Fucosylated lactosamines participate in adhesion of HIV-1 envelope glycoprotein to dendritic cells.

ABSTRACT

Carbohydrates expressed on HIV-1 gp160 are purported to bind to several receptor types that affect virus pathophysiology. Here, we define a potential role for fucosylated glycans involved in the adhesion of cells expressing anchored HIV-1 glycoprotein or HIV virions to human dendritic cells (DCs). We observe that a monoclonal antibody (FH6), with reactivity toward an extended dimeric form of a fucosyl lactosamine, binds to gp120 transfectants, blocking adhesion of these cells and virus particles to human DCs. We observe that serum antibodies induced by peptide mimetic of fucosylated carbohydrate core structures emulate the monoclonal antibody reactivity pattern, showing enhanced reactivity to HIV-1 envelope-expressing cell line and blocking the adhesion of these cells to human DCs. These results suggest a potential role for initial adherence of virally infected cells or virions mediated by fucosylated lactosamines expressed on the envelope protein. As these carbohydrates function as adhesion molecules associated with homing and dissemination processes, such interactions may contribute to the HIV infection process.