The defensive system of tree frog skin identified by peptidomics and RNA sequencing analysis

Amino Acids. 2019 Feb;51(2):345-353. doi: 10.1007/s00726-018-2670-z. Epub 2018 Oct 23.

Abstract

The diversity of defensive peptides from skin of amphibians has been demonstrated. These peptides may have resulted from the diversity of microorganisms encountered by amphibians. In this study, peptidomics and RNA sequencing analyses were used to study deeply the defensive peptides of the skin secretions from Polypedates megacephalus. A total of 99 defensive peptides have been identified from the skin secretions. Among these peptides, 3 peptides were myotropical peptides and 34 peptides classified as protease inhibitor peptides. 5 lectins, 8 antimicrobial peptides, 26 immunomodulatory peptides, 10 wound-healing peptides and 13 other bioactive peptides were identified as belonging to the innate immune system. One antimicrobial peptide Pm-amp1 showed high similarity to antimicrobial peptide marcin-18. This peptide was successfully expressed and showed moderate activity against four tested strains. These identified peptides highlight the extensive diversity of defensive peptides and provide powerful tools to understand the defense weapon of frog.

Keywords: Antimicrobial peptide; Defensive peptides; Frog.

MeSH terms

  • Amphibian Proteins / chemistry*
  • Amphibian Proteins / genetics*
  • Amphibian Proteins / isolation & purification
  • Amphibian Venoms / chemistry*
  • Amphibian Venoms / genetics*
  • Animals
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / genetics
  • Antimicrobial Cationic Peptides / isolation & purification
  • Anura / physiology*
  • Exome Sequencing
  • Female
  • Immunologic Factors / genetics
  • Immunologic Factors / isolation & purification
  • Lectins / genetics
  • Lectins / isolation & purification
  • Male
  • Mass Spectrometry
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / isolation & purification
  • Sequence Analysis, Protein
  • Sequence Analysis, RNA
  • Skin / chemistry*

Substances

  • Amphibian Proteins
  • Amphibian Venoms
  • Antimicrobial Cationic Peptides
  • Immunologic Factors
  • Lectins
  • Protease Inhibitors