Ruminant cluster CD71 uri icon

abstract

  • From a lysate of radiolabeled Theileria parva-infected bovine lymphocytes monoclonal antibody (mAb) IL-A77 immunoprecipitated a molecule of Mr 190 000 under non-reducing conditions, which was shown to be a homodimer of a Mr 90 000 protein after reduction (Naessens et al., 1996). Purification of the bovine transferrin receptor using insoluble bovine transferrin revealed a band of the same Mr which could be bound by mAb IL-A77. Furthermore, the antibody could block binding of labeled bovine transferrin to immature erythroid cells from bone marrow. When cells were metabolically labeled, an additional band was observed when the receptor was precipitated from T. parva-infected lymphocytes, but not from concanavalin A (Con A) stimulated and cultured lymphocytes (Naessens et al., 1996). mAb IL-A165 could inhibit the binding of IL-A77 to T. parva-infected cells, suggesting it also detects transferrin receptor (Davis et al., 1996, this volume)
  • Two monoclonal antibodies (mAbs) belong to this cluster: IL-A77 and IL-A165. They clustered closely in PC16c. The first mAb, an IgM, was raised against bovine activated B cells, the second was an IgG1 raised against bovine bone marrow cells.

publication date

  • 1996
  • 1996
  • 1996