LBP/BPI homologue in Eisenia andrei earthworms

Dev Comp Immunol. 2016 Jan;54(1):1-6. doi: 10.1016/j.dci.2015.08.008. Epub 2015 Aug 18.

Abstract

LBP/BPIs are pattern recognition receptors that are often present in vertebrates and in invertebrates, and they play a defense role against pathogens. We have identified 1698 bp cDNA sequence from the Eisenia andrei earthworm with predicted amino acid sequence that shares homology with the LBP/BPI family (EaLBP/BPI). Sequence analysis of EaLBP/BPI proved the existence of two conserved domains with the potential ability to bind LPS. The predicted molecular mass of the EaLBP/BPI protein is 53.5 kDa, and its high basicity (pI 9.8) is caused by its high arginine content. Constitutive transcription of the Ealbp/bpi gene was shown in all tested tissues, with the highest level in coelomocytes and seminal vesicles; the lowest level was detected in the intestine. On the contrary, another earthworm LPS-binding molecule CCF (coelomic cytolytic factor) was expressed only in the intestine and coelomocytes. In E. andrei coelomocytes, the transcription of Ealbp/bpi gene was up-regulated in response to bacterial stimulation, reaching a maximum at 8 and 16 h post stimulation with Bacillus subtilis and Escherichia coli, respectively.

Keywords: CCF; Earthworm; Eisenia; LBP/BPI; LPS; PRR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antimicrobial Cationic Peptides / genetics*
  • Base Sequence
  • Blood Proteins / genetics*
  • Cloning, Molecular
  • In Situ Hybridization
  • Molecular Sequence Data
  • Oligochaeta / genetics*
  • Oligochaeta / immunology*
  • Phylogeny
  • Reverse Transcriptase Polymerase Chain Reaction

Substances

  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • bactericidal permeability increasing protein