| Full text | |
| Author(s): |
Marroquin-Quelopana, Miryam
;
Oyama Júnior, Sergio
;
Pertinhez, Thelma Aguiar
;
Spisni, Alberto
;
Juliano, Maria Aparecida
;
Juliano, Luiz
;
Colli, Walter
;
Alves, Maria Júlia M.
[8]
Total Authors: 8
|
| Document type: | Journal article |
| Source: | Biochemical and Biophysical Research Communications; v. 325, n. 2, p. 612-618, Dec. 2004. |
| Field of knowledge: | Biological Sciences - Biochemistry |
| 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 â-propeller and a C-terminus â-sandwich interconnected by an á-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-MK2 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. (AU) | |
| FAPESP's process: | 99/12459-9 - Trypanosoma cruzi: parasite-host cell interaction |
| Grantee: | Maria Julia Manso Alves |
| Support Opportunities: | Research Projects - Thematic Grants |