Modulation of interleukin-15-induced human neutrophil responses by the plant lectin Viscum album agglutinin-I

Clin Immunol. 2001 Nov;101(2):229-36. doi: 10.1006/clim.2001.5105.

Abstract

The plant lectin Viscum album agglutinin-I (VAA-I) and the interleukin-15 (IL-15) cytokine are two molecules with potential therapeutic properties known to modulate neutrophil functions when used separately. This study was conducted in order to better understand the mode of action of VAA-I and to elucidate how VAA-I could modulate IL-15-induced neutrophil responses. We found that VAA-I cannot induce phosphorylation events in human neutrophils. However, it enhances phagocytosis by itself without altering IL-15-induced phagocytosis. VAA-I was found to reverse the ability of IL-15 to delay neutrophil apoptosis and this was correlated with an inhibition of IL-15-induced de novo protein synthesis. In addition, we also found that IL-15 cannot reverse or attenuate the caspase-induced gelsolin fragmentation observed during apoptosis as assessed by immunoblotting. We conclude that VAA-I can be used to modulate some, but not all, IL-15-induced neutrophil responses and that it acts independent of phosphorylation events.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adjuvants, Immunologic / pharmacology*
  • Apoptosis / drug effects
  • Dose-Response Relationship, Drug
  • Gelsolin / metabolism
  • Humans
  • Interleukin-15 / pharmacology*
  • Interleukin-2 / pharmacology
  • Neutrophils / drug effects*
  • Neutrophils / physiology
  • Phagocytosis / drug effects
  • Phosphorylation
  • Plant Preparations*
  • Plant Proteins*
  • Protein Biosynthesis
  • Ribosome Inactivating Proteins
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological / pharmacology*

Substances

  • Adjuvants, Immunologic
  • Gelsolin
  • Interleukin-15
  • Interleukin-2
  • Plant Preparations
  • Plant Proteins
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological
  • VAA-I protein, Viscum album
  • ribosome inactivating protein, Viscum
  • Ribosome Inactivating Proteins