Activities of different cysteine proteases of Paragonimus westermani in cleaving human IgG

Cleaving host immunoglobulins is a well known mechanism of evading host immune reactions exploited by helminth parasites. Secreted cysteine proteases of helminth are a part of enzymes cleaving host IgG. Paragonimus westermani produces at least six different species of the cysteine protease in its developmental stages. This study was undertaken to evaluate comparatively the activities against human IgG by the different enzymes. When the metacercariae, which secrete 27 and 28 kDa cysteine proteases, were incubated in human IgG solution, IgG was degraded at its hinge region. Further incubation resulted complete hydrolysis. From 4-week and 7-week old juveniles and 16-week old adults of P. westermani, five different enzymes at 15, 17, 27, 28 and 53 kDa have been purified, if the enzyme with the same molecular mass is regarded to be identical. In cleaving human IgG, each cysteine protease exhibited decreasing activities with age.