id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-002058-rppsmirp	Carroll, Maria V.	Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG	2010-09-01		.txt	text/plain	5980	320	54	The novel ligands are chaperone protein DnaK, 60 kDa chaperonin-1 (Cpn60.1), glyceraldehyde-3 phosphate dehydrogenase (GAPDH) and lipoprotein lprG. bovis BCG can bind to dendritic-cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN/CD209) to promote entry into human dendritic cells (DCs) and alveolar macrophages Maeda et al., 2003; Tailleux et al., 2003; Pitarque et al., 2005; Appelmelk et al., 2008) . However, the form of this protein identified after capture by the affinity column was not glycosylated at this position, and it is therefore very unlikely that DC-SIGN binds to this ligand via its Ca 2+ -dependent lectin activity. bovis BCG lysate incubated with either 125 I-DC-SIGN or 125 I-DC-SIGNR revealed that DC-SIGN and DC-SIGNR both bind the same protein at around 27 kDa, which corresponds to lprG in our SDS-PAGE system, and is the only ligand detected by this method. DC-SIGN and DC-SIGNR binding to lprG can therefore still occur when the mycobacterial protein has been denatured by SDS-PAGE.	./cache/cord-002058-rppsmirp.txt	./txt/cord-002058-rppsmirp.txt