| Literature DB >> 27177697 |
Alexander Stephan1, Marina Batinica1, Julia Steiger1, Pia Hartmann2,3,4,5, Frank Zaucke6, Wilhelm Bloch7, Mario Fabri1,8.
Abstract
As part of the innate host response neutrophils release neutrophil extracellular traps (NETs), protein:DNA complexes that contain a number of antimicrobial peptides (AMPs), such as cathelicidin. Human cathelicidin in its active form, LL37, has potent antimicrobial activity against bacteria. However, whether LL37 derived from NETs contributes to antimicrobial activity against intracellular pathogens remains unclear. Here, we report that NETs induced by mycobacteria contain cathelicidin. Human macrophages internalized NET-bound cathelicidin, which is transported to lysosomal compartments. Furthermore, using a model of in vitro-generated LL37:DNA complexes we found that LL37 derived from such complexes attacks mycobacteria in macrophage phagolysosomes resulting in antimicrobial activity. Taken together, our results suggest a mechanism by which LL37 in complex with DNA contributes to host defence against intracellular bacteria in human macrophages.Entities:
Keywords: LL37; cathelicidin; macrophage; mycobacteria; neutrophil extracellular trap
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Year: 2016 PMID： 27177697 PMCID： PMC4948035 DOI： 10.1111/imm.12620
Source DB: PubMed Journal: Immunology ISSN： 0019-2805 Impact factor: 7.397