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Release of immunomodulatory Ebola virus glycoprotein-containingmicrovesicles is suppressed by tetherin in a species-specific manner.
Cell Rep. 26, 1841-1853.e6 (2019)
The Ebola virus glycoprotein (EBOV-GP) forms GP-containing microvesicles, so-called virosomes, which are secreted from GP-expressing cells. However, determinants of GP-virosome release and their functionality are poorly understood. We characterized GP-mediated virosome formation and delineated the role of the antiviral factor tetherin (BST2, CD317) in this process. Residues in the EBOV-GP receptor-binding domain (RBD) promote GP-virosome secretion, while tetherin suppresses GP-virosomes by interactions involving the GP-transmembrane domain. Tetherin from multiple species interfered with GP-virosome release, and tetherin from the natural fruit bat reservoir showed the highest inhibitory activity. Moreover, analyses of GP from various ebo-lavirus strains, including the EBOV responsible for the West African epidemic, revealed the most efficient GP-virosome formation by highly pathogenic ebolaviruses. Finally, EBOV-GP-virosomes were immunomodulatory and acted as decoys for EBOV-neutralizing antibodies. Our results indicate that GP-virosome formation might be a determinant of EBOV immune evasion and pathogenicity, which is suppressed by tetherin.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Ebola Virus ; Antiviral Immune Response ; Exosome ; Glycoprotein ; Immune Evasion ; Immune Modulation ; Microvesicles ; Neutralizing Antibody ; Tetherin ; Virosome; Filovirus Glycoproteins; Hiv-1 Release; Cell-surface; Life-cycle; Protein; Entry; Infection; Binding; Pathogenesis; Restriction
ISSN (print) / ISBN
2211-1247
e-ISSN
2211-1247
Journal
Cell Reports
Quellenangaben
Volume: 26,
Issue: 7,
Pages: 1841-1853.e6
Publisher
Cell Press
Publishing Place
50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Virology (VIRO)