Fusogenicity of the Ghana Virus (<i>Henipavirus</i>: <i>Ghanaian bat henipavirus</i>) Fusion Protein is Controlled by the Cytoplasmic Domain of the Attachment Glycoprotein
Kathleen Voigt,
Markus Hoffmann,
Jan Felix Drexler,
Marcel Alexander Müller,
Christian Drosten,
Georg Herrler,
Nadine Krüger
Affiliations
Kathleen Voigt
Institute of Virology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany
Markus Hoffmann
Infection Biology Unit, German Primate Center—Leibniz Institute for Primate Research, 37077 Göttingen, Germany
Jan Felix Drexler
Institute of Virology, Charité Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 10117 Berlin, Germany
Marcel Alexander Müller
Institute of Virology, Charité Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 10117 Berlin, Germany
Christian Drosten
Institute of Virology, Charité Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 10117 Berlin, Germany
Georg Herrler
Institute of Virology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany
Nadine Krüger
Institute of Virology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany
The Ghana virus (GhV) is phylogenetically related to the zoonotic henipaviruses Nipah (NiV) and Hendra virus. Although GhV uses the highly conserved receptor ephrin-B2, the fusogenicity is restricted to cell lines of bat origin. Furthermore, the surface expression of the GhV attachment glycoprotein (G) is reduced compared to NiV and most of this protein is retained in the endoplasmic reticulum (ER). Here, we generated truncated as well as chimeric GhV G proteins and investigated the influence of the structural domains (cytoplasmic tail, transmembrane domain, ectodomain) of this protein on the intracellular transport and the fusogenicity following coexpression with the GhV fusion protein (F). We demonstrate that neither the cytoplasmic tail nor the transmembrane domain is responsible for the intracellular retention of GhV G. Furthermore, the cytoplasmic tail of GhV G modulates the fusogenicity of GhV F and therefore controls the species-restricted fusogenicity of the GhV surface glycoproteins.
