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

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

Author Marroquin-Quelopana, M. Google Scholar
Oyama, S. Google Scholar
Pertinhez, T. A. Google Scholar
Spisni, A. Google Scholar
Juliano, M. A. Google Scholar
Juliano, L. Google Scholar
Colli, W. Google Scholar
Alves, MJM Google Scholar
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
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
Access rights Closed access
Type Article
Web of Science ID WOS:000225279600036

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