Molecular characterization of serine-, alanine-, and proline-rich proteins of Trypanosoma cruzi and their possible role in host cell infection

Molecular characterization of serine-, alanine-, and proline-rich proteins of Trypanosoma cruzi and their possible role in host cell infection

Author Baida, Renata Cristina Pardos Autor UNIFESP Google Scholar
Santos, Marcia RM Autor UNIFESP Google Scholar
Carmo, Mirian S. Autor UNIFESP Google Scholar
Yoshida, Nobuko Autor UNIFESP Google Scholar
Ferreira, Danielle Autor UNIFESP Google Scholar
Ferreira, Aline Teixeira Autor UNIFESP Google Scholar
El Sayed, Najib M. Google Scholar
Andersson, Bjorn Google Scholar
Silveira, Jose Franco da Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Inst Genom Res TIGR
Karolinska Inst
Abstract We previously reported the isolation of a novel protein gene family, termed SAP (serine-, alanine-, and proline-rich protein), from Trypanosoma cruzi. Aided by the availability of the completed genome sequence of T. cruzi, we have now identified 39 full-length sequences of SAP, six pseudogenes and four partial genes. SAPs share a central domain of about 55 amino acids and can be divided into four groups based on their amino (N)- and carboxy (C)-terminal sequences. Some SAPs have conserved N- and C-terminal domains encoding a signal peptide and a glycosylphosphatidylinositol anchor addition site, respectively. Analysis of the expression of SAPs in metacyclic trypomastigotes by two-dimensional electrophoresis and immunoblotting revealed that they are likely to be posttranslationally modified in vivo. We have also demonstrated that some SAPs are shed into the extracellular medium. the recombinant SAP exhibited an adhesive capacity toward mammalian cells, where binding was dose dependent and saturable, indicating a possible ligand-receptor interaction. SAP triggered the host cell Ca2+ response required for parasite internalization. A cell invasion assay performed in the presence of SAP showed inhibition of internalization of the metacyclic forms of the CL strain. Taken together, these results show that SAP is involved in the invasion of mammalian cells by metacyclic trypomastigotes, and they confirm the hypothesis that infective trypomastigotes exploit an arsenal of surface glycoproteins and shed proteins to induce signaling events required for their internalization.
Language English
Date 2006-03-01
Published in Infection and Immunity. Washington: Amer Soc Microbiology, v. 74, n. 3, p. 1537-1546, 2006.
ISSN 0019-9567 (Sherpa/Romeo, impact factor)
Publisher Amer Soc Microbiology
Extent 1537-1546
Origin http://dx.doi.org/10.1128/IAI.74.3.1537-1546.2006
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000235817500011
URI http://repositorio.unifesp.br/handle/11600/28757

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