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Multivalent display and receptor-mediated endocytosis of transferrin on virus-like particles

Academic Article
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Overview

authors

  • Banerjee, D.
  • Liu, A. P.
  • Voss, N. R.
  • Schmid, Sandra
  • Finn, M.G.

publication date

  • June 2010

journal

  • ChemBioChem  Journal

abstract

  • The structurally regular and stable self-assembled capsids derived from viruses can be used as scaffolds for the display of multiple copies of cell- and tissue-targeting molecules and therapeutic agents in a convenient and well-defined manner. The human iron-transfer protein transferrin, a high affinity ligand for receptors upregulated in a variety of cancers, has been arrayed on the exterior surface of the protein capsid of bacteriophage Qbeta. Selective oxidation of the sialic acid residues on the glycan chains of transferrin was followed by introduction of a terminal alkyne functionality through an oxime linkage. Attachment of the protein to azide-functionalized Qbeta capsid particles in an orientation allowing access to the receptor binding site was accomplished by the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) click reaction. Transferrin conjugation to Qbeta particles allowed specific recognition by transferrin receptors and cellular internalization through clathrin-mediated endocytosis, as determined by fluorescence microscopy on cells expressing GFP-labeled clathrin light chains. By testing Qbeta particles bearing different numbers of transferrin molecules, it was demonstrated that cellular uptake was proportional to ligand density, but that internalization was inhibited by equivalent concentrations of free transferrin. These results suggest that cell targeting with transferrin can be improved by local concentration (avidity) effects.

subject areas

  • Alkynes
  • Allolevivirus
  • Animals
  • Capsid Proteins
  • Catalysis
  • Cell Line
  • Clathrin
  • Copper
  • Endocytosis
  • Flow Cytometry
  • Haplorhini
  • Humans
  • Ligands
  • Transferrin
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Research

keywords

  • click chemistry
  • polyvalency
  • receptor-mediated endocytosis
  • transferrin
  • viruses
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Identity

PubMed Central ID

  • PMC4180096

International Standard Serial Number (ISSN)

  • 1439-4227

Digital Object Identifier (DOI)

  • 10.1002/cbic.201000125

PubMed ID

  • 20455239
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Additional Document Info

start page

  • 1273

end page

  • 1279

volume

  • 11

issue

  • 9

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