Dimerization of tetherin is not essential for its antiviral activity against Lassa and Marburg viruses.

• Main Authors: Toshie Sakuma, Akira Sakurai, Jiro Yasuda
• Format: Article
• Language: English
• Published: Public Library of Science (PLoS) 2009-01-01
• Series: PLoS ONE
• Online Access: http://europepmc.org/articles/PMC2735005?pdf=render

Tetherin (also known as BST2, CD317 or HM1.24) has recently been reported to inhibit a wide range of viruses. However, the antiviral mechanism of action of tetherin has not been determined. Both ends of the tetherin molecule are associated with the plasma membrane and it forms a homodimer. Therefore, a model in which progeny virions are retained on the cell surface by dimer formation between tetherin molecules on the viral envelope and plasma membrane has been proposed as the antiviral mechanism of action of this molecule. To investigate this possibility, we examined the correlation between dimerization and antiviral activity of tetherin in Lassa and Marburg virus-like particle production systems using tetherin mutants deficient in dimer formation. However, the tetherin mutant with complete loss of dimerization activity still showed apparent antiviral activity, indicating that dimerization of tetherin is not essential for its antiviral activity. This suggests that tetherin retains progeny virions on the cell surface by a mechanism other than dimerization.