Antimicrobial action of achacin is mediated by L-amino acid oxidase activity

FEBS Lett. 2002 Nov 20;531(3):509-12. doi: 10.1016/s0014-5793(02)03608-6.

Abstract

Achacin is an antibacterial glycoprotein purified from the mucus of the giant snail, Achatina fulica Férussac, as a humoral defense factor. We showed that achacin has L-amino acid oxidase activity and can generate cytotoxic H(2)O(2); however, the concentration of H(2)O(2) was not sufficient to kill bacteria. The antibacterial activity of achacin was inhibited by various H(2)O(2) scavengers. Immunochemical analysis revealed that achacin was preferentially bound to growth-phase bacteria, accounting for the important role in growth-phase-dependent antibacterial activity of achacin. Achacin may act as an important defense molecule against invading bacteria.

MeSH terms

  • Amino Acid Oxidoreductases / metabolism*
  • Amino Acid Sequence
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology*
  • Escherichia coli / drug effects
  • Hydrogen Peroxide / metabolism
  • L-Amino Acid Oxidase
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Neuropeptides / chemistry
  • Neuropeptides / pharmacology*
  • Sequence Homology, Amino Acid
  • Staphylococcus aureus / drug effects

Substances

  • Anti-Bacterial Agents
  • Neuropeptides
  • achacin
  • Hydrogen Peroxide
  • Amino Acid Oxidoreductases
  • L-Amino Acid Oxidase