Abstract

Analysis of rhesus macaque leukocytes disclosed the presence of an 18-residue macrocyclic, tridisulfide antibiotic peptide in granules of neutrophils and monocytes. The peptide, termed rhesus theta defensin-1 (RTD-1), is microbicidal for bacteria and fungi at low micromolar concentrations. Antibacterial activity of the cyclic peptide was threefold greater than that of an open-chain analog, and the cyclic conformation was required for antimicrobial activity in the presence of 150 millimolar sodium chloride. Biosynthesis of RTD-1 involves the head-to-tail ligation of two α-defensin–related nonapeptides, requiring the formation of two new peptide bonds. Thus, host defense cells possess mechanisms for synthesis and granular packaging of macrocyclic antibiotic peptides that are components of the phagocyte antimicrobial armamentarium.

Keywords

PeptideAntimicrobialAntimicrobial peptidesChemistryCyclic peptideLigationBiochemistryDefensinAntibioticsPeptide bondBeta defensinPhagocyteBiologyMicrobiologyMolecular biologyPhagocytosis

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Year
1999
Type
article
Volume
286
Issue
5439
Pages
498-502
Citations
686
Access
Closed

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Yi‐Quan Tang, Jun Yuan, George Ösapay et al. (1999). A Cyclic Antimicrobial Peptide Produced in Primate Leukocytes by the Ligation of Two Truncated α-Defensins. Science , 286 (5439) , 498-502. https://doi.org/10.1126/science.286.5439.498

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DOI
10.1126/science.286.5439.498