Degradation of immunoglobulins, protease inhibitors, and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii.
10.3347/kjp.2002.40.2.93
- Author:
Byoung Kuk NA
;
Jong Hwa CHO
;
Chul Yong SONG
;
Tong Soo KIM
- Publication Type:Original article ; Research Support, Non-U.S. Gov't
- Keywords:
Acanthamoeba;
protease inhibitors;
immunoglobulins;
interleukin-1
- MeSH:
Acanthamoeba/*enzymology/pathogenicity;
Animals;
Endopeptidases/*physiology;
Immunoglobulins/*metabolism;
Interleukin-1/*metabolism;
Protease Inhibitors/*metabolism;
Support, Non-U.S. Gov't;
Virulence
- From:The Korean Journal of Parasitology
2002;40(2):93-99
- CountryRepublic of Korea
- Language:English
-
Abstract:
The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on hosts 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-1alpha (IL-1alpha) and IL-1beta. Its activity was not inhibited by endogenous protease inhibitors, such as alpha2-macroglobulin, alpha1-trypsin inhibitor, and alpha2-antiplasmin. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of hosts 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.
