A gloverin-like antibacterial protein is synthesized in Helicoverpa armigera following bacterial challenge

James A. Mackintosh*, Andrew A. Gooley, Peter H. Karuso, Andrew J. Beattie, Daniel R. Jardine, Duncan A. Veal

*Corresponding author for this work

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

A bacteria inducible antibacterial protein, P2, was isolated from the old world boll-worm Helicoverpa armigera. Fifth-instar larvae were injected with live Escherichia coli NCTC 8196. P2 was isolated by HPLC using reversed- phase and size-exclusion columns. In addition, P2 was isolated by an alternative method of sequential cation-exchange and reversed-phase HPLC. The structure of P2 was determined by N-terminal Edman degradation and mass spectrometry. P2 had similar mass (14.1 kDa) structure and activity to gloverin, an inducible glycine-rich antibacterial protein isolated from Hyalophora gloveri [Axen, A.; Carlsson, A.; Engstrom, Å.; Bennich, H. Eur. J. Biochem. 247:614-619; 1997]. At the N-terminus P2 had ~60% identity with gloverin. P2 is basic, heat stable, and displayed rapid antibacterial action. P2 was active against the Gram-negative bacteria tested and was inactive against the Gram-positive bacteria, Candida albicans, a bovine turbinate cell line, and pestivirus.

Original languageEnglish
Pages (from-to)387-399
Number of pages13
JournalDevelopmental and Comparative Immunology
Volume22
Issue number4
DOIs
Publication statusPublished - 1 Jul 1998

Keywords

  • gloverin
  • helicoverpa armigera
  • insect immunity
  • peptide antibiotics

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