The archaeal Dps nanocage targets kidney proximal tubules via glomerular filtration

J Clin Invest. 2019 Sep 3;129(9):3941-3951. doi: 10.1172/JCI127511.

Abstract

Nature exploits cage-like proteins for a variety of biological purposes, from molecular packaging and cargo delivery to catalysis. These cage-like proteins are of immense importance in nanomedicine due to their propensity to self-assemble from simple identical building blocks to highly ordered architecture and the design flexibility afforded by protein engineering. However, delivery of protein nanocages to the renal tubules remains a major challenge because of the glomerular filtration barrier, which effectively excludes conventional size nanocages. Here, we show that DNA-binding protein from starved cells (Dps) - the extremely small archaeal antioxidant nanocage - is able to cross the glomerular filtration barrier and is endocytosed by the renal proximal tubules. Using a model of endotoxemia, we present an example of the way in which proximal tubule-selective Dps nanocages can limit the degree of endotoxin-induced kidney injury. This was accomplished by amplifying the endogenous antioxidant property of Dps with addition of a dinuclear manganese cluster. Dps is the first-in-class protein cage nanoparticle that can be targeted to renal proximal tubules through glomerular filtration. In addition to its therapeutic potential, chemical and genetic engineering of Dps will offer a nanoplatform to advance our understanding of the physiology and pathophysiology of glomerular filtration and tubular endocytosis.

Keywords: Diagnostic imaging; Drug therapy; Nanotechnology; Nephrology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Archaeal Proteins / pharmacology*
  • DNA-Binding Proteins / pharmacology*
  • Glomerular Filtration Rate / drug effects*
  • Kidney Tubules, Proximal / metabolism*
  • Male
  • Mice
  • Rats
  • Rats, Wistar
  • Recombinant Proteins / pharmacology
  • Sulfolobus solfataricus*

Substances

  • Archaeal Proteins
  • DNA-Binding Proteins
  • Recombinant Proteins