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10.4049/jimmunol.1601226

http://scihub22266oqcxt.onion/10.4049/jimmunol.1601226
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suck abstract from ncbi


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pmid28411186
      J+Immunol 2017 ; 198 (10 ): 4036-4045
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  • Direct Antimicrobial Activity of IFN-? #MMPMID28411186
  • Kaplan A ; Lee MW ; Wolf AJ ; Limon JJ ; Becker CA ; Ding M ; Murali R ; Lee EY ; Liu GY ; Wong GCL ; Underhill DM
  • J Immunol 2017[May]; 198 (10 ): 4036-4045 PMID28411186 show ga
  • 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-? is antimicrobial. Parts of the IFN-? molecular surface (especially helix 4) are cationic and amphipathic, both classic characteristics of antimicrobial peptides, and we observed that IFN-? can directly kill Staphylococcus aureus Further, a mutant S. aureus that is more sensitive to antimicrobial peptides was killed more efficiently by IFN-? than was the wild-type S. aureus, and immunoblotting showed that IFN-? interacts with the bacterial cell surface. To determine whether specific parts of IFN-? are antimicrobial, we synthesized IFN-? 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-? may be directly antimicrobial and be part of a growing family of cytokines and chemokines, called kinocidins, that also have antimicrobial properties.
  • |Animals [MESH]
  • |Anti-Bacterial Agents/*pharmacology [MESH]
  • |Antimicrobial Cationic Peptides/chemistry/pharmacology [MESH]
  • |Cell Membrane/*drug effects [MESH]
  • |Humans [MESH]
  • |Interferon-beta/chemistry/metabolism/pharmacology/*physiology [MESH]
  • |Mice [MESH]
  • |Microbial Sensitivity Tests [MESH]
  • |Staphylococcal Infections/microbiology [MESH]
  • |Staphylococcus aureus/*drug effects/genetics [MESH]


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