id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-253705-utp8po48	Sriwilaijaroen, Nongluk	Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses	2020-04-19		.txt	text/plain	20192	863	46	While HEF glycoproteins of influenza C and D viruses attach to 9-O-acetyl-Neu5Accarrying sugar chains found in the respiratory tract of animals [31] as a receptor determinant for infection in cattle and pigs (only C virus has been detected in humans), HAs of influenza A (Fig. 3a) and B viruses recognize α2-6Neu5Ac-carrying sugar chains and Fig. 3 (continued) σ1 containing a Sia-binding site in its body) interacts with a sialoglycan on a glycoprotein/ glycolipid (a brown dash), which is anchored to the host cell membrane. Variants with the HE gene, which have become circulating strains, could be explained by the finding that the HE protein increases the efficiency of production of infectious virus [78] possibly by acting as a lectin for enhancing viral binding and as an enzyme that destroys receptors by de-O-acetylation (esterase) for enhancing release of trapped virions from the host mucosa and of budding virions from infected cells.	./cache/cord-253705-utp8po48.txt	./txt/cord-253705-utp8po48.txt