Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure

J Biol Chem. 1988 Nov 15;263(32):16709-13.

Abstract

A cationic peptide, designated tachyplesin, was isolated from acid extracts of horseshoe crab (Tachypleus tridentatus) hemocyte debris. It consists of 17 residues and the structure determined by Edman degradation is: (formula; see text) The carboxyl-terminal end of this peptide was identified as arginine alpha-amide, and the whole sequence including the alpha-amide was also confirmed by fast atom bombardment mass spectrometry, indicating a mass value of 2263. Tachyplesin inhibits growth of both Gram-negative and -positive bacteria at low concentrations and formed a complex with bacterial lipopolysaccharide. Tachyplesin seems likely to act as antimicrobial peptide for self-defense in the horseshoe crab against invading microorganisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Anti-Bacterial Agents / analysis
  • Anti-Bacterial Agents / isolation & purification*
  • Antimicrobial Cationic Peptides*
  • Blood Cells / analysis*
  • Brachyura / analysis*
  • DNA-Binding Proteins*
  • Gram-Negative Bacteria / drug effects
  • Gram-Positive Bacteria / drug effects
  • Hemocytes / analysis*
  • Immunodiffusion
  • Mass Spectrometry
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Peptides / analysis
  • Peptides / isolation & purification*
  • Peptides, Cyclic*

Substances

  • Amino Acids
  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • DNA-Binding Proteins
  • Peptides
  • Peptides, Cyclic
  • tachyplesin peptide, Tachypleus tridentatus