Degradation of immunoglobulins, protease inhibitors and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii.
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.
Na
Byoung-Kuk
BK
Department of Biology, College of Natural Science, Chung-Ang University, Seoul 156-756, Korea.
Cho
Jung-Hwa
JH
Song
Chul-Yong
CY
Kim
Tong-Soo
TS
D000048:Acanthamoeba / Q000201:enzymology* / Q000472:pathogenicity; D000818:Animals; D010450:Endopeptidases / Q000502:physiology*; D007136:Immunoglobulins / Q000378:metabolism*; D007375:Interleukin-1 / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*; D014774:Virulence
D007136:Immunoglobulins; D007375:Interleukin-1; D011480:Protease Inhibitors; D010450:Endopeptidases