Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides

Virology. 2004 Jun 1;323(2):268-75. doi: 10.1016/j.virol.2004.02.029.


The ability of five purified amphibian antimicrobial peptides (dermaseptin-1, temporin A, magainin I, and II, PGLa), crude peptide fractions isolated from the skin of Rana pipiens and R. catesbeiana, and four antimicrobial peptides (AMPs) from hybrid striped bass (piscidin-1N, -1H, -2, and -3) were examined for their ability to reduce the infectivity of channel catfish virus (CCV) and frog virus 3 (FV3). All compounds, with the exception of magainin I, markedly reduced the infectivity of CCV. In contrast to CCV, FV3 was 2- to 4-fold less sensitive to these agents. Similar to an earlier study employing two other amphibian peptides, the agents used here acted rapidly and over a wide, physiologically relevant, temperature range to reduce virus infectivity. These results extend our previous findings and strongly suggest that various amphibian and piscine AMPs may play important roles in protecting fish and amphibians from pathogenic viruses.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amphibian Proteins / chemistry
  • Amphibian Proteins / pharmacology*
  • Animals
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Antiviral Agents / chemistry
  • Antiviral Agents / pharmacology*
  • Bass
  • Cells, Cultured
  • Drug Synergism
  • Herpesviridae / drug effects
  • Herpesviridae / pathogenicity*
  • Ictaluridae / virology
  • Molecular Sequence Data
  • Rana catesbeiana
  • Rana pipiens
  • Ranavirus / drug effects
  • Ranavirus / pathogenicity*
  • Skin / chemistry
  • Virus Inactivation*


  • Amphibian Proteins
  • Antimicrobial Cationic Peptides
  • Antiviral Agents