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

• Published in: Plant cell reports 2007-08, Vol.26 (8), p.1391-1398
• Main Authors: Aerts, An M, Thevissen, Karin, Bresseleers, Sara M, Sels, Jan, Wouters, Piet, Cammue, Bruno P. A, François, Isabelle E. J. A
• Format: Article
• Language: English
• Subjects: Arabidopsis - genetics; Arabidopsis - microbiology; Arabidopsis thaliana; Arabidopsis thaliania; Bacteria; beta-Defensins - genetics; beta-Defensins - metabolism; Biological and medical sciences; Biotechnology; Botrytis - physiology; Botrytis cinerea; Flowers & plants; Fundamental and applied biological sciences. Psychology; Genetic engineering; Genetic technics; Human defensin; Humans; Methods. Procedures. Technologies; Plant defensin; Plant Diseases - genetics; Plant Diseases - microbiology; Plants, Genetically Modified; Transgenic animals and transgenic plants; Transgenic plants; Yeasts
• ISSN: 0721-7714; 1432-203X
• DOI: 10.1007/s00299-007-0329-4

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.