Author |
Marroquin-Quelopana, M.
![]() Oyama, S. ![]() Pertinhez, T. A. ![]() Spisni, A. ![]() Juliano, M. A. ![]() Juliano, L. ![]() Colli, W. ![]() Alves, MJM ![]() |
Institution | Universidade de São Paulo (USP) Lab Nacl Luz Sincrotron Univ Parma Universidade Federal de São Paulo (UNIFESP) |
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-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. (C) 2004 Elsevier Inc. All rights reserved. |
Keywords |
Trypanosoma cruzi
laminin adhesion receptor protein domains synthetic peptides homology modeling |
Language | English |
Date | 2004-12-10 |
Published in | Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 325, n. 2, p. 612-618, 2004. |
ISSN | 0006-291X (Sherpa/Romeo, impact factor) |
Publisher | Elsevier B.V. |
Extent | 612-618 |
Origin |
|
Access rights | Closed access |
Type | Article |
Web of Science ID | WOS:000225279600036 |
URI | http://repositorio.unifesp.br/handle/11600/28049 |
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