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Virus-like glycodendrinanoparticles displaying quasi-equivalent nested polyvalency upon glycoprotein platforms potently block viral infection

IIQ

Renato Ribeiro-Viana, Macarena Sánchez-Navarro, Joanna Luczkowiak, Julia R. Koeppe, Rafael Delgado, Javier Rojo, Benjamin G. Davis Nature Communications 2012, Vol. 0, DOI: 10.1038/ncomms2302

Ligand polyvalency is a powerful modulator of protein–receptor interactions. In particular, host–pathogen infection interactions are often mediated by glycan ligand–protein interactions. The study of these interactions using synthetic compounds with very high copy number ligands (carbohydrates) has been limited to heterogeneous systems. Here we report a very efficient strategy to assemble the most highly valent glycodendrimeric constructs yet seen (bearing up to 1,620 glycans). These constructs are well-defined single entities that at diameters of up to 32 nm are capable of mimicking pathogens both in size and in their highly glycosylated surfaces. Through this mimicry these glycodendrinanoparticles are capable of blocking (at picomolar concentrations) a model of the infection of T-lymphocytes and human dendritic cells by Ebola virus. The high associated polyvalency effects (β>10⁶, β/N ~10²–10³) displayed on an unprecedented surface area by precise clusters suggest a general strategy for modulation of such interactions.

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