The glycoprotein of vesicular stomatitis virus promotes release of virus-like particles from tetherin-positive cells.

The glycoprotein of vesicular stomatitis virus promotes release of virus-like particles from tetherin-positive cells.

PLoS One. 2017;12(12):e0189073

Authors: Brinkmann C, Hoffmann M, Lübke A, Nehlmeier I, Krämer-Kühl A, Winkler M, Pöhlmann S

Abstract
Vesicular stomatitis virus (VSV) release from infected cells is inhibited by the interferon (IFN)-inducible antiviral host cell factor tetherin (BST-2, CD317). However, several viruses encode tetherin antagonists and it is at present unknown whether residual VSV spread in tetherin-positive cells is also promoted by a virus-encoded tetherin antagonist. Here, we show that the viral glycoprotein (VSV-G) antagonizes tetherin in transfected cells, although with reduced efficiency as compared to the HIV-1 Vpu protein. Tetherin antagonism did not involve alteration of tetherin expression and was partially dependent on a GXXXG motif in the transmembrane domain of VSV-G. However, mutation of the GXXXG motif did not modulate tetherin sensitivity of infectious VSV. These results identify VSV-G as a tetherin antagonist in transfected cells but fail to provide evidence for a contribution of tetherin antagonism to viral spread.

PMID: 29216247 [PubMed - in process]

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