BST2/Tetherin Overexpression Modulates Morbillivirus Glycoprotein Production to Inhibit Cell-Cell Fusion.

Viruses
James T KellyDalan Bailey

Abstract

The measles virus (MeV), a member of the genus Morbillivirus, is an established pathogen of humans. A key feature of morbilliviruses is their ability to spread by virus-cell and cell-cell fusion. The latter process, which leads to syncytia formation in vitro and in vivo, is driven by the viral fusion (F) and haemagglutinin (H) glycoproteins. In this study, we demonstrate that MeV glycoproteins are sensitive to inhibition by bone marrow stromal antigen 2 (BST2/Tetherin/CD317) proteins. BST2 overexpression causes a large reduction in MeV syncytia expansion. Using quantitative cell-cell fusion assays, immunolabeling, and biochemistry we further demonstrate that ectopically expressed BST2 directly inhibits MeV cell-cell fusion. This restriction is mediated by the targeting of the MeV H glycoprotein, but not other MeV proteins. Using truncation mutants, we further establish that the C-terminal glycosyl-phosphatidylinositol (GPI) anchor of BST2 is required for the restriction of MeV replication in vitro and cell-cell fusion. By extending our study to the ruminant morbillivirus peste des petits ruminants virus (PPRV) and its natural host, sheep, we also confirm this is a broad and cross-species specific phenotype.

References

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Citations

Nov 7, 2019·Viruses·Marion FerrenCyrille Mathieu
Oct 16, 2020·The Journal of General Virology·Nazia ThakurDalan Bailey
Dec 23, 2020·International Journal of Molecular Sciences·Héloïse LeroySerge Benichou

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Methods Mentioned

BETA
PCR
transfection
Assay
transfections
flow cytometry
glycosylation
fluorescence

Software Mentioned

AlignX
Incucyte
Vector Nti package
GraphPad Prism

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