Toxicity of, and histological lesions caused by, ribosome-inactivating proteins, their IgG-conjugates, and their homopolymers

APMIS. 1990 Jul;98(7):585-93. doi: 10.1111/j.1699-0463.1990.tb04975.x.

Abstract

The toxicity of, and the lesions brought about by, several ribosome-inactivating proteins (bryodin, gelonin, momordin, pokeweed antiviral protein from seeds, saporin 6, trichokirin and momorcochin-S), either native, or conjugated to bovine IgG, or polymerized, were studied in the mouse. Severe necrotic liver damage was the main lesion present in animals receiving lethal doses of the proteins. The toxicity of ribosome-inactivating proteins increased after conjugation to IgG or homopolymerization. The toxicity of conjugates to mouse was not predictable from the inhibitory activity on cell-free protein synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Glycoproteins / toxicity
  • Immunoglobulin G
  • Immunotoxins / toxicity*
  • Kidney / drug effects
  • Kidney / pathology*
  • Lethal Dose 50
  • Liver / drug effects
  • Liver / pathology*
  • Mice
  • N-Glycosyl Hydrolases*
  • Necrosis
  • Plant Proteins / toxicity*
  • Protein Synthesis Inhibitors / toxicity*
  • Rabbits
  • Reticulocytes / drug effects
  • Reticulocytes / metabolism
  • Ribosome Inactivating Proteins, Type 1
  • Ribosomes / drug effects*
  • Saporins
  • Toxins, Biological*

Substances

  • Glycoproteins
  • Immunoglobulin G
  • Immunotoxins
  • Plant Proteins
  • Protein Synthesis Inhibitors
  • Ribosome Inactivating Proteins, Type 1
  • Toxins, Biological
  • bryodin
  • trichokirin protein, Trichosanthes kirilowii
  • GEL protein, Gelonium multiflorum
  • N-Glycosyl Hydrolases
  • Saporins
  • pokeweed antiviral protein