Sequence diversity and evolution of antimicrobial peptides in invertebrates

Dev Comp Immunol. 2015 Feb;48(2):324-41. doi: 10.1016/j.dci.2014.05.020. Epub 2014 Jun 17.

Abstract

Antimicrobial peptides (AMPs) are evolutionarily ancient molecules that act as the key components in the invertebrate innate immunity against invading pathogens. Several AMPs have been identified and characterized in invertebrates, and found to display considerable diversity in their amino acid sequence, structure and biological activity. AMP genes appear to have rapidly evolved, which might have arisen from the co-evolutionary arms race between host and pathogens, and enabled organisms to survive in different microbial environments. Here, the sequence diversity of invertebrate AMPs (defensins, cecropins, crustins and anti-lipopolysaccharide factors) are presented to provide a better understanding of the evolution pattern of these peptides that play a major role in host defense mechanisms.

Keywords: Antilipopolysaccharide factors; Antimicrobial peptides; Cecropins; Crustins; Defensins; Sequence diversity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / genetics
  • Antimicrobial Cationic Peptides / immunology*
  • Arthropod Proteins / chemistry
  • Arthropod Proteins / genetics
  • Arthropod Proteins / immunology
  • Evolution, Molecular
  • Invertebrates / classification
  • Invertebrates / genetics*
  • Invertebrates / immunology*
  • Molecular Sequence Data
  • Phylogeny
  • Sequence Alignment

Substances

  • Antimicrobial Cationic Peptides
  • Arthropod Proteins