id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-342291-imn7g084	Ciminski, Kevin	Bats reveal the true power of influenza A virus adaptability	2020-04-16		.txt	text/plain	2478	120	50	Indeed, the HA of the newly discovered Old World bat H9N2 virus binds to α2,3-sialic In contrast, the internal gene segments of the bat-derived IAVs form two outgroups that are located at a more basal position. Conventional IAVs and the bat H9N2 virus possess the surface glycoprotein neuraminidase (NA), which removes sialic acid residues from infected cells to facilitate the release of newly formed viral particles (Fig 2A) . The amazing ability of H18 to rapidly overcome the absence of a functional N11 suggests that the structure of H18 (and possibly H17) may provide a broader scope of evolutionary flexibility than that of conventional sialic acid-dependent IAVs. It is therefore tempting to speculate that bat IAV HA proteins, and in particular H18, might have the potential to adapt to novel and so far unknown entry receptors different from MHC-II (Fig 2D) .	./cache/cord-342291-imn7g084.txt	./txt/cord-342291-imn7g084.txt