Modeling the Trypanosoma cruzi Tc85-11 protein and mapping the laminin-binding site

Miryam Marroquin-Quelopana, Sergio Oyama, Thelma Aguiar Pertinhez, Alberto Spisni, Maria Aparecida Juliano, Luiz Juliano, Walter Colli, Maria Júlia M Alves

Research output: Contribution to journalArticlepeer-review


Trypanosoma cruzi expresses a set of glycoproteins encoded by the gp85/trans-sialidase gene superfamily. In this report a structure model is proposed for a cloned member of the superfamily, the Tc85-11 protein. The structure consists of an N-terminus β-propeller and a C-terminus β-sandwich interconnected by an α-helix. The recombinant protein, corresponding to the N-domain (Tc85-N), binds to laminin in a selective manner. Six synthetic 20-mer peptides from the N-domain adhere onto the surface of LLC-MK 2 cells and two of these peptides specifically inhibit the Tc85-N/laminin interaction, indicating that they are the laminin-binding sites of the molecule. Thus, Tc85-11 and other related members of the family appear to be good candidates to play an important role in T. cruzi infection via a laminin mediated host-parasite interaction.

Original languageEnglish
Pages (from-to)612-618
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Dec 10 2004


  • Adhesion
  • Homology modeling
  • Laminin
  • Protein domains
  • Receptor
  • Synthetic peptides
  • Trypanosoma cruzi

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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