Potency of HIV-1 envelope glycoprotein gp120 antibodies to inhibit the interaction of DC-SIGN with HIV-1 gp120

Annemarie N Lekkerkerker, Irene S Ludwig, Sandra J van Vliet, Yvette van Kooyk, Teunis B H Geijtenbeek

Research output: Contribution to journalArticleAcademicpeer-review

23 Citations (Scopus)


The interaction of DC-SIGN with gp120 provides an attractive target for intervention of HIV-1 transmission. Here, we have investigated the potency of gp120 antibodies to inhibit the DC-SIGN-gp120 interaction. We demonstrate that although the V3 loop is not essential for DC-SIGN binding, antibodies against the V3 loop partially inhibit DC-SIGN binding, suggesting that these antibodies sterically hinder DC-SIGN binding to gp120. Polyclonal antibodies raised against non-glycosylated gp120 inhibited both low and high avidity DC-SIGN-gp120 interactions in contrast to polyclonal antibodies raised against glycosylated gp120. Thus, glycans present on gp120 may prevent the generation of antibodies that block the DC-SIGN-gp120 interactions. Moreover, the polyclonal antibodies against non-glycosylated gp120 efficiently inhibited HIV-1 capture by both DC-SIGN transfectants and immature dendritic cells. Therefore, non-glycosylated gp120 may be an attractive immunogen to elicit gp120 antibodies that block the binding to DC-SIGN. Furthermore, we demonstrate that DC-SIGN binding to gp120 enhanced CD4 binding, suggesting that DC-SIGN induces conformational changes in gp120, which may provide new targets for neutralizing antibodies.

Original languageEnglish
Pages (from-to)465-76
Number of pages12
Issue number2
Publication statusPublished - 24 Nov 2004


  • Animals
  • Antigen-Antibody Reactions
  • CD4 Antigens/immunology
  • Cell Adhesion Molecules/immunology
  • Cells, Cultured
  • Glycosylation
  • HIV Antibodies/pharmacology
  • HIV Envelope Protein gp120/immunology
  • HIV-1/immunology
  • Humans
  • Lectins, C-Type/immunology
  • Mice
  • Receptors, Cell Surface/immunology

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