Next Article in Journal
Platelet Count in Patients with Mild Disease at Admission is Associated with Progression to Severe Hantavirus Cardiopulmonary Syndrome
Next Article in Special Issue
Evolution of Attenuation and Risk of Reversal in Peste des Petits Ruminants Vaccine Strain Nigeria 75/1
Previous Article in Journal
Effects of the Q80K Polymorphism on the Physicochemical Properties of Hepatitis C Virus Subtype 1a NS3 Protease
Previous Article in Special Issue
Probing Morbillivirus Antisera Neutralization Using Functional Chimerism between Measles Virus and Canine Distemper Virus Envelope Glycoproteins
Article Menu

Export Article

Open AccessArticle

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

Viral Glycoproteins Group, The Pirbright Institute, Ash Rd, Guildford, Surrey GU24 0NF, UK
Institute of Immunology and Immunotherapy, The University of Birmingham, Birmingham B15 2TT, UK
Author to whom correspondence should be addressed.
Viruses 2019, 11(8), 692;
Received: 13 June 2019 / Revised: 16 July 2019 / Accepted: 20 July 2019 / Published: 30 July 2019
(This article belongs to the Special Issue Morbilliviruses)
PDF [2600 KB, uploaded 30 July 2019]


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. View Full-Text
Keywords: Morbillivirus; haemagluttinin; measles; PPRV; MeV; BST2; tetherin Morbillivirus; haemagluttinin; measles; PPRV; MeV; BST2; tetherin

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Kelly, J.T.; Human, S.; Alderman, J.; Jobe, F.; Logan, L.; Rix, T.; Gonçalves-Carneiro, D.; Leung, C.; Thakur, N.; Birch, J.; Bailey, D. BST2/Tetherin Overexpression Modulates Morbillivirus Glycoprotein Production to Inhibit Cell–Cell Fusion. Viruses 2019, 11, 692.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top