Stiftung Tierärztliche Hochschule Hannover (TiHo)

Fusogenicity of the Ghana Virus (Henipavirus: Ghanaian bat henipavirus) Fusion Protein is Controlled by the Cytoplasmic Domain of the Attachment Glycoprotein.

Affiliation
Institute of Virology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany.
Voigt, Kathleen;
ORCID
0000-0003-4603-7696
Affiliation
Infection Biology Unit, German Primate Center-Leibniz Institute for Primate Research, 37077 Göttingen, Germany.
Hoffmann, Markus;
Affiliation
Institute of Virology, Charité Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 10117 Berlin, Germany.
Drexler, Jan Felix;
ORCID
0000-0003-2242-5117
Affiliation
Institute of Virology, Charité Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 10117 Berlin, Germany.
Müller, Marcel Alexander;
Affiliation
Institute of Virology, Charité Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 10117 Berlin, Germany.
Drosten, Christian;
ORCID
0000-0002-5827-0957
Affiliation
Institute of Virology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany.
Herrler, Georg;
ORCID
0000-0002-4413-8699
Affiliation
Institute of Virology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany. nadine.krueger@tiho-hannover.de.
Krüger, Nadine

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.

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