Related Experiment Video
Updated: Jun 20, 2026

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
Published on: January 9, 2019
Proteomics computational analyses suggest that the bornavirus glycoprotein is a class III viral fusion protein (gamma
Courtney E Garry1, Robert F Garry
1Department of Microbiology and Immunology, Tulane University Heath Sciences Center, New Orleans, Louisiana 70112, USA. cgarry@gmail.com
Background:
Borna disease virus (BDV) is the type member of the Bornaviridae, a family of viruses that induce often fatal neurological diseases in horses, sheep and other animals, and have been proposed to have roles in certain psychiatric diseases of humans. The BDV glycoprotein (G) is an extensively glycosylated protein that migrates with an apparent molecular mass of 84,000 to 94,000 kilodaltons (kDa). BDV G is post-translationally cleaved by the cellular subtilisin-like protease furin into two subunits, a 41 kDa amino terminal protein GP1 and a 43 kDa carboxyl terminal protein GP2.
Results:
Class III viral fusion proteins (VFP) encoded by members of the Rhabdoviridae, Herpesviridae and Baculoviridae have an internal fusion domain comprised of beta sheets, other beta sheet domains, an extended alpha helical domain, a membrane proximal stem domain and a carboxyl terminal anchor. Proteomics computational analyses suggest that the structural/functional motifs that characterize class III VFP are located collinearly in BDV G. Structural models were established for BDV G based on the post-fusion structure of a prototypic class III VFP, vesicular stomatitis virus glycoprotein (VSV G).
Conclusion:
These results suggest that G encoded by members of the Bornavirdae are class III VFPs (gamma-penetrenes).
Related Concept Videos
Retroviruses
Inhibitors of Virion Maturation and Assembly
Leaky Scanning
Viral Structure
Retrovirus Life Cycles

