title: C-type lectin-independent interaction of complement opsonized HIV with monocyte-derived dendritic cells.
abstract: HIV directly activates the complement cascade and is, therefore, opsonized with C3-cleavage products in vivo. This cloud of C3 fragments on the viral surface may impair the interaction of the HIV envelope glycoproteins gp120/gp41 with C-type lectins expressed on immature dendritic cells (iDC). Therefore, we determined the accessibility of gp120 after opsonization and compared the interaction of DC with non-opsonized or complement-opsonized HIV. The recognition of native gp120 was drastically impaired when the virus was covered by complement. Independent of opsonization, similar amounts of HIV bound to DC. The interaction of iDC and the infection of DC-PBL co-cultures with non-opsonized virus was significantly reduced by mannan and antibodies which inhibit the ICAM-1-CR3 interaction. The binding of opsonized virus to iDC was reduced by an anti-CR3-antibody, which interferes with the binding of C3 fragments, but was not affected by mannan. Complement enhanced the HIV infection of DC and DC-PBL co-cultures significantly. Mannan did not inhibit the complement-dependent enhancement of infection. Thus, non-opsonized and opsonized HIV interacted with iDC, although the binding mechanisms seemed to differ. As HIV is opsonized in vivo, the C-type lectin-independent interaction of opsonized viruses with iDC has to be taken into account.
authors.affiliation: Division of Hygiene and Microbiology, Innsbruck Medical University, Ludwig Boltzmann Institute for AIDS Research, Innsbruck, Austria.
authors.forename: Monika
authors.initials: M
authors.lastname: Pruenster
authors.forename: Doris
authors.initials: D
authors.lastname: Wilflingseder
authors.forename: Zoltán
authors.initials: Z
authors.lastname: Bánki
authors.forename: Christoph G
authors.initials: CG
authors.lastname: Ammann
authors.forename: Brigitte
authors.initials: B
authors.lastname: Muellauer
authors.forename: Martina
authors.initials: M
authors.lastname: Meyer
authors.forename: Cornelia
authors.initials: C
authors.lastname: Speth
authors.forename: Manfred P
authors.initials: MP
authors.lastname: Dierich
authors.forename: Heribert
authors.initials: H
authors.lastname: Stoiber
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology / Q000494:pharmacology; D015704:CD4 Antigens / Q000276:immunology; D015815:Cell Adhesion Molecules / Q000276:immunology; D018920:Coculture Techniques; D003176:Complement C3 / Q000276:immunology*; D003713:Dendritic Cells / Q000276:immunology* / Q000821:virology*; D006678:HIV / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000276:immunology*; D015658:HIV Infections / Q000276:immunology*; D006801:Humans; D007113:Immunity, Innate / Q000276:immunology; D018799:Intercellular Adhesion Molecule-1 / Q000276:immunology; D037181:Lectins, C-Type / Q000276:immunology; D008351:Mannans / Q000276:immunology; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D000911:Antibodies, Monoclonal; D015704:CD4 Antigens; D015815:Cell Adhesion Molecules; D003176:Complement C3; D015699:HIV Envelope Protein gp120; D018799:Intercellular Adhesion Molecule-1; D037181:Lectins, C-Type; D008351:Mannans; D011956:Receptors, Cell Surface; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin