Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides

James A. Mackintosh*, Duncan A. Veal, Andrew J. Beattie, Andrew A. Gooley

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    85 Citations (Scopus)

    Abstract

    Reported here is the isolation and characterization of two antibacterial peptides synthesized in an ant Myrmecia gulosa in response to bacterial challenge. The peptides were purified by reversed-phase high performance liquid chromatography and characterized by peptide sequencing and mass spectrometry. Both peptides were formed from 16 amino acids, were rich in proline (~30%), and had N-acetylgalactosamine O-linked to a conserved threonine. The activity of a synthetic non-glycosylated isoform was markedly reduced demonstrating that glycosylation was necessary for maximum activity. The peptides were active only against growing Escherichia coli. They were inactive against stationary cells, Gram-positive bacteria, the yeast Candida albicans, two species of mammalian cells, and bovine pestivirus.

    Original languageEnglish
    Pages (from-to)6139-6143
    Number of pages5
    JournalJournal of Biological Chemistry
    Volume273
    Issue number11
    DOIs
    Publication statusPublished - 13 Mar 1998

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