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Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR

H Feinberg1, D A Mitchell, K Drickamer

  • 1Department of Structural Biology, University School of Medicine, Stanford, CA 94305, USA.

Science (New York, N.Y.)
|December 12, 2001
PubMed

Insights

Dendritic cell specific intracellular adhesion molecule-3 grabbing nonintegrin (DC-SIGN) binds to HIV, promoting infection. Understanding DC-SIGN and DC-SIGNR binding to high-mannose oligosaccharides may lead to new HIV prophylactics.

Area of Science:

  • Immunology
  • Virology
  • Structural Biology

Background:

  • Dendritic cell specific intracellular adhesion molecule-3 grabbing nonintegrin (DC-SIGN) is a C-type lectin on dendritic cells that binds ICAM-3, mediating initial T cell interactions.
  • DC-SIGN and the related DC-SIGNR receptor bind to oligosaccharides on the human immunodeficiency virus (HIV) envelope, enhancing viral infection of T cells.

Purpose of the Study:

  • To elucidate the structural basis of DC-SIGN and DC-SIGNR recognition of oligosaccharides.
  • To explore the potential of these interactions for developing novel HIV prophylactics.

Main Methods:

  • X-ray crystallography was used to determine the structures of the carbohydrate-recognition domains of DC-SIGN and DC-SIGNR bound to oligosaccharides.
  • Binding studies were conducted to assess the selectivity of these receptors for specific oligosaccharides.

Main Results:

  • The crystal structures revealed how DC-SIGN and DC-SIGNR bind to specific oligosaccharide structures.
  • Binding studies confirmed that these receptors selectively recognize endogenous high-mannose oligosaccharides.

Conclusions:

  • DC-SIGN and DC-SIGNR's selective recognition of high-mannose oligosaccharides provides a molecular understanding of their role in HIV infection.
  • Targeting these interactions represents a promising new strategy for developing effective HIV prophylactics.

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