id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-330767-jja2wcfz	Voigt, Kathleen	Fusogenicity of the Ghana Virus (Henipavirus: Ghanaian bat henipavirus) Fusion Protein is Controlled by the Cytoplasmic Domain of the Attachment Glycoprotein	2019-08-29		.txt	text/plain	6059	263	48	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). In previous studies, it has been shown that the transport of GhV G to the cell surface is significantly reduced compared to NiV G and that the majority of the GhV G protein accumulates in the endoplasmic reticulum (ER), suggesting that the amount of surface-expressed GhV G is not efficient enough to trigger conformational changes in the F protein that are required to acquire the fusion-active form of F [35, 36] . However, whereas the glycoproteins of NiV and HeV induce cell-to-cell fusion in a broad variety of cells from different host species, syncytium formation upon expression of GhV F and G proteins is restricted to certain bat cells [32] [33] [34] [35] .	./cache/cord-330767-jja2wcfz.txt	./txt/cord-330767-jja2wcfz.txt