The glycoproteins of Marburg and Ebola virus and their potential roles in pathogenesis
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Updated: Oct 19, 2026

Modeling The Lifecycle Of Ebola Virus Under Biosafety Level 2 Conditions With Virus-like Particles Containing Tetracistronic Minigenomes
Published on: September 27, 2014
H Feldmann1, V E Volchkov, V A Volchkova
1Institut für Virologie, Philipps-Universität Marburg, Germany.
Abstract:
Filoviruses cause systemic infections that can lead to severe hemorrhagic fever in human and non-human primates. The primary target of the virus appears to be the mononuclear phagocytic system. As the virus spreads through the organism, the spectrum of target cells increases to include endothelial cells, fibroblasts, hepatocytes, and many other cells. There is evidence that the filovirus glycoprotein plays an important role in cell tropism, spread of infection, and pathogenicity. Biosynthesis of the glycoprotein forming the spikes on the virion surface involves cleavage by the host cell protease furin into two disulfide linked subunits GP1 and GP2. GP1 is also shed in soluble form from infected cells. Different strains of Ebola virus show variations in the cleavability of the glycoprotein, that may account for differences in pathogenicity, as has been observed with influenza viruses and paramyxoviruses. Expression of the spike glycoprotein of Ebola virus, but not of Marburg virus, requires transcriptional editing. Unedited GP mRNA yields the nonstructural glycoprotein sGP, which is secreted extensively from infected cells. Whether the soluble glycoproteins GP1 and sGP interfere with the humoral immune response and other defense mechanisms remains to be determined.
Insights
Filoviruses, like Ebola, cause severe hemorrhagic fever by infecting various cells. Their glycoprotein
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Filoviruses, including Ebola virus, cause severe systemic infections and hemorrhagic fever in humans and primates.
- The virus initially targets the mononuclear phagocytic system, then spreads to endothelial cells, fibroblasts, and hepatocytes.
- The filovirus glycoprotein is crucial for cell tropism, infection spread, and pathogenicity.
Purpose of the Study:
- To investigate the role of filovirus glycoprotein in cell tropism, infection spread, and pathogenicity.
- To explore the significance of glycoprotein cleavage by host cell protease furin.
- To understand the implications of transcriptional editing in Ebola virus glycoprotein expression.
Main Methods:
- Analysis of filovirus glycoprotein biosynthesis, including cleavage into GP1 and GP2 subunits by furin.
- Investigation of soluble glycoprotein shedding (GP1 and sGP) from infected cells.
- Comparative analysis of Ebola virus and Marburg virus glycoprotein expression, focusing on transcriptional editing.
Main Results:
- Filovirus glycoprotein cleavage by furin yields GP1 and GP2 subunits; GP1 is shed as a soluble form.
- Variations in glycoprotein cleavability among Ebola virus strains may correlate with pathogenicity differences.
- Ebola virus glycoprotein expression requires transcriptional editing, unlike Marburg virus; unedited mRNA produces secreted sGP.
Conclusions:
- The filovirus glycoprotein's structure, cleavage, and expression are critical factors in viral pathogenesis.
- Transcriptional editing plays a distinct role in Ebola virus glycoprotein expression compared to Marburg virus.
- The potential immunomodulatory effects of soluble glycoproteins GP1 and sGP require further investigation.
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