Activities of temporin family peptides against the chytrid fungus (Batrachochytrium dendrobatidis) associated with global amphibian declines

Antimicrob Agents Chemother. 2003 Mar;47(3):1157-60. doi: 10.1128/AAC.47.3.1157-1160.2003.

Abstract

Temporin A and structurally related peptides produced in amphibian dermal granular glands and in wasp venom were tested for growth inhibition of Batrachochytrium dendrobatidis, a pathogen associated with global amphibian declines. Two natural amphibian temporins, a wasp temporin, and six synthetic analogs effectively inhibited growth. Differences in potency due to amino acid substitution suggest that ability to penetrate membranes and form an alpha-helical structure is important for their effectiveness against this pathogen.

Publication types

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

MeSH terms

  • Amino Acid Substitution
  • Amphibians / microbiology*
  • Animal Diseases / transmission*
  • Animals
  • Anti-Infective Agents / chemical synthesis
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / pharmacology*
  • Antimicrobial Cationic Peptides
  • Fungi / drug effects*
  • Fungi / growth & development
  • Microbial Sensitivity Tests
  • Mycoses / transmission
  • Mycoses / veterinary*
  • Population
  • Proteins / chemical synthesis
  • Proteins / chemistry
  • Proteins / pharmacology*
  • Wasp Venoms / chemistry

Substances

  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Proteins
  • Wasp Venoms
  • temporin