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Journal of Virology, February 2009, p. 1837-1844, Vol. 83, No. 4
0022-538X/09/$08.00+0     doi:10.1128/JVI.02211-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Broad-Spectrum Inhibition of Retroviral and Filoviral Particle Release by Tetherin{triangledown}

Nolwenn Jouvenet,1 Stuart J. D. Neil,1,{dagger} Maria Zhadina,1 Trinity Zang,1 Zerina Kratovac,1 Youngnam Lee,1 Matthew McNatt,1 Theodora Hatziioannou,1 and Paul D. Bieniasz1,2*

Aaron Diamond AIDS Research Center and the Rockefeller University,1 Howard Hughes Medical Institute, New York, New York2

Received 19 October 2008/ Accepted 14 November 2008

The expression of many putative antiviral genes is upregulated when cells encounter type I interferon (IFN), but the actual mechanisms by which many IFN-induced gene products inhibit virus replication are poorly understood. A recently identified IFN-induced antiretroviral protein, termed tetherin (previously known as BST-2 or CD317), blocks the release of nascent human immunodeficiency virus type 1 (HIV-1) particles from infected cells, and an HIV-1 accessory protein, Vpu, acts as a viral antagonist of tetherin. Here, we show that tetherin is capable of blocking not only the release of HIV-1 particles but also the release of particles assembled using the major structural proteins of a variety of prototype retroviruses, including members of the alpharetrovirus, betaretrovirus, deltaretrovirus, lentivirus, and spumaretrovirus families. Moreover, we show that the release of particles assembled using filovirus matrix proteins from Marburg virus and Ebola virus is also sensitive to inhibition by tetherin. These findings indicate that tetherin is a broadly specific inhibitor of enveloped particle release, and therefore, inhibition is unlikely to require specific interactions with viral proteins. Nonetheless, tetherin colocalized with nascent virus-like particles generated by several retroviral and filoviral structural proteins, indicating that it is present at, or recruited to, sites of particle assembly. Overall, tetherin is potentially active against many enveloped viruses and likely to be an important component of the antiviral innate immune defense.

* Corresponding author. Mailing address: Aaron Diamond AIDS Research Center, 455 First Avenue, New York, NY 10016. Phone: (212) 448-5070. Fax: (212) 725-1126. E-mail: pbienias{at}adarc.org

{triangledown} Published ahead of print on 26 November 2008.

{dagger} Present address: Department of Infectious Disease, King's College London, Guy's Hospital, London, United Kingdom.

Journal of Virology, February 2009, p. 1837-1844, Vol. 83, No. 4
0022-538X/09/$08.00+0     doi:10.1128/JVI.02211-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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