J Gen Virol Try IJSEM Online
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 87 (2006), 3029-3037; DOI 10.1099/vir.0.82035-0

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Claus, C.
Right arrow Articles by Liebert, U. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Claus, C.
Right arrow Articles by Liebert, U. G.
Agricola
Right arrow Articles by Claus, C.
Right arrow Articles by Liebert, U. G.
© 2006 Society for General Microbiology

Rubella virus pseudotypes and a cell–cell fusion assay as tools for functional analysis of the rubella virus E2 and E1 envelope glycoproteins

Claudia Claus1, Jörg Hofmann1, Klaus Überla2 and U. G. Liebert1

1 Institute of Virology, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
2 Department of Molecular and Medical Virology, Ruhr University Bochum, Bochum, Germany

Correspondence
Claudia Claus
claudia.claus{at}medizin.uni-leipzig.de

The rubivirus Rubella virus contains the two envelope glycoproteins E2 and E1 as a heterodimeric spike complex embedded in its lipid envelope. The functions of both proteins, especially of E2, in the process of viral entry are still not entirely understood. In order to dissect E2 and E1 entry functions from post-entry steps, pseudotypes of lentiviral vectors based on Simian immunodeficiency virus were used. C-terminally modified E2 and E1 variants successfully pseudotyped lentiviral vector particles. This is the first report to show that not only E1, but also E2, is able to mediate infectious viral entry. Furthermore, a cell–cell fusion assay was used to further clarify membrane-fusion activities of E2 and E1 as one of the early steps of infection. It was demonstrated that the capsid protein, when coexpressed in cis, enhances the degree of E2- and E1-mediated cell–cell fusion.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2006 by the Society for General Microbiology.