Degradation of immunoglobulins, protease inhibitors and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii

Korean J Parasitol. 2002 Jun;40(2):93-9. doi: 10.3347/kjp.2002.40.2.93.

Abstract

The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on host's defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (sIgA), IgG, and IgM. It also degraded interleukin-1 alpha (IL-1 alpha) and IL-1 beta. Its activity was not inhibited by endogenous protease inhibitors, such as alpha 2-macroglobulin, alpha 1-trypsin inhibitor, and alpha 2-antiplasmin. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of host's defense-oriented or regulatory proteins by the Acanthamoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acanthamoeba / enzymology*
  • Acanthamoeba / pathogenicity
  • Animals
  • Endopeptidases / physiology*
  • Immunoglobulins / metabolism*
  • Interleukin-1 / metabolism*
  • Protease Inhibitors / metabolism*
  • Virulence

Substances

  • Immunoglobulins
  • Interleukin-1
  • Protease Inhibitors
  • Endopeptidases