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

82 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

Fingerprint

Dive into the research topics of 'Isolation from an ant <i>Myrmecia gulosa</i> of two inducible <i>O</i>-glycosylated proline-rich antibacterial peptides'. Together they form a unique fingerprint.

Cite this