| Literature DB >> 28411186 |
Amber Kaplan1, Michelle W Lee2,3,4, Andrea J Wolf5, Jose J Limon5, Courtney A Becker5, Minna Ding5, Ramachandran Murali6, Ernest Y Lee2,3,4, George Y Liu3,7, Gerard C L Wong8,3,4, David M Underhill9,6.
Abstract
Type I IFNs are a cytokine family essential for antiviral defense. More recently, type I IFNs were shown to be important during bacterial infections. In this article, we show that, in addition to known cytokine functions, IFN-β is antimicrobial. Parts of the IFN-β molecular surface (especially helix 4) are cationic and amphipathic, both classic characteristics of antimicrobial peptides, and we observed that IFN-β can directly kill Staphylococcus aureus Further, a mutant S. aureus that is more sensitive to antimicrobial peptides was killed more efficiently by IFN-β than was the wild-type S. aureus, and immunoblotting showed that IFN-β interacts with the bacterial cell surface. To determine whether specific parts of IFN-β are antimicrobial, we synthesized IFN-β helix 4 and found that it is sufficient to permeate model prokaryotic membranes using synchrotron x-ray diffraction and that it is sufficient to kill S. aureus These results suggest that, in addition to its well-known signaling activity, IFN-β may be directly antimicrobial and be part of a growing family of cytokines and chemokines, called kinocidins, that also have antimicrobial properties.Entities:
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Year: 2017 PMID: 28411186 PMCID: PMC5469413 DOI: 10.4049/jimmunol.1601226
Source DB: PubMed Journal: J Immunol ISSN: 0022-1767 Impact factor: 5.422