Immuno-gold-labelling of CUT-1, CUT-2 and cuticlin epitopes in Caenorhabditis elegans and Heterorhabditis sp. processed by high pressure freezing and freeze-substitution

J Submicrosc Cytol Pathol. 1995 Jul;27(3):341-7.

Abstract

CUT-1 and CUT-2 are two distinct protein components of cuticlin, the insoluble residue of the cuticles of nematodes. In previous experiments of gold-immuno-labelling on sections of chemically fixed Caenorhabditis elegans, CUT-1 and CUT-2 epitopes were specifically lost. Cryo-immobilization of C. elegans under high pressure followed by freeze-substitution, however, resulted in a good preservation of these antigenic sites and of the ultrastructure of the worms. The entomopathogenic nematode Heterorhabditis sp. processed by the same cryopreparation protocol has shown a strong reactivity with anti-sera raised against CUT-1, CUT-2 and against the whole cuticlin residue of C. elegans. The localization of these epitopes was conserved across the two species.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Helminth / metabolism
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans / ultrastructure*
  • Caenorhabditis elegans Proteins*
  • Epitopes / metabolism
  • Frozen Sections
  • Helminth Proteins / immunology
  • Helminth Proteins / metabolism*
  • Immunohistochemistry
  • Microscopy, Immunoelectron
  • Rhabditoidea / metabolism*
  • Rhabditoidea / ultrastructure*
  • Species Specificity

Substances

  • Antigens, Helminth
  • CUT-2 protein, C elegans
  • Caenorhabditis elegans Proteins
  • EPICUT-1 protein, Ascaris suum
  • Epitopes
  • Helminth Proteins
  • CUT-1 protein, C elegans