Defb14, the murine orthologue of human b-defensin-3, displays chemoattracting and antimicrobial properties irrelevant of a dis

نویسندگان

  • Karen Taylor
  • David J. Clarke
  • Bryan McCullough
  • Joost Oppenheim
  • Dusan Uhrin
  • John R. W. Govan
  • Dominic J. Campopiano
  • Derek MacMillan
  • Perdita E. Barran
  • Julia R. Dorin
چکیده

MRC Human Genetics Unit, Edinburgh EH4 2XU, Scotland, U.K. School of Chemistry, University of Edinburgh, Edinburgh EH9 3JJ, UK Laboratory of Molecular Immunoregulation, Center for Cancer Research, Scientific Application and International Cooperation, Inc. (SAIC)-Frederick, National Cancer Institute at Frederick, Frederick, MD 21702, USA. Cystic Fibrosis Laboratory, Medical Microbiology, University of Edinburgh, Department of Chemistry, Christopher Ingold Laboratories, University College London, WC1H 0AJ, UK

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Human b-defensin 3 has immunosuppressive activity in vitro and in vivo

b-defensins are antimicrobial peptides with an essential role in the innate immune response. In addition b-defensins can also chemoattract cells involved in adaptive immunity. Until now, based on evidence from dendritic cell stimulation, human b defensin-3 (hBD3) was considered pro-inflammatory. We present evidence here that hBD3 lacks pro-inflammatory activity in human and mouse primary M/. In...

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Human β-defensin 3 has immunosuppressive activity in vitro and in vivo

Beta-defensins are antimicrobial peptides with an essential role in the innate immune response. In addition beta-defensins can also chemoattract cells involved in adaptive immunity. Until now, based on evidence from dendritic cell stimulation, human beta defensin-3 (hBD3) was considered pro-inflammatory. We present evidence here that hBD3 lacks pro-inflammatory activity in human and mouse prima...

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Peptide Fragments of a ß-defensin Derivative with Potent

22 β-defensins are known to be both antimicrobial and able to chemoattract various 23 immune cells. Although the sequences of paralogous genes are not highly conserved, the core24 defensin structure is retained. Defb14-1C V has similar bactericidal activity to its parent 25 peptide (murine β-defensin Defb14) despite all but one of the canonical six cysteines being 26 substituted with alanines. ...

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Multi-function Plant Defensin, Antimicrobial and Heavy Metal Adsorbent Peptide

Background: Defensin peptide isolated from plants are often heterogeneous in length, sequence and structure, but they are mostly small, cationic and amphipathic. Plant defensins exhibit broad-spectrum antibacterial and antifungal activities against Gram-positive and Gram-negative bacteria, fungi and etc. Plant defensins also play an important role in innate immunity, such as he...

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تاریخ انتشار 2007