Title: Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins
Authors: Broekaert, Willem ×
Mariën, W.
Terras, F.R.
De Bolle, Miguel
Proost, Paul
Van Damme, Jozef
Dillen, L.
Claeys, M.
Rees, S.B.
Vanderleyden, Jozef
Cammue, Bruno #
Issue Date: May-1992
Publisher: American Chemical Society
Series Title: Biochemistry vol:31 issue:17 pages:4308-4314
Abstract: Two antimicrobial peptides (Ac-AMP1 and Ac-AMP2) were isolated from seeds of amaranth (Amaranthus caudatus), and their physicochemical and biological properties were characterized. On the basis of fast atom bombardment mass spectroscopy, Ac-AMP1 and Ac-AMP2 have monoisotopic molecular masses of 3025 and 3181, respectively. Both proteins have pI values above 10. The amino acid sequence of Ac-AMP1 (29 residues) is identical to that of Ac-AMP2 (30 residues), except that the latter has 1 additional residue at the carboxyl terminus. The sequences are highly homologous to the cysteine/glycine-rich domain occurring in many chitin-binding proteins. Both Ac-AMP1 and Ac-AMP2 bind to chitin in a reversible way. Ac-AMP1 and Ac-AMP2 inhibit the growth of different plant pathogenic fungi at much lower doses than other known antifungal chitin-binding proteins. In addition, they show some activity on Gram-positive bacteria. The antimicrobial effect of Ac-AMP1 and Ac-AMP2 is strongly antagonized by cations.
ISSN: 0006-2960
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Academic Center for General Practice
Centre of Microbial and Plant Genetics
Laboratory of Molecular Immunology (Rega Institute)
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science