Lysenin family proteins in earthworm coelomocytes - Comparative approach

Dev Comp Immunol. 2017 Feb:67:404-412. doi: 10.1016/j.dci.2016.08.011. Epub 2016 Aug 24.

Abstract

Sphingomyelin-binding proteins of the lysenin family were originally identified in earthworms belonging to the genus Eisenia comprised of at least two distinct species, E. andrei and E. fetida, until recently considered subspecies or morphotypes of E. foetida (sic). In the present study the presence of lysenin and lysenin-related protein 2 (LRP-2, known also as fetidin) was detected in coelomocytes retrieved from all investigated adult specimens of E. andrei, and E. fetida. They were accompanied by LRP-3 and LRP-1 in some specimens of E. andrei and E. fetida, respectively. Lysenins were not observed in a third composting lumbricid species, Dendrobaena veneta, which served as a convenient negative reference for techniques and procedures used in the study. The pore-forming potential of soluble and cellular fractions of coelomic fluid was studied towards sheep red blood cells and sphingomyelin-rich liposomes. After experimental depletion the potential was restored in parallel with restoration of chloragocyte-derived eleocytes in both E. andrei and E. fetida.

Keywords: COI barcoding; Dendrobaena veneta/Eisenia hortensis; Eisenia andrei; Eisenia fetida; Lysenin-related proteins; Mass spectrometry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Hemolysis*
  • Mass Spectrometry
  • Oligochaeta / immunology*
  • Phagocytes / immunology*
  • Pore Forming Cytotoxic Proteins / metabolism
  • Protein Binding
  • Proteins / genetics
  • Proteins / metabolism*
  • Species Specificity
  • Sphingomyelins / metabolism
  • Toxins, Biological / genetics
  • Toxins, Biological / metabolism*

Substances

  • Pore Forming Cytotoxic Proteins
  • Proteins
  • Sphingomyelins
  • Toxins, Biological
  • fetidin
  • lysenin