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

Kathleen Voigt,Christian Drosten,Markus Hoffmann,Georg Herrler,Jan Felix Drexler,Marcel Alexander Müller,Nadine Krüger

doi:10.3390/v11090800

Abstract

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.

Highlights

Viral RNA of the Ghana virus (GhV, formerly termed Kumasi virus, GenBank accession no.: HQ660129.1) was detected in a straw-colored fruit bat (Eidolon helvum) in 2009 [1]
The GhV G protein consists of three major domains: the N-terminal cytoplasmic domain (CD), the transmembrane domain (TM), and the C-terminal ectodomain (ED)
A hallmark of the henipaviruses NiV and HeV is their strong fusion activity, which requires the interaction between the viral surface proteins F and G

Summary

Introduction

Viral RNA of the Ghana virus (GhV, formerly termed Kumasi virus, GenBank accession no.: HQ660129.1) was detected in a straw-colored fruit bat (Eidolon helvum) in 2009 [1]. HeV and NiV emerged from their reservoir host pteropid bats [2,3,4] causing severe and often fatal diseases in humans and domestic animals such as pigs and horses [5,6,7,8]. Due to their zoonotic potential, their high pathogenicity, and the lack of approved therapeutics and a vaccine licensed for use in humans, HeV and NiV are classified as biosafety level. The G protein is a type II membrane protein and is responsible

Methods

Results

Conclusion