Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor
Nenhuma Miniatura disponível
Data
2001-06-01
Autores
Magdesian, M. H.
Giordano, R.
Ulrich, Alexander Henning [UNIFESP]
Juliano, Maria Aparecida [UNIFESP]
Juliano, Luiz [UNIFESP]
Schumacher, R. I.
Colli, W.
Alves, MJM
Orientadores
Tipo
Artigo
Título da Revista
ISSN da Revista
Título de Volume
Resumo
The infective trypomastigote stage of Trypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/transsialidase 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.
Descrição
Citação
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 276, n. 22, p. 19382-19389, 2001.