dimerization of tetherin is not essential for its antiviral activity against lassa and marburg viruses二聚tetherin不是必不可少的对拉沙热病毒和马尔堡病毒的抗病毒活性.pdfVIP

Dimerization of Tetherin Is Not Essential for Its Antiviral Activity against Lassa and Marburg Viruses Toshie Sakuma, Akira Sakurai, Jiro Yasuda* First Department of Forensic Science, National Research Institute of Police Science, Kashiwa, Japan Abstract 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. Citation: Sakuma T, Sakurai A, Yasuda J (2009) Dimerization of Tetherin Is Not Essential for Its Antiviral Activity against Lassa and Marburg Viruses. PLoS ONE 4(9): e6934. doi:10.1371/journal.pone.0006934 Editor: Olivier Schwartz, Institut Pasteur, France Received May 10, 2009; Accepted August 13, 2009; Published September 9, 2009 Copyright: 2009 Sakuma et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium,