Expression of Ebolavirus glycoprotein on the target cells enhances viral entry

<p>Abstract</p> <p>Background</p> <p>Entry of Ebolavirus to the target cells is mediated by the viral glycoprotein GP. The native GP exists as a homotrimer on the virions and contains two subunits, a surface subunit (GP1) that is involved in receptor binding and a trans...

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Main Authors: Manicassamy Balaji, Rong Lijun
Format: Article
Language:English
Published: BMC 2009-06-01
Series:Virology Journal
Online Access:http://www.virologyj.com/content/6/1/75
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spelling doaj-14d742b8079b4c5c9f536ab53fd2aa042020-11-25T01:41:38ZengBMCVirology Journal1743-422X2009-06-01617510.1186/1743-422X-6-75Expression of Ebolavirus glycoprotein on the target cells enhances viral entryManicassamy BalajiRong Lijun<p>Abstract</p> <p>Background</p> <p>Entry of Ebolavirus to the target cells is mediated by the viral glycoprotein GP. The native GP exists as a homotrimer on the virions and contains two subunits, a surface subunit (GP1) that is involved in receptor binding and a transmembrane subunit (GP2) that mediates the virus-host membrane fusion. Previously we showed that over-expression of GP on the target cells blocks GP-mediated viral entry, which is mostly likely due to receptor interference by GP1.</p> <p>Results</p> <p>In this study, using a tetracycline inducible system, we report that low levels of GP expression on the target cells, instead of interfering, specifically enhance GP mediated viral entry. Detailed mapping analysis strongly suggests that the fusion subunit GP2 is primarily responsible for this novel phenomenon, here referred to as <it>trans </it>enhancement.</p> <p>Conclusion</p> <p>Our data suggests that GP2 mediated <it>trans </it>enhancement of virus fusion occurs via a mechanism analogous to eukaryotic membrane fusion processes involving specific <it>trans </it>oligomerization and cooperative interaction of fusion mediators. These findings have important implications in our current understanding of virus entry and superinfection interference.</p> http://www.virologyj.com/content/6/1/75
collection DOAJ
language English
format Article
sources DOAJ
author Manicassamy Balaji
Rong Lijun
spellingShingle Manicassamy Balaji
Rong Lijun
Expression of Ebolavirus glycoprotein on the target cells enhances viral entry
Virology Journal
author_facet Manicassamy Balaji
Rong Lijun
author_sort Manicassamy Balaji
title Expression of Ebolavirus glycoprotein on the target cells enhances viral entry
title_short Expression of Ebolavirus glycoprotein on the target cells enhances viral entry
title_full Expression of Ebolavirus glycoprotein on the target cells enhances viral entry
title_fullStr Expression of Ebolavirus glycoprotein on the target cells enhances viral entry
title_full_unstemmed Expression of Ebolavirus glycoprotein on the target cells enhances viral entry
title_sort expression of ebolavirus glycoprotein on the target cells enhances viral entry
publisher BMC
series Virology Journal
issn 1743-422X
publishDate 2009-06-01
description <p>Abstract</p> <p>Background</p> <p>Entry of Ebolavirus to the target cells is mediated by the viral glycoprotein GP. The native GP exists as a homotrimer on the virions and contains two subunits, a surface subunit (GP1) that is involved in receptor binding and a transmembrane subunit (GP2) that mediates the virus-host membrane fusion. Previously we showed that over-expression of GP on the target cells blocks GP-mediated viral entry, which is mostly likely due to receptor interference by GP1.</p> <p>Results</p> <p>In this study, using a tetracycline inducible system, we report that low levels of GP expression on the target cells, instead of interfering, specifically enhance GP mediated viral entry. Detailed mapping analysis strongly suggests that the fusion subunit GP2 is primarily responsible for this novel phenomenon, here referred to as <it>trans </it>enhancement.</p> <p>Conclusion</p> <p>Our data suggests that GP2 mediated <it>trans </it>enhancement of virus fusion occurs via a mechanism analogous to eukaryotic membrane fusion processes involving specific <it>trans </it>oligomerization and cooperative interaction of fusion mediators. These findings have important implications in our current understanding of virus entry and superinfection interference.</p>
url http://www.virologyj.com/content/6/1/75
work_keys_str_mv AT manicassamybalaji expressionofebolavirusglycoproteinonthetargetcellsenhancesviralentry
AT ronglijun expressionofebolavirusglycoproteinonthetargetcellsenhancesviralentry
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