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

被引：18
|
作者：
Marroquin-Quelopana, M
Oyama, S
Pertinhez, TA
Spisni, A
Juliano, MA
Juliano, L
Colli, W
Alves, MJM
机构：
[1] Univ Sao Paulo, Inst Quim, BR-05508900 Sao Paulo, Brazil
[2] Lab Nacl Luz Sincrotron, Ctr Biol Mol Estrutural, BR-13084971 Campinas, SP, Brazil
[3] Univ Parma, Dept Expt Med Sec Chem & Struct Biochem, I-43100 Parma, Italy
[4] Univ Fed Sao Paulo, BR-04023900 Sao Paulo, SP, Brazil
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 325卷 / 02期
基金：
巴西圣保罗研究基金会;
关键词：
Trypanosoma cruzi; laminin; adhesion; receptor; protein domains; synthetic peptides; homology modeling;
D O I：
10.1016/j.bbrc.2004.10.068
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：612 / 618
页数：7
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