Trypanosoma cruzi interaction with the extra-cellular matrix: modeling the TC85-11 protein and mapping the laminin-binding site / Trypanosoma cruzi e a interação com a matriz extracelular: modelagem da proteína Tc85-11 e determinação do sítio de ligação a laminina

AUTOR(ES)
DATA DE PUBLICAÇÃO

2003

RESUMO

Trypanosoma cruzi expresses the Tc85 proteins, a set of surface glycoproteins belonging to the gp85/trans-sialidase supergene family. In this report we show a structure model for Tc85-11 a member of this family, which has adhesive properties to laminin and to the host cell surfaces. That structure consists in an N-terminus β-propeller and a C-terminus β-sandwich domains connected by a long α-helix. The recombinant protein corresponding to the N-domain (Tc85-N), but not to the C-domain (Tc85-C), was able to bind laminin in a specific manner. Five synthetic 20-mer peptides from the N-domain adhere onto LLC-MK2 cell surface and inhibit the T. cruzi infection. Two of these peptides can also inhibit specifically Tc85-N - laminin interaction and may represent the laminin-binding site. These results reinforce the hypothesis that the Tc85-11 protein is a multi-adhesive protein, since it also binds to citokeratin-18 by C-terminus domain. On the other hand, the treatment of host cells with Tc85-N increases the expression of laminin in the cell culture, as was previously reported for treatment with T. cruzi released antigens. In summary, Tc85-11 protein may play an important role in the host-parasite interaction, including the modulation of ECM expression.

ASSUNTO(S)

trypanosoma cruzi laminin tc85-11 moleculas de adesão adhesionmolecules trypanosoma cruzi laminina tc85-11

ACESSO AO ARTIGO

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