Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds

J Biol Chem. 1992 Feb 5;267(4):2228-33.

Abstract

We have isolated from seeds of Mirabilis jalapa L. two antimicrobial peptides, designated Mj-AMP1 and Mj-AMP2, respectively. These peptides are highly basic and consist of 37 and 36 residues for Mj-AMP1 and Mj-AMP2, respectively. Both peptides contain three disulfide bridges and differ from one another only by 4 amino acids. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the reduced and unreduced peptides suggests that the peptides associate into dimers in their native form. The Mj-AMPs exhibit a broad spectrum of antifungal activity since they are active against all 13 tested plant pathogenic fungi. Concentrations required for 50% inhibition of fungal growth vary from 6 to 300 micrograms/ml for Mj-AMP1 and from 0.5 to 20 micrograms/ml for Mj-AMP2. These peptides were also active on two tested Gram-positive bacteria but were apparently nontoxic for Gram-negative bacteria and cultured human cells. Although the Mj-AMPs show sequence similarity to mu-agatoxins, a class of insecticidal neurotoxic peptides isolated from the venom of spiders, they do not affect pulse transmission in insect nerves.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / isolation & purification
  • Anti-Bacterial Agents / pharmacology*
  • Anti-Bacterial Agents / toxicity
  • Antifungal Agents / pharmacology
  • Cells, Cultured
  • Chromatography, Ion Exchange
  • Cockroaches / drug effects
  • Electrophoresis, Polyacrylamide Gel
  • Endothelium, Vascular / drug effects
  • Fibroblasts / drug effects
  • Humans
  • Mass Spectrometry
  • Molecular Sequence Data
  • Neurons / drug effects
  • Peptides / isolation & purification
  • Peptides / pharmacology*
  • Peptides / toxicity
  • Plant Proteins / isolation & purification
  • Plant Proteins / pharmacology*
  • Plant Proteins / toxicity
  • Seeds / chemistry

Substances

  • AMP1 protein, Mirabilis jalapa
  • AMP2 protein, Mirabilis jalapa
  • Anti-Bacterial Agents
  • Antifungal Agents
  • Peptides
  • Plant Proteins