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J. Biol. Chem., Vol. 276, Issue 34, 32016-32021, August 24, 2001

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Peptide Mimics of the Vesicular Stomatitis Virus G-protein Transmembrane Segment Drive Membrane Fusion in Vitro^*

Dieter Langosch^§, Bettina Brosig, and Rüdiger Pipkorn^¶

From the  Department of Neurobiology, Universität Heidelberg, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany and the ^¶ German Cancer Research Center, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany

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 modeled 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, transmembrane segment 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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