id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-354868-pqn59ojj	Yao, Hebang	A high-affinity RBD-targeting nanobody improves fusion partner’s potency against SARS-CoV-2	2020-09-25		.txt	text/plain	3231	236	58	title: A high-affinity RBD-targeting nanobody improves fusion partner's potency against SARS-CoV-2 Considerable research have been devoted to the development of neutralizing antibodies, including llama-derived single-chain nanobodies, to target the receptor-binding motif (RBM) and to block ACE2-RBD binding. A high-affinity RBD binder without neutralizing activity 85 Previously, we generated 99 sybodies from three highly diverse synthetic libraries by ribosome and phage display with in vitro selections against the SARS-CoV-2 RBD. Consistent with its inability to neutralize SARS-CoV-2 pseudovirus, SR31 did not affect RBD-ACE2 binding (Fig. 1C) . Most RBD-targeting neutralizing antibodies, including neutralizing nanobodies characterized so far (8, 13-15, 19, 20, 22-24, 26-28, 34, 35, 37) , engage the RBD at the receptor-binding motif (RBM) (Fig. 3A) , thus competing off ACE2 and preventing viral entry. Taken together, the structural data rationalize the high-affinity binding between SR31 and RBD, and its inability to neutralize SARS-CoV-2. Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2	./cache/cord-354868-pqn59ojj.txt	./txt/cord-354868-pqn59ojj.txt