id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-319118-47ovbto5	Yu, Xiaojuan	Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27	2015-08-18		.txt	text/plain	4796	254	53	We previously reported two human monoclonal antibodies that target the receptor binding domain (RBD) of the spike and exhibit strong neutralization activity against live and pesudotyped MERS-CoV infection. We found Trp535 as an anchor residue in the RBD for MERS-27 recognition, and its interaction with N-linked carbohydrates of DPP4 is important for the binding to DPP4 and for viral entry of MERS-CoV. In sum, results of viral entry, neutralization, and binding assays consistently indicated that Trp535 and Asp539 are critical for both MERS-CoV spike glycoprotein recognition by MERS-27 and binding with receptor DPP4. The interaction between Trp535 of RBD and the DPP4 carbohydrate is also important for receptor binding and viral entry of MERS-CoV. The receptor binding domain of the new Middle East respiratory syndrome coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies A conformation-dependent neutralizing monoclonal antibody specifically targeting receptor-binding domain in Middle East respiratory syndrome coronavirus spike protein	./cache/cord-319118-47ovbto5.txt	./txt/cord-319118-47ovbto5.txt