The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps

Research output: Contribution to journalArticle

Abstract

NETs (neutrophil extracellular traps) have been described as a fundamental innate immune defence mechanism. During formation of NETs, the nuclear membrane is disrupted by an as-yet unknown mechanism. In the present study we investigated the role of human cathelicidin LL-37 in nuclear membrane disruption and formation of NETs. Immunofluorescence microscopy revealed that 5 μM LL-37 significantly facilitated NET formation by primary human blood-derived neutrophils alone, in the presence of the classical chemical NET inducer PMA or in the presence of Staphylococcus aureus. Parallel assays with a random LL-37 fragment library indicated that the NET induction is mediated by the hydrophobic character of the peptide. The trans-localization of LL-37 towards the nucleus and the disruption of the nuclear membrane were visualized using confocal fluorescence microscopy. In conclusion, the present study demonstrates a novel role for LL-37 in the formation of NETs.

Details

Authors
  • Ariane Neumann
  • Evelien T. M. Berends
  • Andreas Nerlich
  • E. Margo Molhoek
  • Richard L. Gallo
  • Timo Meerloo
  • Victor Nizet
  • Hassan Y. Naim
  • Maren von Köckritz-Blickwede
External organisations
  • University of Veterinary Medicine Hannover
Research areas and keywords

Keywords

  • Amino Acid Sequence, Animals, Cathelicidins, Extracellular Traps, Humans, Male, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Neutrophils, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
Original languageEnglish
Pages (from-to)3-11
Number of pages9
JournalThe Biochemical journal
Volume464
Issue number1
StatePublished - 2014 Nov 15
Publication categoryResearch
Peer-reviewedYes
Externally publishedYes