A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution

One of the facets of the host defense of higher insects is the rapid and transient synthesis, following bacterial challenge or trauma, of a battery of potent antibacterial peptides (Steiner, H., Hultmark, D., Engstrom, A., Bennich, H., and Boman, H. G. (1981) Nature 292, 246-248). The best character...

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Bibliographic Details
Published in:The Journal of biological chemistry 1993-07, Vol.268 (20), p.14893-14897
Main Authors: Bulet, P, Dimarcq, J.L, Hetru, C, Lagueux, M, Charlet, M, Hegy, G, Dorsselaer, A. van, Hoffmann, J.A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aminoacids, peptides. Hormones. Neuropeptides
AMINOAZUCARES
AMINOSUCRE
Analytical, structural and metabolic biochemistry
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Base Sequence
Biological and medical sciences
Carbohydrates - analysis
Cloning, Molecular
DNA
DROSOPHILA
ESCHERICHIA
Escherichia coli - drug effects
Fundamental and applied biological sciences. Psychology
Gas Chromatography-Mass Spectrometry
Glycopeptides - chemistry
Glycopeptides - genetics
Glycopeptides - pharmacology
Glycosylation
Life Sciences
Molecular Sequence Data
PATHOGENESE
PATOGENESIS
PEPTIDE
PEPTIDOS
PROPIEDADES ANTIMICROBIANAS
PROPRIETE ANTIMICROBIENNE
Proteins
REACCIONES QUIMICAS
REACTION CHIMIQUE
SECUENCIA NUCLEICA
SEQUENCE NUCLEIQUE
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Summary:One of the facets of the host defense of higher insects is the rapid and transient synthesis, following bacterial challenge or trauma, of a battery of potent antibacterial peptides (Steiner, H., Hultmark, D., Engstrom, A., Bennich, H., and Boman, H. G. (1981) Nature 292, 246-248). The best characterized of these peptides are the cecropins (ibid.), 4-kDa peptides devoid of cysteines, and the insect defensins (Hoffmann, J. A., and Hetru, C. (1992) Immunol. Today 13, 411-415), 4- kDa peptides with three intramolecular disulfide bridges. Several other inducible antibacterial peptides have been characterized only at the level of their amino acid sequences (Hoffmann, J. A., Dimarcq, J. L., and Bulet, P. (1992) Medecine and Sciences 8, 432-439). We report here the isolation of a novel 19-residue prolinerich inducible antibacterial peptide from Drosophila. In contrast to all previous reports on antibacterial peptides, this molecule carries a substitution as evidenced by molecular mass determinations; our data show that this reflects the O-glycosylation of a Thr residue by an N-acetylgalactosamine plus a galactose. A synthetic nonsubstituted peptide of identical amino acid sequence has an activity several times lower (5-10) than the native compound. Our data suggest that this substitution represents a post-translational modification essential for the full biological activity of this novel peptide
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)82417-6