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Ligand polyvalency is a powerful modulator of protein–receptor interactions. Host–pathogen infection interactions are often mediated by glycan ligand–protein interactions, yet its interrogation with very high copy number ligands has been limited to heterogenous systems. Here we report that through the use of nested layers of multivalency we are able to assemble the most highly valent glycodendrimeric constructs yet seen (bearing up to 1,620 glycans). These constructs are pure and 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 glyco-dendri-protein-nano-particles 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.We acknowledge the financial support by the MICINN of Spain CTQ2008-01694 and CTQ2011-23410, the EU RTN CARMUSYS (PITN-GA-2008-213592), Instituto de Salud Carlos III (FIS PI080806 and PI1101580) and Fundación para la Investigación y Prevención del SIDA (FIPSE 36749) and the European FEDER funds. We thank Professors A. Sánchez (Centers for Disease Control and Prevention, Atlanta, GA) and M.G. Finn (TSRI, La Jolla, CA) for providing Zaire Ebola Virus glycoprotein and p75m/Qβ plasmids, respectively. MSN thanks Fundación Ramón Areces for funding, BGD is a Royal Society Wolfson Research Merit Award recipient and is supported by an EPSRC LSI Platform grant.Peer Reviewe

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