Original Publication Date: 15 February, 2017
Publication / Source: Future Virology
Authors: Xiangguo Qiu & Vinayakumar Siragam
Ebola virus (EBOV) is a member of the Filoviridae family, which comprises negative-sense, single-stranded RNA viruses with a genome size of approximately 19,000 base pairs. The EBOV genome encodes seven structural proteins with different functional roles in viral replication and host immune evasion (reviewed in ): the nucleoprotein (NP), polymerase cofactor (VP35), matrix protein (VP40), glycoprotein (GP), transcription activator (VP30), secondary matrix protein (VP24) and RNA polymerase (L). Among the seven genes, the EBOV gp gene gives rise to several distinct proteins. The predominant products of the GP gene, the soluble glycoprotein (sGP)/delta peptide (Δ-peptide) and the small soluble glycoprotein (ssGP) are generated through transcriptional editing. They are some of the most studied proteins due to their multifunctional but unclear role in EBOV pathogenesis. The sGP and ssGP are thought to influence the endothelial cell barrier function [2,3]. However, the mechanism by which these proteins affect barrier function is still unclear.