Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR
2001; American Association for the Advancement of Science; Volume: 294; Issue: 5549 Linguagem: Inglês
10.1126/science.1066371
ISSN1095-9203
AutoresH. Feinberg, Daniel A. Mitchell, Kurt Drickamer, William I. Weis,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoDendritic cell specific intracellular adhesion molecule–3 (ICAM-3) grabbing nonintegrin (DC-SIGN), a C-type lectin present on the surface of dendritic cells, mediates the initial interaction of dendritic cells with T cells by binding to ICAM-3. DC-SIGN and DC-SIGNR, a related receptor found on the endothelium of liver sinusoids, placental capillaries, and lymph nodes, bind to oligosaccharides that are present on the envelope of human immunodeficiency virus (HIV), an interaction that strongly promotes viral infection of T cells. Crystal structures of carbohydrate-recognition domains of DC-SIGN and of DC-SIGNR bound to oligosaccharide, in combination with binding studies, reveal that these receptors selectively recognize endogenous high-mannose oligosaccharides and may represent a new avenue for developing HIV prophylactics.
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