The Ebola Virus Soluble Glycoprotein (sGP) Does Not Affect Lymphocyte Apoptosis and Adhesion to Activated Endothelium

Ebola virus infection is associated with the release of a soluble glycoprotein (sGP) from infected cells. The sGP has been proposed to modulate Ebola virus pathogenesis in primates but little is known about the role of this protein during infection and disease manifestation. So far sGP has been shown to revert the effect of tumor necrosis factor a (TNF-a) on endothelial permeability, indicating that the function of sGP might be antiinflammatory. Since bystander apoptosis of lymphocytes has been demonstrated in Ebola virus infections, we aimed to investigate the ability of sGP to modulate lymphocyte apoptosis and adhesion of lymphocytes to activated endothelium. Recombinant sGP alone or together with TNF-a and the death receptors TRAIL and FAS neither increased nor decreased apoptosis of Jurkat cells, a well-established human lymphocytic cell line. In addition, Jurkat cell adhesion to native or activated human umbilical vein endothelial cells was also found to be not altered by sGP. In 1976, Ebola virus (EBOV), a member of the family Filoviridae, emerged as the causative pathogen for one of the most severe forms of viral hemorrhagic fever (VHF) in humans and nonhuman primates. To date, there have been 2000 reported cases worldwide with resultin