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Nehls, J. ; Businger, R.* ; Hoffmann, M.* ; Brinkmann, C.* ; Fehrenbacher, B.* ; Schaller, M.* ; Maurer, B.* ; Schönfeld, C.* ; Kramer, D.* ; Hailfinger, S.* ; Pöhlmann, S.* ; Schindler, M.

Release of immunomodulatory Ebola virus glycoprotein-containingmicrovesicles is suppressed by tetherin in a species-specific manner.

Cell Rep. 26, 1841-1853.e6 (2019)
Publ. Version/Full Text Research data DOI PMC
Open Access Gold
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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
Language english
Publication Year 2019
HGF-reported in Year 2019
ISSN (print) / ISBN 2211-1247
e-ISSN 2211-1247
Journal Cell Reports
Quellenangaben Volume: 26, Issue: 7, Pages: 1841-1853.e6 Article Number: , Supplement: ,
Publisher Cell Press
Publishing Place 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Reviewing status Peer reviewed
Institute(s) Institute of Virology (VIRO)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Immune Response and Infection
PSP Element(s) G-502700-006
DOI 10.1016/j.celrep.2019.01.065
WOS ID WOS:000458403600015
Scopus ID 85061144429
PubMed ID 30759394
Erfassungsdatum 2019-03-13
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