Journal of General Virology

Biosynthesis and role of filoviral glycoproteins

Heinz Feldmann,¹ Viktor E. Volchkov,² Valentina A. Volchkova,² Ute Ströher³ and Hans-Dieter Klenk³

¹ Canadian Science Centre for Human and Animal Health, 1015 Arlington Street, Winnipeg, Manitoba, Canada R3E 3R2
² Biologie des Filovirus, Claude Bernard University Lyon-1, 46 Allée d'Italie, 69007 Lyon, France
³ Institut für Virologie, Philipps-Universität, Robert-Koch-Str. 17, D-35037 Marburg, Germany

Marburg and Ebola viruses cause systemic infections leading to severe haemorrhagic fever in human and non-human primates. There is evidence that the filovirus glycoproteins play an important role in cell tropism, the spread of infection and pathogenicity. Biosynthesis of the transmembrane glycoprotein involves a series of co- and post-translational events, including proteolytic cleavage by a host cell protease. Cleavage leads to two disulphide-linked subunits, GP₁ and GP₂, of which GP₂ anchors the molecule into the membrane. Although cleavage is not a requirement for Ebola virus infectivity in cell culture, the role of cleavage in vivo is unknown. Different strains of Ebola virus show variations in the cleavability of the glycoprotein that may account for differences in pathogenicity. Expression of the transmembrane glycoprotein of Ebola virus, but not of Marburg virus, requires transcriptional editing. Unedited transcripts yield the non-structural glycoprotein sGP, which is extensively secreted from infected cells. The role of the different soluble glycoproteins produced during filovirus infections is unknown, but they may interfere with the host immune response and other defence mechanisms.

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© 2001 SGM

This article is now available in the December 2001 print issue of JGV (vol. 82, 2839–2848). The complete issue of the journal may be seen in electronic form on JGV Online.