The composition and immunological suppression of a novel proteinaceous
material, a neutral thiol pretense (NTP), isolated from the metacerca
ria of the helminth Paragonimus westermani are reported. From cDNA clo
ning and sequencing, the protease was found to be composed of 215 amin
o acid residues and closely resembled the known cysteine proteases. Tr
eatment of adult mice with the enzyme suppressed the delayed footpad r
eaction and haemagglutinin antibody production, and reduced expression
of the major histocompatibility complex and interleukin 2 receptor on
lymphocytes, and induced suppressor cells in the spleen. In addition,
stable and long-term skin graft survival was achieved by concomitant
administration of the enzyme at a low dose.