Yersinia enterocolitica-mediated degradation of neutrophil extracellular traps (NETs)

Research output: Contribution to journalArticle

Abstract

Neutrophil extracellular trap (NET) formation is described as a tool of the innate host defence to fight against invading pathogens. Fibre-like DNA structures associated with proteins such as histones, cell-specific enzymes and antimicrobial peptides are released, thereby entrapping invading pathogens. It has been reported that several bacteria are able to degrade NETs by nucleases and thus evade the NET-mediated entrapment. Here we studied the ability of three different Yersinia serotypes to induce and degrade NETs. We found that the common Yersinia enterocolitica serotypes O:3, O:8 and O:9 were able to induce NETs in human blood-derived neutrophils during the first hour of co-incubation. At later time points, the NET amount was reduced, suggesting that degradation of NETs has occurred. This was confirmed by NET degradation assays with phorbol-myristate-acetate-pre-stimulated neutrophils. In addition, we found that the Yersinia supernatants were able to degrade purified plasmid DNA. The absence of Ca(2+) and Mg(2+) ions, but not that of a protease inhibitor cocktail, completely abolished NET degradation. We therefore postulate that Y. enterocolitica produces Ca(2+)/Mg(2+)-dependent NET-degrading nucleases as shown for some Gram-positive pathogens.

Details

Authors
  • Helene Möllerherm
  • Ariane Neumann
  • Katrin Schilcher
  • Stefanie Blodkamp
  • Nathalie E Zeitouni
  • Petra Dersch
  • Petra Lüthje
  • Hassan Y. Naim
  • Annelies S Zinkernagel
  • Maren von Köckritz-Blickwede
External organisations
  • University of Veterinary Medicine Hannover
Research areas and keywords

Keywords

  • Amino Acid Sequence, Bacterial Proteins, Calcium, Endodeoxyribonucleases, Extracellular Traps, Humans, Immunity, Innate, Magnesium, Membrane Proteins, Neutrophils, Sequence Alignment, Serogroup, Yersinia enterocolitica, Journal Article, Research Support, Non-U.S. Gov't
Original languageEnglish
Article numberfnv192
JournalFEMS Microbiology Letters
Volume362
Issue number23
Publication statusPublished - 2015 Dec
Publication categoryResearch
Peer-reviewedYes
Externally publishedYes