Five disulfide bridges stabilize a hevein‐type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.)

FEBS Letters

Peumans, Willy J²  Van Damme, Jo¹  Coosemans, Jozef²  Proost, Paul¹  Van den Bergh, Karolien P.B²  Van Damme, Els J.M² 

[1] Laboratory of Molecular Immunology, Katholieke Universiteit Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium;Laboratory of Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, 3001 Leuven, Belgium

关键词: Antimicrobial peptide;    Bark;    Hevein;    Spindle tree;    Euonymus europaeus L;   

DOI  :  10.1016/S0014-5793(02)03474-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A small 45 amino acid residue antifungal polypeptide was isolated from the bark of spindle tree (Euonymus europaeus L.). Though the primary structure of this so-called E. europaeus chitin-binding protein or Ee-CBP is highly similar to the hevein domain, it distinguishes itself from most previously identified hevein-type antimicrobial peptides (AMP) by the presence of two extra cysteine residues that form an extra disulfide bond. Due to these five disulfide bonds Ee-CBP is a remarkably stable protein. Agar diffusion and microtiterplate assays demonstrated that Ee-CBP is a potent antimicrobial protein. IC₅₀-values as low as 1 μg/ml were observed for the fungus Botrytis cinerea. Comparative assays further demonstrated that Ee-CBP is a stronger inhibitor of fungal growth than Ac-AMP2 from Amaranthus caudatus seeds, which is considered one of the most potent antifungal hevein-type plant proteins.

【 授权许可】

Unknown