The identification and molecular characterization of Trypanosoma cruzi amastigote surface protein-1, a member of the trans-sialidase gene super-family1Note: Nucleotide sequence data reported in this paper is available in the GenBank data base under the Accession no. U74494.1

Santos, M. A. M.; Garg, Nisha; Tarleton, Rick L.

doi:10.1016/s0166-6851(96)02840-x

Cited by 15 publications

(5 citation statements)

References 29 publications

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“…Whether they are receptors for the gp85/TS proteins remains to be investigated. It is known that amastigote forms do express proteins from the gp85/TS family and may, therefore, interact intracellularly with cytokeratins [ 27 , 39 ] and other cytoskeletal proteins. This interaction may be important for parasite proliferation in the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

Trypanosoma cruzi Binds to Cytokeratin through Conserved Peptide Motifs Found in the Laminin-G-Like Domain of the gp85/Trans-sialidase Proteins

et al. 2015

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BackgroundChagas' disease, caused by the protozoan parasite Trypanosoma cruzi, is a disease that affects millions of people most of them living in South and Central Americas. There are few treatment options for individuals with Chagas' disease making it important to understand the molecular details of parasite infection, so novel therapeutic alternatives may be developed for these patients. Here, we investigate the interaction between host cell intermediate filament proteins and the T. cruzi gp85 glycoprotein superfamily with hundreds of members that have long been implicated in parasite cell invasion.Methodology/Principal FindingsAn in silico analysis was utilized to identify peptide motifs shared by the gp85 T. cruzi proteins and, using phage display, these selected peptide motifs were screened for their ability to bind to cells. One peptide, named TS9, showed significant cell binding capacity and was selected for further studies. Affinity chromatography, phage display and invasion assays revealed that peptide TS9 binds to cytokeratins and vimentin, and prevents T. cruzi cell infection. Interestingly, peptide TS9 and a previously identified binding site for intermediate filament proteins are disposed in an antiparallel β-sheet fold, present in a conserved laminin-G-like domain shared by all members of the family. Moreover, peptide TS9 overlaps with an immunodominant T cell epitope.Conclusions/SignificanceTaken together, the present study reinforces previous results from our group implicating the gp85 superfamily of glycoproteins and the intermediate filament proteins cytokeratin and vimentin in the parasite infection process. It also suggests an important role in parasite biology for the conserved laminin-G-like domain, present in all members of this large family of cell surface proteins.

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Section: Discussionmentioning

confidence: 99%

Trypanosoma cruzi Binds to Cytokeratin through Conserved Peptide Motifs Found in the Laminin-G-Like Domain of the gp85/Trans-sialidase Proteins

et al. 2015

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“…These proteins have complete or degenerate Asp box motifs (SxDxGxTW); the VTVxNVxLYNR motif characteristic of all TS members; and a signal sequence for cleavage/addition of GPI anchor at the C-terminal region (Figure 3) [60, 62, 95]. ASP-1, ASP-2, and TSA-1 are targets of T. cruzi -specific CD8 + cytotoxic T lymphocytes and they induce strong antibody responses in infected mice and humans [40, 41, 96, 97]. ASP-1 and ASP-2 are amastigote surface proteins, whereas TSA-1 is a trypomastigote surface antigen [40, 41].…”

Section: Trans-sialidase Superfamilymentioning

confidence: 99%

“…ASP-1, ASP-2, and TSA-1 are targets of T. cruzi -specific CD8 + cytotoxic T lymphocytes and they induce strong antibody responses in infected mice and humans [40, 41, 96, 97]. ASP-1 and ASP-2 are amastigote surface proteins, whereas TSA-1 is a trypomastigote surface antigen [40, 41]. SA85 glycoproteins are expressed by amastigote and bloodstream trypomastigote forms.…”

Section: Trans-sialidase Superfamilymentioning

confidence: 99%

A Brief View of the Surface Membrane Proteins fromTrypanosoma cruzi

Pech-Canul

Monteón

Solís-Oviedo

2017

Journal of Parasitology Research

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Trypanosoma cruzi is the causal agent of Chagas' disease which affects millions of people around the world mostly in Central and South America. T. cruzi expresses a wide variety of proteins on its surface membrane which has an important role in the biology of these parasites. Surface molecules of the parasites are the result of the environment to which the parasites are exposed during their life cycle. Hence, T. cruzi displays several modifications when they move from one host to another. Due to the complexity of this parasite's cell surface, this review presents some membrane proteins organized as large families, as they are the most abundant and/or relevant throughout the T. cruzi membrane.

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“…TSs of group II are expressed in trypomastigotes and intracellular amastigotes and were also described in T. rangeli [ 136 ]. This group comprises members of the so-called GP85 glycoproteins (ASP-1, ASP-2, TSA-1, Tc85, SA85, GP82, and GP90 among others) [ 137 ] which are related to host-cell attachment [ 138 , 139 , 140 , 141 , 142 ], strong antibody responses in mice and humans [ 143 , 144 , 145 ] and T. cruzi internalization and invasion [ 141 , 146 , 147 , 148 ]. They shared with the TSs of group I, apart from the common TS motif VTVxNVxLYNR, the motifs known Asp-box (SxDxGxTW) and the C-terminal GPI anchor.…”

Section: Principal Multi-gene Families Of T Cruzimentioning

confidence: 99%

Trypanosoma Cruzi Genome: Organization, Multi-Gene Families, Transcription, and Biological Implications

Herreros-Cabello

Callejas-Hernández

Gironès

et al. 2020

Genes

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Chagas disease caused by the parasite Trypanosoma cruzi affects millions of people. Although its first genome dates from 2005, its complexity hindered a complete assembly and annotation. However, the new sequencing methods have improved genome annotation of some strains elucidating the broad genetic diversity and complexity of this parasite. Here, we reviewed the genomic structure and regulation, the genetic diversity, and the analysis of the principal multi-gene families of the recent genomes for several strains. The telomeric and sub-telomeric regions are sites with high recombination events, the genome displays two different compartments, the core and the disruptive, and the genome plasticity seems to play a key role in the survival and the infection process. Trypanosoma cruzi (T. cruzi) genome is composed mainly of multi-gene families as the trans-sialidases, mucins, and mucin-associated surface proteins. Trans-sialidases are the most abundant genes in the genome and show an important role in the effectiveness of the infection and the parasite survival. Mucins and MASPs are also important glycosylated proteins of the surface of the parasite that play a major biological role in both insect and mammal-dwelling stages. Altogether, these studies confirm the complexity of T. cruzi genome revealing relevant concepts to better understand Chagas disease.

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The identification and molecular characterization of Trypanosoma cruzi amastigote surface protein-1, a member of the trans-sialidase gene super-family1Note: Nucleotide sequence data reported in this paper is available in the GenBank data base under the Accession no. U74494.1

Cited by 15 publications

References 29 publications

Trypanosoma cruzi Binds to Cytokeratin through Conserved Peptide Motifs Found in the Laminin-G-Like Domain of the gp85/Trans-sialidase Proteins

Trypanosoma cruzi Binds to Cytokeratin through Conserved Peptide Motifs Found in the Laminin-G-Like Domain of the gp85/Trans-sialidase Proteins

A Brief View of the Surface Membrane Proteins fromTrypanosoma cruzi

Trypanosoma Cruzi Genome: Organization, Multi-Gene Families, Transcription, and Biological Implications

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