Characterization and cDNA cloning of a defensin-like peptide, harmoniasin, from Harmonia axyridis

J Microbiol Biotechnol. 2012 Nov;22(11):1588-90. doi: 10.4014/jmb.1206.06064.

Abstract

We compared the mRNA expression profile of the Harmonia axyridis larvae that were either untreated or treated with LPS. The extracted mRNAs were subjected to ACP RTPCR analysis using a combination of arbitrary primers and oligo (dT) primer. Among the 47 DEGs differentially expressed, we identified a cDNA showing homology with defensin-like antibacterial peptide. The cDNA showed a putative 32-residue signal sequence and a 50-residue mature peptide named harmoniasin. We also investigated the antibacterial activity of the harmoniasin analog, which exhibited potent antibacterial activities against Gramnegative and -positive bacteria strains and it also evidenced no hemolytic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology
  • Bacteria / drug effects
  • Base Sequence
  • Cloning, Molecular*
  • Coleoptera / chemistry
  • Coleoptera / genetics*
  • Coleoptera / metabolism
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • DNA, Complementary / metabolism
  • Defensins / chemistry
  • Defensins / genetics*
  • Defensins / metabolism
  • Defensins / pharmacology
  • Insect Proteins / chemistry
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism
  • Insect Proteins / pharmacology
  • Molecular Sequence Data
  • Protein Sorting Signals
  • Sequence Homology, Amino Acid

Substances

  • Anti-Bacterial Agents
  • DNA, Complementary
  • Defensins
  • Insect Proteins
  • Protein Sorting Signals