The cecropin superfamily of toxic peptides

J Mol Microbiol Biotechnol. 2006;11(1-2):94-103. doi: 10.1159/000092821.

Abstract

All sequenced peptide toxins of the cecropin, pleurocidin and dermaceptin/ceratotoxin families in the National Center for Biotechnology Information (NCBI) database as of May 2005 were identified and shown to comprise a single superfamily. The peptide sequences were multiply aligned, revealing conserved residues that may play roles in structure and function. Signature sequences were derived for each of the 3 constituent families. Phylogenetic analyses revealed the relationships of these peptides to each other, and average hydropathy/amphipathicity studies provided structural information. This study serves to characterize a large superfamily of toxic peptides that perform host defense functions in a range of animal kingdoms.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Amphibian Proteins / chemistry*
  • Amphibian Proteins / classification
  • Animals
  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / classification
  • Databases, Protein
  • Evolution, Molecular
  • Fish Proteins / chemistry*
  • Fish Proteins / classification
  • Insect Proteins / chemistry*
  • Insect Proteins / classification
  • Molecular Sequence Data
  • Phylogeny

Substances

  • Amphibian Proteins
  • Antimicrobial Cationic Peptides
  • Fish Proteins
  • Insect Proteins
  • pleurocidin
  • dermaseptin