Immunosuppression by a neutral thiol protease from parasitic helminth larvae in mice
作者： F. HAMAJIMA , M. YAMAMOTO , S. TSURU , K. YAMAKAMI , T. FUJINO
DOI: 10.1111/J.1365-3024.1994.TB00348.X
关键词: Cysteine protease 、 Immune system 、 Biology 、 Cysteine 、 Proteases 、 Transplantation 、 Protease 、 Paragonimus westermani 、 Enzyme 、 Immunology
摘要: SUMMARY The composition and immunological suppression of a novel proteinaceous material, neutral thiol protease (NTP), isolated from the metacercaria helminth Paragonimus westermani are reported. From cDNA cloning sequencing, was found to be composed 215 amino acid residues closely resembled known cysteine proteases. Treatment adult mice with enzyme suppressed delayed footpad reaction haemagglutinin antibody production, reduced expression major histocompatibility complex interleukin 2 receptor on lymphocytes, induced suppressor cells in spleen. In addition, stable long-term skin graft survival achieved by concomitant administration at low dose.
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