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M102579200v1
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Papers In Press, published online ahead of print June 19, 2001
J. Biol. Chem, 10.1074/jbc.M102579200
Submitted on March 22, 2001
Revised on June 19, 2001
Accepted on June 19, 2001

Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro

Dieter Langosch, Bettina Brosig, and Rudiger Pipkorn

Neurobiology, Universitaet Heidelberg, Heidelberg 69120

Corresponding Author: langosch{at}sun0.urz.uni-heidelberg.de

The efficiency of cell-cell fusion mediated by heterologously expressed vesicular stomatitis virus G-protein has previously been shown to be affected by mutating its transmembrane segment. Here, we show that a synthetic peptide modelled after this transmembrane segment drives liposome-liposome fusion. Addition of millimolar Ca2+-concentrations strongly potentiated the effect of the peptides suggesting that Ca2+-mediated liposome aggregation supports the activity of the peptide. Peptide-driven fusion was suppressed by lysolipid, an established inhibitor of natural membrane fusion, and involved inner and outer leaflets of the liposomal bilayer. Thus, TMS-peptide-driven liposome fusion exhibits important hallmarks characteristic of natural membrane fusion. Importantly, the mutations previously shown to attenuate the function of full-length G-protein in cell-cell fusion also attenuated the fusogenicity of the peptide, albeit in a less pronounced fashion. Therefore, the function of the peptide mimic is dependent on its primary structure, similar to full-length G-protein. Together, our data suggest that the G-protein transmembrane segment is an autonomous functional domain. We propose that it acts at a late step in membrane fusion elicited by vesicular stomatitis virus.


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