id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-274708-w6gmscv4	Mathewson, Alison C.	Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2	2008-11-17		.txt	text/plain	2800	135	60	Although in different groups, the coronaviruses severe acute respiratory syndrome-coronavirus (SARS-CoV) and NL63 use the same receptor, angiotensin converting enzyme (ACE)-2, for entry into the host cell. (2007) showed that incubation of a tagged form of the RBD with cell lines expressing a number of natural and synthetic ACE-2 variants indicated that the ACE-2 contact residues critical for binding both SARS-CoV and NL63 S overlap (Li et al., 2007) . To investigate CoV S protein binding to ACE-2 in a unified format, we produced soluble and cell-bound versions of the two S proteins through the use of baculovirus expression vectors designed for secretion of proteins as Fc-tagged fusion proteins (Chen et al., 2007) or, separately, displayed on the insect cell surface following tagging with the VSV G protein transmembrane (TM) domain (Chapple & Jones, 2002 ) (see Supplementary Fig. S1 , available in JGV Online). Identification of residues in the receptor-binding domain (RBD) of the spike protein of human coronavirus NL63 that are critical for the RBD-ACE2 receptor interaction	./cache/cord-274708-w6gmscv4.txt	./txt/cord-274708-w6gmscv4.txt