Molecular Characterization of Serine-, Alanine-, and Proline-Rich Proteins of Trypanosoma cruzi and Their Possible Role in Host Cell Infection
| Autor: | José Franco da Silveira, Björn Andersson, Márcia R. M. Santos, Najib M. El Sayed, Nobuko Yoshida, Alice T. Ferreira, Mirian Silva do Carmo, Renata C. P. Baida, Danielle Ferreira |
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| Rok vydání: | 2006 |
| Předmět: |
Signal peptide
genetic structures Proline Trypanosoma cruzi media_common.quotation_subject Molecular Sequence Data Immunology Protozoan Proteins Biology Microbiology law.invention Serine law Animals Humans Amino Acid Sequence Internalization Peptide sequence media_common Alanine chemistry.chemical_classification biology.organism_classification Amino acid Infectious Diseases Biochemistry chemistry Recombinant DNA Calcium Proline-Rich Protein Domains Parasitology Fungal and Parasitic Infections Peptides Cell Adhesion Molecules Genome Protozoan HeLa Cells |
| Zdroj: | Infection and Immunity. 74:1537-1546 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.74.3.1537-1546.2006 |
| Popis: | 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 Ca 2+ 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. |
| Databáze: | OpenAIRE |
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