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Korean J Parasitol. 2002 Jun;40(2):93-9.

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

Author information

1
Department of Biology, College of Natural Science, Chung-Ang University, Seoul 156-756, Korea.

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.

PMID:
12073735
PMCID:
PMC2721049
[Indexed for MEDLINE]
Free PMC Article

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