id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-267537-akzydy7l	Dang, Ha V.	An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections	2019-09-30		.txt	text/plain	9566	545	52	Cryo-electron microscopy, triggering and fusion studies show the antibody binds to a prefusion-specific quaternary epitope, conserved in NiV F and HeV F glycoproteins, and prevents membrane fusion and viral entry. To elucidate the mechanism of 5B3-mediated neutralization of NiV and HeV, we determined a cryo-EM structure of a stabilized NiV F ectodomain trimer in complex with the 5B3 antibody Fab fragment at 3.5 Å resolution (Fig. 2a,b , Table 1 and Extended Data 1). To further study the mechanism of action of 5B3/h5B3.1 in the context of a full-length, membrane-embedded F glycoprotein, we carried out cell-cell fusion assays in the presence of varying concentrations of mAbs. We observed that 5B3 and h5B3.1 prevented NiV F-and HeV F-mediated membrane fusion in a concentration-dependent manner, consistent with the expectation that trapping F in the prefusion conformation actually resulted in inhibition of membrane fusion (Figs.	./cache/cord-267537-akzydy7l.txt	./txt/cord-267537-akzydy7l.txt