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Five disulfide bridges stabilize a hevein‐type antimicrobial peptide from the bark of spindle tree ( Euonymus europaeus L.)
Author(s) -
Van den Bergh Karolien P.B,
Proost Paul,
Van Damme Jo,
Coosemans Jozef,
Van Damme Els J.M,
Peumans Willy J
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03474-9
Subject(s) - antimicrobial , biochemistry , cysteine , chemistry , peptide , residue (chemistry) , biology , microbiology and biotechnology , enzyme
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. IC 50 ‐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.