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• W2170594801 abstract "Abstract Cathelicidins constitute potent antimicrobial peptides characterized by a high cationic charge that enables strong interactions with nucleic acids. In fact, the only human cathelicidin LL-37 triggers rapid sensing of nucleic acids by plasmacytoid dendritic cells (pDC). Among the porcine cathelicidins, phylogenetic analysis of the C-terminal mature peptide showed that porcine myeloid antimicrobial peptide (PMAP)-36 was the most closely related of the 11 porcine cathelicidins to human LL-37. Despite several investigations evaluating potent antimicrobial functions of porcine cathelicidins, nothing is known about their ability to promote pDC activation. We therefore investigated the capacity of the proline-arginine–rich 39-aa peptide, PMAP-23, PMAP-36, and protegrin-1 to complex with bacterial DNA or synthetic RNA molecules and facilitate pDC activation. We demonstrate that these peptides mediate a rapid and efficient uptake of nucleic acids within minutes, followed by robust IFN-α responses. The highest positively charged cathelicidin, PMAP-36, was found to be the most potent peptide tested for this effect. The peptide–DNA complexes were internalized and also found to associate with the cell membranes of pDC. The amphipathic conformation typical of PMAP-36 was not required for IFN-α induction in pDC. We also demonstrate that PMAP-36 can mediate IFN-α induction in pDC stimulated by Escherichia coli, which alone fail to activate pDC. This response was weaker with a scrambled PMAP-36, relating to its lower antimicrobial activity. Collectively, our data suggest that the antimicrobial and nucleic acid–complexing properties of cathelicidins can mediate pDC activation-promoting adaptive immune responses against microbial infections." @default.
• W2170594801 created "2016-06-24" @default.
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• W2170594801 date "2014-07-01" @default.
• W2170594801 modified "2023-10-02" @default.
• W2170594801 title "Porcine Cathelicidins Efficiently Complex and Deliver Nucleic Acids to Plasmacytoid Dendritic Cells and Can Thereby Mediate Bacteria-Induced IFN-α Responses" @default.
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• W2170594801 doi "https://doi.org/10.4049/jimmunol.1303219" @default.
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