Assembling different antennas of the gp120 high mannose-type glycans on gold nanoparticles provides superior binding to the anti-HIV antibody 2G12 than the individual antennas

In order to re-build Man(9)GlcNAc(2) clusters of the HIV gp120 glycoprotein, similar to 2 nm gold glyconanoparticles (GNPs) were coated with the synthetic partial structures of Man(9), the tetramannoside Man alpha 1-2Man alpha 1-2Man alpha 1- 3Man alpha 1- and the pentamannoside Man alpha 1-2Man alpha 1-3[Man alpha 1-2Man alpha 1-6]Man alpha 1-. Their interactions with the anti-HIV broadly neutralizing antibody 2G12 were studied by surface plasmon resonance (SPR)-based biosensors and saturation transfer difference (STD)-NMR spectroscopy. A synergistic effect of the tetra- and pentamannosides multimerized on a same GNP was observed. The assembly of these antennas of the gp120 high-mannose type glycan on GNPs provided superior binding to the anti-HIV antibody 2G12 with respect to GNPs carrying only the individual oligomannosides. The results presented in this work provide new molecular information on the interactions between clusters of oligomannosides and 2G12 that could help in the design of a carbohydrate-based vaccine against HIV. (C) 2014 Elsevier Ltd. All rights reserved.