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Updated: Jun 3, 2026

Modeling The Lifecycle Of Ebola Virus Under Biosafety Level 2 Conditions With Virus-like Particles Containing Tetracistronic Minigenomes
Published on: September 27, 2014
A new Ebola virus nonstructural glycoprotein expressed through RNA editing
Masfique Mehedi1, Darryl Falzarano, Jochen Seebach
1Department of Medical Microbiology, University of Manitoba, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Researchers identified a new Ebola virus (EBOV) glycoprotein, small soluble glycoprotein (ssGP), produced by transcriptional editing. This ssGP, distinct from sGP, is N-glycosylated and forms homodimers but lacks sGP's anti-inflammatory function.
Area of Science:
- Virology
- Molecular Biology
- Protein Biochemistry
Background:
- Ebola virus (EBOV) causes severe hemorrhagic fever.
- The EBOV glycoprotein (GP) gene undergoes transcriptional editing.
- A small soluble glycoprotein (ssGP) was postulated but not identified.
Purpose of the Study:
- To identify and characterize the expression of the putative ssGP.
- To determine the role of transcriptional editing in producing EBOV glycoproteins.
Main Methods:
- Analysis of GP gene-derived transcripts in vitro and in vivo.
- Optimized 2D gel electrophoresis for protein detection.
- Biochemical analysis of recombinant ssGP.
Main Results:
- ssGP transcripts constitute approximately 5% of GP gene products.
- ssGP expression and secretion were confirmed during EBOV infection.
- ssGP is an N-glycosylated, disulfide-linked homodimer.
Conclusions:
- A novel EBOV nonstructural glycoprotein, ssGP, is produced via GP gene transcriptional editing.
- ssGP shares structural similarities with sGP but lacks its anti-inflammatory properties.
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