Abstract
We purified a soluble gp83 trans-sialidase (gp83-TSA), from phospholipase C-treated Trypanosoma cruzi trypomastigote membranes, which binds to myoblasts, fibroblasts and macrophages to mediate trypanosome entry. Myoblasts display a single class of receptors for the gp83-TSA present at 4×104 per myoblast with a Kd of 8 nM. Monovalent Fab fragments of the monoclonal antibody 4A4 specific for gp83-TSA inhibit gp83-TSA binding to myoblasts, fibroblasts and macrophages, block the trypanosomes from attaching to and entering these cells and neutralize T. cruzi infection in BALB/c mice. This is the first demonstration that gp83-TSA is a ligand that T. cruzi uses to attach to cells.
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