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Determination of the disulfide array of the first inducible antifungal peptide from insects: drosomycin from Drosophila melanogaster
Author(s) -
Michaut Lydia,
Fehlbaum Pascale,
Moniatte Marc,
Van Dorsselaer Alain,
Reichhart Jean-Marc,
Bulet Philippe
Publication year - 1996
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 - 10.1016/0014-5793(96)00992-1
Subject(s) - edman degradation , peptide , drosophila melanogaster , mode of action , disulfide bond , complementary dna , antifungal , biology , cyclic peptide , biochemistry , gene , residue (chemistry) , intramolecular force , chemistry , peptide sequence , stereochemistry , microbiology and biotechnology
Drosomycin is a 44‐residue antifungal peptide with four intramolecular disulfide bridges which have been isolated from immune‐challenged Drosophila . To produce adequate amounts of this peptide for 3D‐structure analysis, studies on the mode of action and activity spectrum, we expressed a synthetic cDNA in Saccharomyces cerevisiae . For this purpose, we used the mating factor α gene and concomitantly overexpressed the KEX2 gene to increase the yield of fully processed drosomycin. Using a combination of Edman degradation and mass spectrometry, we show that drosomycin shares the same array of intramolecular disulfide bridges than plant defensins, in addition to their sequence similarities.