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Nucleic Acids Research 2006 34(5):e41; doi:10.1093/nar/gkl053
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Published online 15 March 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

J1 mutagenesis

Fusoselect: cell–cell fusion activity engineered by directed evolution of a retroviral glycoprotein

Christoph A. Merten, Jörn Stitz1, Gundula Braun, Julia Medvedovska, Klaus Cichutek and Christian J. Buchholz*

Division of Medical Biotechnology, Paul-Ehrlich-Institut 63225 Langen, Germany 1Biotechnology and Bioengineering Group, Institute for Chemical and Bio-Engineering, Swiss Federal Institute of Technology CH-8093 Zurich, Switzerland

*To whom correspondence should be addressed. Tel: ++49 6103 77 4011; Fax: ++49 6103 771255; Email: bucch{at}pei.de

Received December 5, 2005. Revised December 29, 2005. Accepted February 24, 2006.

Membrane fusion plays a key role in many biological processes including vesicle trafficking, synaptic transmission, fertilization or cell entry of enveloped viruses. As a common feature the fusion process is mediated by distinct membrane proteins. We describe here ‘Fusoselect’, a universal procedure allowing the identification and engineering of molecular determinants for cell–cell fusion-activity by directed evolution. The system couples cell–cell fusion with the release of retroviral particles, but can principally be applied to membrane proteins of non-viral origin as well. As a model system, we chose a {gamma}-retroviral envelope protein, which naturally becomes fusion-active through proteolytic processing by the viral protease. The selection process evolved variants that, in contrast to the parental protein, mediated cell–cell fusion in absence of the viral protease. Detailed analysis of the variants revealed molecular determinants for fusion competence in the cytoplasmic tail (CT) of retroviral Env proteins and demonstrated the power of Fusoselect.

Present address: Christoph Merten, ISIS—Bidogie chimique, 670 83 Strasbourg, France.


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