Dimerization of tetherin is not essential for its antiviral activity against Lassa and Marburg viruses
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...
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| description | 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. |
| doi_str_mv | 10.1371/journal.pone.0006934 |
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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. 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This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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This suggests that tetherin retains progeny virions on the cell surface by a mechanism other than dimerization.</description><subject>Animals</subject><subject>Antigens</subject><subject>Antigens, CD - chemistry</subject><subject>Antiviral activity</subject><subject>Antiviral agents</subject><subject>Antiviral Agents - chemistry</subject><subject>Antiviral Agents - pharmacology</subject><subject>B cells</subject><subject>Bone marrow</subject><subject>Cell growth</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - virology</subject><subject>Cell surface</subject><subject>Cercopithecus aethiops</subject><subject>Chemical bonds</subject><subject>Cloning</subject><subject>COS Cells</subject><subject>Dimerization</subject><subject>Disulfides</subject><subject>Ebola virus</subject><subject>Filoviridae</subject><subject>Forensic sciences</subject><subject>Glycoproteins</subject><subject>GPI-Linked Proteins</subject><subject>Humans</subject><subject>Lassa virus - metabolism</subject><subject>Marburg virus disease</subject><subject>Marburgvirus - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sakuma, Toshie</au><au>Sakurai, Akira</au><au>Yasuda, Jiro</au><au>Schwartz, Olivier</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dimerization of tetherin is not essential for its antiviral activity against Lassa and Marburg viruses</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2009-09-09</date><risdate>2009</risdate><volume>4</volume><issue>9</issue><spage>e6934</spage><epage>e6934</epage><pages>e6934-e6934</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>19742323</pmid><doi>10.1371/journal.pone.0006934</doi><tpages>e6934</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antigens Antigens, CD - chemistry Antiviral activity Antiviral agents Antiviral Agents - chemistry Antiviral Agents - pharmacology B cells Bone marrow Cell growth Cell Membrane - metabolism Cell Membrane - virology Cell surface Cercopithecus aethiops Chemical bonds Cloning COS Cells Dimerization Disulfides Ebola virus Filoviridae Forensic sciences Glycoproteins GPI-Linked Proteins Humans Lassa virus - metabolism Marburg virus disease Marburgvirus - metabolism Membrane Glycoproteins - chemistry Models, Biological Multiple myeloma Mutants Mutation Offspring Particle production Plasmids - metabolism Progeny Proteins Viral infections Virion - metabolism Virions Virology Virology/Emerging Viral Diseases Virology/Host Antiviral Responses Virology/Virion Structure, Assembly, and Egress Viruses |
| title | Dimerization of tetherin is not essential for its antiviral activity against Lassa and Marburg viruses |
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