| Literature DB >> 15530437 |
Miryam Marroquin-Quelopana1, Sergio Oyama, Thelma Aguiar Pertinhez, Alberto Spisni, Maria Aparecida Juliano, Luiz Juliano, Walter Colli, Maria Júlia M Alves.
Abstract
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 beta-propeller and a C-terminus beta-sandwich interconnected by an alpha-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.Entities:
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Year: 2004 PMID： 15530437 DOI： 10.1016/j.bbrc.2004.10.068
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575