Protease activity of 80 kDa protein secreted from the apicomplexan parasite Toxoplasma gondii.
This study describes the characterization of 80 kDa protease showing gelationlytic property among three proteases in the excretory/secretory proteins (ESP) from Toxoplasma gondii. The protease activity was detected in the ESP but not in the somatic extract of RH tachyzoites. This protease was active only in the presence of calcium ion but not other divalent cationic ions such as Cu(2+), Zn(2+), Mg(2+), and Mn(2+), implying that Ca(2+) is critical factor for the activation of the protease. The 80 kDa protease was optimally active at pH 7.5. Its gelatinolytic activity was maximal at 37 degrees C, and significant level of enzyme activity of the protease remained after heat treatment at 56 degrees C for 30 min or 100 degrees C for 10 min. This thermostable enzyme was strongly inhibited by metal chelators, i.e., EDTA, EGTA, and 1,10- phenanthroline. Thus, the 80 kDa protease in the ESP secreted by T. gondii was classified as a calcium dependent neutral metalloprotease.
Song
Kyoung-Ju
KJ
Department of Parasitology and Catholic Institute of Parasitic Diseases, College of Medicine, Catholic University of Korea, Seoul 137-701, Korea. skjy1261@hanmail.net
Nam
Ho-Woo
HW
D000818:Animals; D002118:Calcium / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013696:Temperature; D014122:Toxoplasma / Q000201:enzymology*
D010450:Endopeptidases; D002118:Calcium