The Role of the Transmembrane and of the Intraviral Domain of Glycoproteins in Membrane Fusion of Enveloped Viruses |
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Authors: | Britta Schroth-Diez Kai Ludwig Bolormaa Baljinnyam Christine Kozerski Qiang Huang Andreas Herrmann |
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Affiliation: | (1) Institut für Biologie/Biophysik, Mathematisch-Naturwissenschaftliche Fakultät I, Humboldt-Universität zu Berlin, Invalidenstrasse 42, D-10115 Berlin, Germany;(2) Present address: Institut für Organische Chemie, Freie Universität zu Berlin, Takustr. 3, D-14195 Berlin, Germany;(3) Present address: Department of Cell Biology, University of Virginia, Health System, School of Medicine, Box P.O. 800732, Charlottesville, Virginia 22908-0732, USA |
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Abstract: | Fusion of enveloped viruses with their target membrane is mediated by viral integral glycoproteins. A conformational change of their ectodomain triggers membrane fusion. Several studies suggest that an extended, triple-stranded rod-shaped -helical coiled coil resembles a common structural and functional motif of the ectodomain of fusion proteins. From that, it is believed that essential features of the fusion process are conserved among the various enveloped viruses. However, this has not been established so far for the highly conserved transmembrane and intraviral sequences of fusion proteins. The article will focus on the role of both sequences in the fusion process. Recent studies from various enveloped viruses strongly imply that a transmembrane domain with a minimum length is required for later steps of membrane fusion, i.e., the formation and enlargement of the aqueous fusion pore. Although no specific sequence of the TM is necessary for pore formation, distinct properties and motifs of the domain may be obligatory to ascertain full fusion activity. However, with some exceptions, the intraviral domain seems to be not required for fusion activity of viral fusion proteins. |
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Keywords: | Membrane fusion virus protein transmembrane domain intraviral domain |
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