Key result
Monovalent Fab fragments of the monoclonal antibody 4A4 specific for gp83-TSA inhibited gp83-TSA binding to cells and neutralized T. cruzi infection in BALB/c mice.
The study identifies gp83-TSA as a key ligand for Trypanosoma cruzi cell entry and demonstrates that targeting it with specific antibodies can neutralize infection in vitro and in vivo.
Hypothesis-generating for gp83-TSA blockade in Chagas; human studies required before clinical consideration.
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 4x10(4) per myoblast with a K(d) 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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Villalta et al. (2001) studied Trypanosoma cruzi infection. Monovalent Fab fragments of monoclonal antibody 4A4 specific for gp83-TSA was evaluated on Trypanosome attachment, entry, and infection neutralization. Monovalent Fab fragments of the monoclonal antibody 4A4 specific for gp83-TSA inhibited gp83-TSA binding to cells and neutralized T. cruzi infection in BALB/c mice.
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