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Open Access

Carbon Nanoparticles Inhibit the Antimicrobial Activities of the Human Cathelicidin LL-37 through Structural Alteration

Fern Findlay, Jan Pohl, Pavel Svoboda, Priyanka Shakamuri, Kevin McLean, Neil F. Inglis, Lorna Proudfoot and Peter G. Barlow
J Immunol August 16, 2017, ji1700706; DOI: https://doi.org/10.4049/jimmunol.1700706
Fern Findlay
*School of Applied Sciences, Edinburgh Napier University, Edinburgh EH11 4BN, United Kingdom;
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Jan Pohl
†Biotechnology Core Facility Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; and
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Pavel Svoboda
†Biotechnology Core Facility Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; and
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Priyanka Shakamuri
†Biotechnology Core Facility Branch, Centers for Disease Control and Prevention, Atlanta, GA 30333; and
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Kevin McLean
‡Moredun Proteomics Facility, Moredun Research Institute, Penicuik EH26 0PZ, United Kingdom
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Neil F. Inglis
‡Moredun Proteomics Facility, Moredun Research Institute, Penicuik EH26 0PZ, United Kingdom
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Lorna Proudfoot
*School of Applied Sciences, Edinburgh Napier University, Edinburgh EH11 4BN, United Kingdom;
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Peter G. Barlow
*School of Applied Sciences, Edinburgh Napier University, Edinburgh EH11 4BN, United Kingdom;
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Abstract

Host defense peptides, also known as antimicrobial peptides, are key elements of innate host defense. One host defense peptide with well-characterized antimicrobial activity is the human cathelicidin, LL-37. LL-37 has been shown to be upregulated at sites of infection and inflammation and is regarded as one of the primary innate defense molecules against bacterial and viral infection. Human exposure to combustion-derived or engineered nanoparticles is of increasing concern, and the implications of nanomaterial exposure on the human immune response is poorly understood. However, it is widely acknowledged that nanoparticles can interact strongly with several immune proteins of biological significance, with these interactions resulting in structural and functional changes of the proteins involved. This study investigated whether the potent antibacterial and antiviral functions of LL-37 were inhibited by exposure to, and interaction with, carbon nanoparticles, together with characterizing the nature of the interaction. LL-37 was exposed to carbon black nanoparticles in vitro, and the antibacterial and antiviral functions of the peptide were subsequently assessed. We demonstrate a substantial loss of antimicrobial function when the peptide was exposed to low concentrations of nanomaterials, and we further show that the nanomaterial-peptide interaction resulted in a significant change in the structure of the peptide. The human health implications of these findings are significant, as, to our knowledge, this is the first evidence that nanoparticles can alter host defense peptide structure and function, indicating a new role for nanoparticle exposure in increased disease susceptibility.

Footnotes

  • This work was supported by an Edinburgh Napier University Research Studentship (to F.F.) and Tenovus Scotland (E12/01) (to P.G.B.).

  • Received May 12, 2017.
  • Accepted July 22, 2017.
  • Copyright © 2017 by The American Association of Immunologists, Inc.

This article is distributed under The American Association of Immunologists, Inc., Reuse Terms and Conditions for Author Choice articles.

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The Journal of Immunology: 209 (3)
The Journal of Immunology
Vol. 209, Issue 3
1 Aug 2022
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Carbon Nanoparticles Inhibit the Antimicrobial Activities of the Human Cathelicidin LL-37 through Structural Alteration
Fern Findlay, Jan Pohl, Pavel Svoboda, Priyanka Shakamuri, Kevin McLean, Neil F. Inglis, Lorna Proudfoot, Peter G. Barlow
The Journal of Immunology August 16, 2017, ji1700706; DOI: 10.4049/jimmunol.1700706

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Carbon Nanoparticles Inhibit the Antimicrobial Activities of the Human Cathelicidin LL-37 through Structural Alteration
Fern Findlay, Jan Pohl, Pavel Svoboda, Priyanka Shakamuri, Kevin McLean, Neil F. Inglis, Lorna Proudfoot, Peter G. Barlow
The Journal of Immunology August 16, 2017, ji1700706; DOI: 10.4049/jimmunol.1700706
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