Virus-like glycodendrinanoparticles displaying quasi-equivalent nested polyvalency upon glycoprotein platforms potently block viral infection
Renato Ribeiro-Viana,
Macarena Sánchez-Navarro,
Joanna Luczkowiak,
Julia R. Koeppe,
Rafael Delgado (),
Javier Rojo () and
Benjamin G. Davis ()
Additional contact information
Renato Ribeiro-Viana: University of Oxford, Chemistry Research Laboratory
Macarena Sánchez-Navarro: University of Oxford, Chemistry Research Laboratory
Joanna Luczkowiak: Laboratorio de Microbiología Molecular, Instituto de Investigación Hospital 12 de Octubre (imas12)
Julia R. Koeppe: University of Oxford, Chemistry Research Laboratory
Rafael Delgado: Laboratorio de Microbiología Molecular, Instituto de Investigación Hospital 12 de Octubre (imas12)
Javier Rojo: Glycosystems Laboratory, Instituto de Investigaciones Químicas (IIQ), CSIC—Universidad de Sevilla
Benjamin G. Davis: University of Oxford, Chemistry Research Laboratory
Nature Communications, 2012, vol. 3, issue 1, 1-9
Abstract:
Abstract 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.
Date: 2012
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/ncomms2302 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2302
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms2302
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().