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Ubiquitously expressed Human Beta Defensin 1 (hBD1) forms bacteria-entrapping nets in a redox dependent mode of action

Raschig, Judith ; Mailänder-Sánchez, Daniela ; Berscheid, Anne ; Berger, Jürgen ; Strömstedt, Adam A ; Courth, Lioba F ; Malek, Nisar P ; Brötz-Oesterhelt, Heike ; Wehkamp, Jan; Monack, Denise M. (editor)

PLoS Pathogens, 2017, Vol.13(3) [Tạp chí có phản biện]

ISSN: 1553-7366 ; E-ISSN: 1553-7374 ; DOI: 10.1371/journal.ppat.1006261 ; PMCID: 5376342 ; PMID: 28323883

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  • Nhan đề:
    Ubiquitously expressed Human Beta Defensin 1 (hBD1) forms bacteria-entrapping nets in a redox dependent mode of action
  • Tác giả: Raschig, Judith ; Mailänder-Sánchez, Daniela ; Berscheid, Anne ; Berger, Jürgen ; Strömstedt, Adam A ; Courth, Lioba F ; Malek, Nisar P ; Brötz-Oesterhelt, Heike ; Wehkamp, Jan
  • Monack, Denise M. (editor)
  • Chủ đề: Research Article ; Biology And Life Sciences ; Biology And Life Sciences ; Medicine And Health Sciences ; Biology And Life Sciences ; Research And Analysis Methods ; Physical Sciences ; Physical Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Medicine And Health Sciences ; Medicine And Health Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Medicine And Health Sciences ; Biology And Life Sciences
  • Là 1 phần của: PLoS Pathogens, 2017, Vol.13(3)
  • Mô tả: Ever since the discovery of endogenous host defense antimicrobial peptides it has been discussed how these evolutionary conserved molecules avoid to induce resistance and to remain effective. Human ß-defensin 1 (hBD1) is an ubiquitously expressed endogenous antimicrobial peptide that exhibits qualitatively distinct activities between its oxidized and reduced forms. Here, we explore these antimicrobial mechanisms. Surprisingly, using electron microscopy we detected a so far unknown net-like structure surrounding bacteria, which were treated with the reduced but not the oxidized form of hBD1. A transmigration assay demonstrated that hBD1-derived nets capture bacteria and inhibit bacterial transmigration independent of bacterial killing. The presence of nets could completely prevent migration of hBD1 resistant pathogens and are stable in the presence of human duodenal secretion with a high amount of proteases. In contrast to HD6, cysteins are necessary for net formation. This redox-dependent function serves as an additional mechanism of action for hBD1 and differs from net formation by other defensins such as Paneth cell-derived human α-defensin 6 (HD6). While hBD1red and hBD1ox have distinct antimicrobial profiles and functions, only the reduced form provides additional host protection by entrapping bacteria in extracellular net structures preventing bacterial invasion. Better understanding of the modes of action of endogenous host peptides will help to find new antimicrobial strategies. Author summary The human body is constantly challenged by commensal and by pathogenic bacteria. Antimicrobial molecules of the innate immune system protect the human body from bacterial overgrowth and keep human microbiota in balance. One of the most prominent antimicrobial molecules is the human beta defensin 1 (hBD1). It is, in contrast to other defensins, constantly expressed by epithelial cells and exhibit diverse host antimicrobial strategies, which are much more complex than expected some years ago. Here, we aimed to study the unknown mechanisms of the different redox forms of hBD1. We detected, besides bacterial cell wall disruption, a so far unknown net-like structure surrounding bacteria, which entraps bacteria, independent of bacterial components and antimicrobial activity. Of note, these nets are depending on the amino acid cysteine and these nets are stable even in the presence of physiological human duodenal fluid. We demonstrated that net formation by reduced hBD1 prevents bacterial translocation, including hBD1 resistant pathogens. These findings highlight the complexity of these conserved antimicrobial defense mechanisms and help to find new antimicrobial strategies.
  • Số nhận dạng: ISSN: 1553-7366 ; E-ISSN: 1553-7374 ; DOI: 10.1371/journal.ppat.1006261 ; PMCID: 5376342 ; PMID: 28323883

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