Viruses, Vol. 11, Pages 800: Fusogenicity of the Ghana Virus (Henipavirus: Ghanaian bat henipavirus) Fusion Protein is Controlled by the Cytoplasmic Domain of the Attachment Glycoprotein

Viruses, Vol. 11, Pages 800: Fusogenicity of the Ghana Virus (Henipavirus: Ghanaian bat henipavirus) Fusion Protein is Controlled by the Cytoplasmic Domain of the Attachment Glycoprotein Viruses doi: 10.3390/v11090800 Authors: Kathleen Voigt Markus Hoffmann Jan Felix Drexler Marcel Alexander Müller Christian Drosten Georg Herrler Nadine Krüger 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.
Source: Viruses - Category: Virology Authors: Tags: Article Source Type: research

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Source: Current Opinion in Virology - Category: Virology Source Type: research
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Source: PLoS Neglected Tropical Diseases - Category: Tropical Medicine Authors: Source Type: research
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