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J. Biol. Chem., Vol. 276, Issue 22, 19382-19389, June 1, 2001
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From the Departamento de Bioquímica, Instituto de
Química, Universidade de São Paulo, Caixa Postal 26077, São Paulo 05513-970, São Paulo, Brazil and
** Universidade Federal de São Paulo, São Paulo
04023-900, São Paulo, Brazil
The infective trypomastigote stage of
Trypanosoma cruzi expresses a set of surface glycoproteins
that are known collectively as Tc85 and belong to the
gp85/trans-sialidase supergene family. A member of this family,
Tc85-11, with adhesive properties to laminin and cell surfaces was
recently cloned. In this report, the Tc85-11 domain for cell binding
and its corresponding receptor on epithelial cell LLC-MK2
are described. Using synthetic peptides corresponding to the Tc85-11
carboxyl-terminal segment, we show that the mammalian cell-binding
domain colocalizes to the most conserved motif of the trypanosome
gp85/trans-sialidase supergene family (VTVXNVFLYNR). Even
though Tc85-11 binds to laminin, the 19-residue cell-binding peptide
(peptide J) does not contain the laminin-binding site, because it does
not bind to laminin or inhibit cell binding to this glycoprotein. The
host cell receptor for the peptide was characterized as cytokeratin
18. Addition of anti-cytokeratin antibodies to the culture
medium significantly inhibited the infection of epithelial cells by
T. cruzi. Tc85-11 is a multiadhesive glycoprotein, encoding at least two different binding sites, one for laminin and one
for cytokeratin 18, that allow the parasite to overcome the barriers
imposed by cell membranes, extracellular matrices, and basal laminae to
reach the definitive host cell. This is the first description of a
direct interaction between cytokeratin and a protozoan parasite.
Infection by Trypanosoma cruzi
IDENTIFICATION OF A PARASITE LIGAND AND ITS HOST CELL
RECEPTOR*
,
,
*
This work was supported by Grants 95/4562-3 and 99/12459-9
from the Fundação de Amparo à Pesquisa do Estado de
São Paulo (to M. J. M. A. and W. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Submitted as part of a doctoral thesis at the Universidade
de São Paulo, São Paulo, Brazil.
§
A post-doctoral fellow from the Fundação de Amparo
à Pesquisa do Estado de São Paulo.
¶
Present address: M. D. Anderson Cancer Center, Houston,
Texas 77030.
A visiting professor with a Fundação de Amparo
à Pesquisa do Estado de São Paulo-Deutscher Akademischer
Austauschdienst joint fellowship.
To whom correspondence should be addressed: Departamento de
Bioquímica, Instituto de Química, Universidade de
São Paulo, Caixa Postal 26077, São Paulo 05599-970,
São Paulo, Brazil. Tel.: 55-11-3818-3810 ext. 233; Fax:
55-11-3815-5579; E-mail: mjmalves@iq.usp.br.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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