Oligomerization of the Macrophage Mannose Receptor Enhances gp120-mediated Binding of HIV-1

• Published in: The Journal of biological chemistry Vol. 284; no. 17; pp. 11027 - 11038
• Main Authors: Lai, Joey, Bernhard, Oliver K., Turville, Stuart G., Harman, Andrew N., Wilkinson, John, Cunningham, Anthony L.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 24.04.2009; American Society for Biochemistry and Molecular Biology
• Subjects: Acetylgalactosamine - metabolism; Animals; Calcium; Calcium - metabolism; Carbohydrates; Cell adhesion molecules; Cross-Linking Reagents - chemistry; Cysteine - metabolism; Dendritic cells; Dimerization; Envelope protein; Flow Cytometry; fucose; Glycoprotein gp120; HIV Envelope Protein gp120 - metabolism; HIV-1 - metabolism; Human immunodeficiency virus 1; Humans; Langerhans cells; Langerhans Cells - metabolism; Langerhans Cells - virology; Lectins; Lectins, C-Type - chemistry; Lectins, C-Type - metabolism; Macrophages; Macrophages - metabolism; Macrophages - virology; mannan; Mannose; Mannose Receptor; Mannose receptors; Mannose-Binding Lectins - chemistry; Mannose-Binding Lectins - metabolism; Mass spectroscopy; Monocytes; N-Acetylgalactosamine; N-Acetylglucosamine; Oligomerization; oligosaccharides; Oligosaccharides - metabolism; Pathogens; Protein Structure and Folding; Rats; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - metabolism; Virions

C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dend...