id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-274480-aywdmj6o	Song, Wenfei	Identification of residues on human receptor DPP4 critical for MERS-CoV binding and entry	2014-10-21		.txt	text/plain	2815	147	57	Middle East respiratory syndrome coronavirus (MERS-CoV) infects host cells through binding the receptor binding domain (RBD) on its spike glycoprotein to human receptor dipeptidyl peptidase 4 (hDPP4). Previously, we have generated a panel of MERS-CoV mutant RBD proteins at the residues D539, Y499, D510, E513, L506, W553 and V555 to characterize their impacts on binding activity to hDPP4 and the entry efficiency into target cells. To study the impacts of the substitutions of the critical residues on hDPP4 described above on the interaction between MERS-CoV RBD and hDDP4, we determined the binding efficiency between these two proteins by employing SPR technique. To further study the importance of the critical residues on hDPP4 on viral entry, we measured the entry efficiency of pseudovirus into COS7 cells expressing the wide-type and mutant forms of hDPP4. These results are consistent with our findings and suggest these residues play an important role in RBD binding and viral entry, and determining the tropism to MERS-CoV infection.	./cache/cord-274480-aywdmj6o.txt	./txt/cord-274480-aywdmj6o.txt