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PAS‐1, a protein affinity purified from Ascaris suum worms, maintains the ability to modulate the immune response to a bystander antigen
Author(s) -
Oshiro Telma M,
Enobe Cristina S,
Araújo Cláudia A,
Macedo Mahasti S,
MacedoSoares Maria Fernanda
Publication year - 2006
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1111/j.1440-1711.2005.01404.x
Subject(s) - ascaris suum , antigen , ovalbumin , immune system , immunoglobulin e , biology , bystander effect , antibody , immunology , helminths
Helminth infections and parasite components have potent immunomodulatory effects on a host's immune system. In the present study, we investigated the effect of PAS‐1, a protein component of Ascaris suum adult worms recognized by a monoclonal antibody (MAIP‐1), on humoral and cell‐mediated responses to a bystander antigen (ovalbumin [OVA]). MAIP‐1 recognized only one of the three polypeptide chains of PAS‐1, but neutralized the suppressive effect of the whole worm extract on OVA‐specific antibody production. PAS‐1 inhibited antibody production against a T‐cell‐dependent, but not a T‐cell‐independent, antigen in a dose‐dependent way. IgM, IgG 1 , IgG 2b , and also IgE and anaphylactic IgG 1 levels were downregulated. In addition, PAS‐1 inhibited OVA‐specific delayed type hypersensitivity reactions in the footpad of mice, showing a potent immunosuppressive activity on both Th1 and Th2 responses that seems to be mediated by the induction of large amounts of IL‐10 and IL‐4. Indeed, PAS‐1‐specific spleen cells secreted sevenfold more IL‐10 and threefold more IL‐4 than OVA‐specific cells in response to in vitro restimulation with the respective antigens. In conclusion, we showed that PAS‐1, a single protein component from A. suum , maintains all its immunosuppressive properties.