id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-348729-kejlm425	Liu, Xiaoyu	Neutralizing Antibodies Isolated by a site-directed Screening have Potent Protection on SARS-CoV-2 Infection	2020-05-04		.txt	text/plain	3457	178	50	SARS-CoV-2 infects host cells by interacting with angiotensin converting enzyme-2 (ACE2) via the S1 receptor-binding domain (RBD) of its surface spike glycoprotein. Among them, 4A3 and three domain antibodies (4A12, 4D5, and 4A10) were identified to act as neutralizing antibodies due to their capabilities to block the interaction between SARS-CoV-2-RBD and ACE2-positive cells. These determined infection mechanisms indicated that blocking the interaction of SARS-CoV-2-RBD and ACE2 would cause a direct neutralizing effect against virus. This information suggests that the ACE2 interface of SARS-CoV-2-RBD might have high immunogenicity, which would be a suitable targeting epitope to develop SARS-CoV-2-specific antibodies with potent neutralizing function by in vitro screening. We performed site-directed antibody screening by phage display and finally obtained one IgG antibody and three single domain antibodies with potent neutralizing activities for SARS-CoV-2. Notably, the eluted phage exhibited a stronger binding signal on SARS-CoV-2-RBD compared to that on SARS-CoV-2-RBD mut, especially those from the domain antibody library ( Figure 2C ), indicating an expected precleaning effect during selection.	./cache/cord-348729-kejlm425.txt	./txt/cord-348729-kejlm425.txt