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  • Schistosomiasis is a major human parasitic disease with a global impact. Schistosoma japonicum, the most difficult to control, can survive within host veins for decades. Mechanisms of immune evasion by the parasite, including antigenic variation and surface masking, have been implicated but not well defined. In this study, we defined the immunoglobulin-binding proteomes of S. japonicum using human IgG, IgM, and IgE as the molecular bait for affinity purification, followed by protein identification by liquid chromatography with tandem mass spectrometry (LC-MS/MS). Several proteins situated at the tegument of S. japonicum were able to nonselectively bind to the Fc domain of host immunoglobulins, indicating a mechanism for the avoidance of host immune attachment and recognition. The profile of the immunoglobulin-binding proteomes provides further clues for immune evasion mechanisms adopted by S. japonicum.
Subject
  • Immunology
  • Immune system
  • Antibodies
  • Chromatography
  • Glycoproteins
  • IARC Group 2B carcinogens
  • Infectious causes of cancer
  • Helminthiases
  • Parasitic helminths of humans
  • Animals described in 1904
  • Diplostomida
  • Parasitic animals of mammals
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