Halocyntin and papillosin, two new antimicrobial peptides isolated from hemocytes of the solitary tunicate, Halocynthia papillosa

J Pept Sci. 2009 Jan;15(1):48-55. doi: 10.1002/psc.1101.

Abstract

We report here the screening of five marine invertebrate species from two taxa (tunicates and echinoderms) for the presence of cationic antimicrobial peptides (AMP) in defence cells (hemocytes). Antimicrobial activities were detected only in the two tunicates Microcosmus sabatieri and Halocynthia papillosa. In addition, we report the isolation and characterization of two novel peptides from H. papillosa hemocytes. These molecules display antibacterial activity against Gram-positive and Gram-negative bacteria. Complete peptide characterization was obtained by a combination of Edman degradation and mass spectrometry. The mature molecules, named halocyntin and papillosin, comprise 26 and 34 amino acid residues, respectively. Their primary structure display no significant similarities with previously described AMP.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / isolation & purification
  • Anti-Bacterial Agents / pharmacology*
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / isolation & purification
  • Antimicrobial Cationic Peptides / pharmacology*
  • Circular Dichroism
  • Erythrocytes / drug effects
  • Hemocytes / chemistry*
  • Microbial Viability / drug effects
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / isolation & purification
  • Peptides / pharmacology*
  • Sheep
  • Urochordata / chemistry*

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Peptides
  • halocyntin protein, Halocynthia papillosa
  • papillosin protein, Halocynthia papillosa