Text
Keywords: Ebola; ebolavirus; filovirus; lysin; viroporin; enterotoxin; ion channel Ebola; ebolavirus; filovirus; lysin; viroporin; enterotoxin; ion channel
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Gallaher, W.R.; Garry, R.F. Modeling of the Ebola Virus Delta Peptide Reveals a Potential Lytic Sequence Motif. Viruses 2015, 7, 285-305.

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