id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-296657-mymndjvd	Higuchi, Yusuke	High affinity modified ACE2 receptors prevent SARS-CoV-2 infection	2020-09-16		.txt	text/plain	3509	195	51	The extracellular domain of modified ACE2 fused to the Fc region of the human immunoglobulin IgG1 had stable structure and neutralized SARS-CoV-2 pseudotyped lentivirus and authentic virus with more than 100-fold lower concentration than wild-type. Engineering ACE2 decoy receptors with directed evolution is a promising approach to develop a SARS-CoV-2 neutralizing drug that has affinity comparable to monoclonal antibodies yet displaying resistance to escape mutations of virus. Three cycles of screening resulted in an identification of mutant ACE2 clones with more than 100-fold higher binding affinity to the RBD and lower half-maximal inhibitory concentration (IC50) for SARS-CoV-2 pseudotyped lentivirus as well as authentic virus. We engineered ACE2 to bind the RBD of the SARS-CoV-2 spike protein with the combination of surface display of mutagenized library and fluorescence-activated cell sorting (FACS) to perform the evolution in 293T human cells.	./cache/cord-296657-mymndjvd.txt	./txt/cord-296657-mymndjvd.txt