id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-254735-8reu45yz	Reguera, Juan	Structural Bases of Coronavirus Attachment to Host Aminopeptidase N and Its Inhibition by Neutralizing Antibodies	2012-08-02		.txt	text/plain	8064	410	59	Here we describe the crystal structures of the receptor-binding domains (RBDs) of two closely related CoV strains, transmissible gastroenteritis virus (TGEV) and porcine respiratory CoV (PRCV), in complex with their receptor, porcine APN (pAPN), or with a neutralizing antibody. The report uncovers a unique virus-receptor recognition mode that engages a glycan N-linked to the pAPN ectodomain, revealing structural determinants of the receptor-binding specificity in CoVs. Neutralizing antibodies target viral residues used for binding to the APN receptor and entry into host cells, showing that efficient CoV neutralization requires immune responses focused toward key receptor binding motifs in the virus envelope. The RBD tip, shown here as the pAPN-binding edge of the domain (Figure 3) , is the main S protein determinant of antigenic site A, recognized by the most effective neutralizing antibodies of TGEV and related CoV infections [25, 26] .	./cache/cord-254735-8reu45yz.txt	./txt/cord-254735-8reu45yz.txt