Immunosuppression by a neutral thiol protease from parasitic helminth larvae in mice.
The composition and immunological suppression of a novel proteinaceous material, a neutral thiol protease (NTP), isolated from the metacercaria of the helminth Paragonimus westermani are reported. From cDNA cloning and sequencing, the protease was found to be composed of 215 amino acid residues and closely resembled the known cysteine proteases. Treatment of adult mice with the enzyme suppressed the delayed footpad reaction 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.
Hamajima
F
F
Department of Parasitology, National Defense Medical College, Tokorozawa, Japan.
Yamamoto
M
M
Tsuru
S
S
Yamakami
K
K
Fujino
T
T
Hamajima
H
H
Katsura
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000494:pharmacology*; D005260:Female; D006085:Graft Survival / Q000187:drug effects; D007165:Immunosuppression Therapy; D007814:Larva / Q000201:enzymology; D051379:Mice; D008806:Mice, Inbred AKR; D008809:Mice, Inbred C3H; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D010238:Paragonimus / Q000201:enzymology*; D015375:Receptors, Interleukin-2 / Q000096:biosynthesis; D016038:Skin Transplantation; D050378:T-Lymphocytes, Regulatory / Q000276:immunology
D015375:Receptors, Interleukin-2; D003546:Cysteine Endopeptidases