Plant Cell Reports

, Volume 26, Issue 8, pp 1391–1398

Arabidopsis thaliana plants expressing human beta-defensin-2 are more resistant to fungal attack: functional homology between plant and human defensins

  • An M. Aerts
  • Karin Thevissen
  • Sara M. Bresseleers
  • Jan Sels
  • Piet Wouters
  • Bruno P. A. Cammue
  • Isabelle E. J. A. François
Biotic and Abiotic Stress

DOI: 10.1007/s00299-007-0329-4

Cite this article as:
Aerts, A.M., Thevissen, K., Bresseleers, S.M. et al. Plant Cell Rep (2007) 26: 1391. doi:10.1007/s00299-007-0329-4

Abstract

Human beta-defensin-2 (hBD-2) is a small antimicrobial peptide with potent activity against different Gram-negative bacteria and fungal/yeast species. Since human beta-defensins and plant defensins share structural homology, we set out to analyse whether there also exists a functional homology between these defensins of different eukaryotic kingdoms. To this end, we constructed a plant transformation vector harbouring the hBD-2 coding sequence, which we transformed to Arabidopsis thaliana plants, giving rise to A. thaliana plants indeed expressing hBD-2. Furthermore, we could demonstrate that this heterologously produced hBD-2 possesses antifungal activity in vitro. Finally, we could show that hBD-2 expressing A. thaliana plants are more resistant against the broad-spectrum fungal pathogen Botrytis cinerea as compared to untransformed A. thaliana plants, and that this resistance is correlated with the level of active hBD-2 produced in these transgenic plants. Hence, we demonstrated a functional homology, next to the already known structural homology, between defensins originating from different eukaryotic kingdoms. To our knowledge, this is the first time that this is specifically demonstrated for plant and mammalian defensins.

Keywords

Arabidopsis thaliania Botrytis cinerea Human defensin Plant defensin 

Abbreviations

AMP

Antimicrobial protein

CRP

Cross-reactive protein

Dm-AMP

Dahlia merckii antimicrobial protein

hBD-2

Human beta-defensin-2

IC50

Concentration causing 50% inhibition of fungal growth

MAR

Matrix attachment region

PTGS

Post-transcriptional gene silencing

RsAFP

Raphanus sativus antifungal protein

Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • An M. Aerts
    • 1
  • Karin Thevissen
    • 1
  • Sara M. Bresseleers
    • 1
  • Jan Sels
    • 1
  • Piet Wouters
    • 1
  • Bruno P. A. Cammue
    • 1
  • Isabelle E. J. A. François
    • 1
  1. 1.Centre of Microbial and Plant GeneticsKatholieke Universiteit LeuvenHeverleeBelgium

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