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  1. Article ; Online: Trypanosoma cruzi: single cell live imaging inside infected tissues.

    Ferreira, Bianca Lima / Orikaza, Cristina Mary / Cordero, Esteban Mauricio / Mortara, Renato Arruda

    Cellular microbiology

    2016  Volume 18, Issue 6, Page(s) 779–783

    Abstract: Although imaging the live Trypanosoma cruzi parasite is a routine technique in most laboratories, identification of the parasite in infected tissues and organs has been hindered by their intrinsic opaque nature. We describe a simple method for in vivo ... ...

    Abstract Although imaging the live Trypanosoma cruzi parasite is a routine technique in most laboratories, identification of the parasite in infected tissues and organs has been hindered by their intrinsic opaque nature. We describe a simple method for in vivo observation of live single-cell Trypanosoma cruzi parasites inside mammalian host tissues. BALB/c or C57BL/6 mice infected with DsRed-CL or GFP-G trypomastigotes had their organs removed and sectioned with surgical blades. Ex vivo organ sections were observed under confocal microscopy. For the first time, this procedure enabled imaging of individual amastigotes, intermediate forms and motile trypomastigotes within infected tissues of mammalian hosts.
    MeSH term(s) Animals ; Chagas Disease/parasitology ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Microscopy, Confocal ; Single-Cell Analysis/methods ; Trypanosoma cruzi/cytology ; Trypanosoma cruzi/pathogenicity
    Chemical Substances Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2016-01-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 1468320-9
    ISSN 1462-5822 ; 1462-5814
    ISSN (online) 1462-5822
    ISSN 1462-5814
    DOI 10.1111/cmi.12553
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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: miR-138-5p induces aggressive traits by targeting Trp53 expression in murine melanoma cells, and correlates with poor prognosis of melanoma patients.

    da Cruz, Adriana Taveira / Hunger, Aline / de Melo, Fabiana Henriques Machado / Monteiro, Ana Carolina / Paré, Geneviève Catherine / Lai, Dulce / Alves-Fernandes, Débora Kristina / Ayub, Ana Luisa Pedroso / Cordero, Esteban Mauricio / Filho, José Franco da Silveira / Schneider-Stock, Regine / Strauss, Bryan Eric / Tron, Victor / Jasiulionis, Miriam Galvonas

    Neoplasia (New York, N.Y.)

    2021  Volume 23, Issue 8, Page(s) 823–834

    Abstract: Deregulation of miRNAs contributes to the development of distinct cancer types, including melanoma, an aggressive form of skin cancer characterized by high metastatic potential and poor prognosis. The expression of a set of 580 miRNAs was investigated in ...

    Abstract Deregulation of miRNAs contributes to the development of distinct cancer types, including melanoma, an aggressive form of skin cancer characterized by high metastatic potential and poor prognosis. The expression of a set of 580 miRNAs was investigated in a model of murine melanoma progression, comprising non-metastatic (4C11-) and metastatic melanoma (4C11+) cells. A significant increase in miR-138-5p expression was found in the metastatic 4C11+ melanoma cells compared to 4C11-, which prompted us to investigate its role in melanoma aggressiveness. Functional assays, including anoikis resistance, colony formation, collective migration, serum-deprived growth capacity, as well as in vivo tumor growth and experimental metastasis were performed in 4C11- cells stably overexpressing miR-138-5p. miR-138-5p induced an aggressive phenotype in mouse melanoma cell lines leading to increased proliferation, migration and cell viability under stress conditions. Moreover, by overexpressing miR-138-5p, low-growing and non-metastatic 4C11- cells became highly proliferative and metastatic in vivo, similar to the metastatic 4C11+ cells. Luciferase reporter analysis identified the tumor suppressor Trp53 as a direct target of miR-138-5p. Using data sets from independent melanoma cohorts, miR-138-5p and P53 expression were also found deregulated in human melanoma samples, with their levels negatively and positively correlated with prognosis, respectively. Our data shows that the overexpression of miR-138-5p contributes to melanoma metastasis through the direct suppression of Trp53.
    MeSH term(s) 3' Untranslated Regions ; Animals ; Cell Line, Tumor ; Gene Expression Regulation, Neoplastic ; Humans ; Melanoma/genetics ; Melanoma/mortality ; Melanoma/pathology ; Mice ; MicroRNAs/genetics ; Neoplasm Metastasis ; Neoplasm Staging ; Prognosis ; RNA Interference ; Survival Analysis ; Tumor Suppressor Protein p53/genetics
    Chemical Substances 3' Untranslated Regions ; MIRN138 microRNA, human ; MIRN138 microRNA, mouse ; MicroRNAs ; Trp53 protein, mouse ; Tumor Suppressor Protein p53
    Language English
    Publishing date 2021-07-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483840-0
    ISSN 1476-5586 ; 1522-8002
    ISSN (online) 1476-5586
    ISSN 1522-8002
    DOI 10.1016/j.neo.2021.05.015
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  3. Article: Regulatory elements in the 3′ untranslated region of the GP82 glycoprotein are responsible for its stage-specific expression in Trypanosoma cruzi metacyclic trypomastigotes

    Bayer-Santos, Ethel / Gentil, Luciana Girotto / Cordero, Esteban Maurício / Corrêa, Paulo Roberto Ceridório / da Silveira, José Franco

    Acta tropica. 2012 Sept., v. 123, no. 3

    2012  

    Abstract: Gene expression in Trypanosoma cruzi is regulated at the post-transcriptional level and cis-acting elements present in the 3′ untranslated region (3′UTR) play an important role by interacting with regulatory proteins. Previous studies demonstrated that ... ...

    Abstract Gene expression in Trypanosoma cruzi is regulated at the post-transcriptional level and cis-acting elements present in the 3′ untranslated region (3′UTR) play an important role by interacting with regulatory proteins. Previous studies demonstrated that the GP82 surface glycoprotein, which is involved in host cell invasion, is up-regulated in the infective metacyclic trypomastigote form, and that GP82 mRNA half-life is longer in this form compared to the non-infective epimastigote form. Here, we demonstrate that the 3′UTR of the GP82 transcript is involved in this developmental regulation, promoting higher expression of the green fluorescent protein (GFP) reporter in metacyclic trypomastigotes than in epimastigotes. A series of stepwise deletions in the 3′UTR was created and results suggest that the mechanism regulating GP82 expression involves multiple elements in the 3′UTR.
    Keywords Trypanosoma cruzi ; cell invasion ; epimastigotes ; gene expression ; gene expression regulation ; glycoproteins ; green fluorescent protein ; half life ; messenger RNA ; regulatory proteins ; trypomastigotes
    Language English
    Dates of publication 2012-09
    Size p. 230-233.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 210415-5
    ISSN 1873-6254 ; 0001-706X
    ISSN (online) 1873-6254
    ISSN 0001-706X
    DOI 10.1016/j.actatropica.2012.03.014
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  4. Article ; Online: Genetic structure and expression of the surface glycoprotein GP82, the main adhesin of Trypanosoma cruzi metacyclic trypomastigotes.

    Correa, Paulo Roberto Ceridorio / Cordero, Esteban Mauricio / Gentil, Luciana Girotto / Bayer-Santos, Ethel / da Silveira, José Franco

    TheScientificWorldJournal

    2013  Volume 2013, Page(s) 156734

    Abstract: T. cruzi improves the likelihood of invading or adapting to the host through its capacity to present a large repertoire of surface molecules. The metacyclic stage-specific surface glycoprotein GP82 has been implicated in host cell invasion. GP82 is ... ...

    Abstract T. cruzi improves the likelihood of invading or adapting to the host through its capacity to present a large repertoire of surface molecules. The metacyclic stage-specific surface glycoprotein GP82 has been implicated in host cell invasion. GP82 is encoded by multiple genes from the trans-sialidase superfamily. GP82 shows a modular organization, with some variation of N-terminal region flanking a conserved central core where the binding sites to the mammalian cell and gastric mucin are located. The function of GP82 as adhesin in host cell invasion process could expose the protein to an intense conservative and selective pressure. GP82 is a GPI-anchored surface protein, synthesized as a 70 kDa precursor devoid of N-linked sugars. GPI-minus variants accumulate in the ER indicating that GPI anchor acts as a forward transport signal for progressing along the secretory pathway as suggested for T. cruzi mucins. It has been demonstrated that the expression of GP82 is constitutive and may be regulated at post-transcriptional level, for instance, at translational level and/or mRNA stabilization. GP82 mRNAs are mobilized to polysomes and consequently translated, but only in metacyclic trypomastigotes. Analysis of transgenic parasites indicates that the mechanism regulating GP82 expression involves multiple elements in the 3'UTR.
    MeSH term(s) 3' Untranslated Regions ; Amino Acid Sequence ; Binding Sites ; Cell Adhesion ; Chagas Disease/parasitology ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Multigene Family ; Polyribosomes/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; RNA Processing, Post-Transcriptional ; RNA Stability ; Trypanosoma cruzi/genetics ; Trypanosoma cruzi/pathogenicity ; Trypanosoma cruzi/physiology ; Variant Surface Glycoproteins, Trypanosoma/genetics ; Variant Surface Glycoproteins, Trypanosoma/metabolism
    Chemical Substances 3' Untranslated Regions ; Protozoan Proteins ; Variant Surface Glycoproteins, Trypanosoma ; glycoprotein GP82, Trypanosoma cruzi
    Language English
    Publishing date 2013-02-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2075968-X
    ISSN 1537-744X ; 1537-744X
    ISSN (online) 1537-744X
    ISSN 1537-744X
    DOI 10.1155/2013/156734
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  5. Article ; Online: Regulatory elements in the 3' untranslated region of the GP82 glycoprotein are responsible for its stage-specific expression in Trypanosoma cruzi metacyclic trypomastigotes.

    Bayer-Santos, Ethel / Gentil, Luciana Girotto / Cordero, Esteban Maurício / Corrêa, Paulo Roberto Ceridório / da Silveira, José Franco

    Acta tropica

    2012  Volume 123, Issue 3, Page(s) 230–233

    Abstract: Gene expression in Trypanosoma cruzi is regulated at the post-transcriptional level and cis-acting elements present in the 3' untranslated region (3'UTR) play an important role by interacting with regulatory proteins. Previous studies demonstrated that ... ...

    Abstract Gene expression in Trypanosoma cruzi is regulated at the post-transcriptional level and cis-acting elements present in the 3' untranslated region (3'UTR) play an important role by interacting with regulatory proteins. Previous studies demonstrated that the GP82 surface glycoprotein, which is involved in host cell invasion, is up-regulated in the infective metacyclic trypomastigote form, and that GP82 mRNA half-life is longer in this form compared to the non-infective epimastigote form. Here, we demonstrate that the 3'UTR of the GP82 transcript is involved in this developmental regulation, promoting higher expression of the green fluorescent protein (GFP) reporter in metacyclic trypomastigotes than in epimastigotes. A series of stepwise deletions in the 3'UTR was created and results suggest that the mechanism regulating GP82 expression involves multiple elements in the 3'UTR.
    MeSH term(s) 3' Untranslated Regions ; DNA Mutational Analysis ; Gene Expression Regulation ; Genes, Reporter ; Green Fluorescent Proteins/analysis ; Green Fluorescent Proteins/genetics ; Protein Biosynthesis ; Protozoan Proteins/biosynthesis ; Protozoan Proteins/genetics ; Sequence Deletion ; Trypanosoma cruzi/genetics ; Trypanosoma cruzi/growth & development ; Variant Surface Glycoproteins, Trypanosoma/biosynthesis ; Variant Surface Glycoproteins, Trypanosoma/genetics
    Chemical Substances 3' Untranslated Regions ; Protozoan Proteins ; Variant Surface Glycoproteins, Trypanosoma ; glycoprotein GP82, Trypanosoma cruzi ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2012-09
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 210415-5
    ISSN 1873-6254 ; 0001-706X
    ISSN (online) 1873-6254
    ISSN 0001-706X
    DOI 10.1016/j.actatropica.2012.03.014
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    In stock of ZB MED Cologne/Königswinter

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  6. Article ; Online: Molecular Characterization of a Novel Family of Trypanosoma cruzi Surface Membrane Proteins (TcSMP) Involved in Mammalian Host Cell Invasion.

    Martins, Nadini Oliveira / Souza, Renata Torres de / Cordero, Esteban Mauricio / Maldonado, Danielle Cortez / Cortez, Cristian / Marini, Marjorie Mendes / Ferreira, Eden Ramalho / Bayer-Santos, Ethel / Almeida, Igor Correia de / Yoshida, Nobuko / Silveira, José Franco da

    PLoS neglected tropical diseases

    2015  Volume 9, Issue 11, Page(s) e0004216

    Abstract: Background: The surface coat of Trypanosoma cruzi is predominantly composed of glycosylphosphatidylinositol-anchored proteins, which have been extensively characterized. However, very little is known about less abundant surface proteins and their role ... ...

    Abstract Background: The surface coat of Trypanosoma cruzi is predominantly composed of glycosylphosphatidylinositol-anchored proteins, which have been extensively characterized. However, very little is known about less abundant surface proteins and their role in host-parasite interactions.
    Methodology/ principal findings: Here, we described a novel family of T. cruzi surface membrane proteins (TcSMP), which are conserved among different T. cruzi lineages and have orthologs in other Trypanosoma species. TcSMP genes are densely clustered within the genome, suggesting that they could have originated by tandem gene duplication. Several lines of evidence indicate that TcSMP is a membrane-spanning protein located at the cellular surface and is released into the extracellular milieu. TcSMP exhibited the key elements typical of surface proteins (N-terminal signal peptide or signal anchor) and a C-terminal hydrophobic sequence predicted to be a trans-membrane domain. Immunofluorescence of live parasites showed that anti-TcSMP antibodies clearly labeled the surface of all T. cruzi developmental forms. TcSMP peptides previously found in a membrane-enriched fraction were identified by proteomic analysis in membrane vesicles as well as in soluble forms in the T. cruzi secretome. TcSMP proteins were also located intracellularly likely associated with membrane-bound structures. We demonstrated that TcSMP proteins were capable of inhibiting metacyclic trypomastigote entry into host cells. TcSMP bound to mammalian cells and triggered Ca2+ signaling and lysosome exocytosis, events that are required for parasitophorous vacuole biogenesis. The effects of TcSMP were of lower magnitude compared to gp82, the major adhesion protein of metacyclic trypomastigotes, suggesting that TcSMP may play an auxiliary role in host cell invasion.
    Conclusion/significance: We hypothesized that the productive interaction of T. cruzi with host cells that effectively results in internalization may depend on diverse adhesion molecules. In the metacyclic forms, the signaling induced by TcSMP may be additive to that triggered by the major surface molecule gp82, further increasing the host cell responses required for infection.
    MeSH term(s) Animals ; Calcium Signaling ; Cell Adhesion ; Cell Line ; Conserved Sequence ; Endocytosis ; Humans ; Membrane Proteins/analysis ; Membrane Proteins/genetics ; Microscopy, Fluorescence ; Multigene Family ; Protein Binding ; Protein Structure, Tertiary ; Trypanosoma cruzi/chemistry ; Trypanosoma cruzi/genetics ; Trypanosoma cruzi/physiology
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2015-11-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2429704-5
    ISSN 1935-2735 ; 1935-2727
    ISSN (online) 1935-2735
    ISSN 1935-2727
    DOI 10.1371/journal.pntd.0004216
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  7. Article ; Online: Unique behavior of Trypanosoma cruzi mevalonate kinase: A conserved glycosomal enzyme involved in host cell invasion and signaling.

    Ferreira, Éden Ramalho / Horjales, Eduardo / Bonfim-Melo, Alexis / Cortez, Cristian / da Silva, Claudio Vieira / De Groote, Michel / Sobreira, Tiago José Paschoal / Cruz, Mário Costa / Lima, Fabio Mitsuo / Cordero, Esteban Mauricio / Yoshida, Nobuko / da Silveira, José Franco / Mortara, Renato Arruda / Bahia, Diana

    Scientific reports

    2016  Volume 6, Page(s) 24610

    Abstract: Mevalonate kinase (MVK) is an essential enzyme acting in early steps of sterol isoprenoids biosynthesis, such as cholesterol in humans or ergosterol in trypanosomatids. MVK is conserved from bacteria to mammals, and localizes to glycosomes in ... ...

    Abstract Mevalonate kinase (MVK) is an essential enzyme acting in early steps of sterol isoprenoids biosynthesis, such as cholesterol in humans or ergosterol in trypanosomatids. MVK is conserved from bacteria to mammals, and localizes to glycosomes in trypanosomatids. During the course of T. cruzi MVK characterization, we found that, in addition to glycosomes, this enzyme may be secreted and modulate cell invasion. To evaluate the role of TcMVK in parasite-host cell interactions, TcMVK recombinant protein was produced and anti-TcMVK antibodies were raised in mice. TcMVK protein was detected in the supernatant of cultures of metacyclic trypomastigotes (MTs) and extracellular amastigotes (EAs) by Western blot analysis, confirming its secretion into extracellular medium. Recombinant TcMVK bound in a non-saturable dose-dependent manner to HeLa cells and positively modulated internalization of T. cruzi EAs but inhibited invasion by MTs. In HeLa cells, TcMVK induced phosphorylation of MAPK pathway components and proteins related to actin cytoskeleton modifications. We hypothesized that TcMVK is a bifunctional enzyme that in addition to playing a classical role in isoprenoid synthesis in glycosomes, it is secreted and may modulate host cell signaling required for T. cruzi invasion.
    Language English
    Publishing date 2016--26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep24610
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  8. Article ; Online: Trypanosoma cruzi: Genome characterization of phosphatidylinositol kinase gene family (PIK and PIK-related) and identification of a novel PIK gene.

    Oliveira, Priscila / Lima, Fabio Mitsuo / Cruz, Mario Costa / Ferreira, Renata Carmona / Sanchez-Flores, Alejandro / Cordero, Esteban Maurício / Cortez, Danielle Rodrigues / Ferreira, Éden Ramalho / Briones, Marcelo Ribeiro da Silva / Mortara, Renato Arruda / da Silveira, José Franco / Bahia, Diana

    Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases

    2014  Volume 25, Page(s) 157–165

    Abstract: Chagas disease is caused by the protozoan Trypanosoma cruzi which affects 10 million people worldwide. Very few kinases have been characterized in this parasite, including the phosphatidylinositol kinases (PIKs) that are at the heart of one of the major ... ...

    Abstract Chagas disease is caused by the protozoan Trypanosoma cruzi which affects 10 million people worldwide. Very few kinases have been characterized in this parasite, including the phosphatidylinositol kinases (PIKs) that are at the heart of one of the major pathways of intracellular signal transduction. Recently, we have classified the PIK family in T. cruzi using five different models based on the presence of PIK conserved domains. In this study, we have mapped PIK genes to the chromosomes of two different T. cruzi lineages (G and CL Brener) and determined the cellular localization of two PIK members. The kinases have crucial roles in metabolism and are assumed to be conserved throughout evolution. For this reason, they should display a conserved localization within the same eukaryotic species. In spite of this, there is an extensive polymorphism regarding PIK localization at both genomic and cellular levels, among different T. cruzi isolates and between T. cruzi and Trypanosomabrucei, respectively. We showed in this study that the cellular localization of two PIK-related proteins (TOR1 and 2) in the T. cruzi lineage is distinct from that previously observed in T. brucei. In addition, we identified a new PIK gene with peculiar feature, that is, it codes for a FYVE domain at N-terminal position. FYVE-PIK genes are phylogenetically distant from the groups containing exclusively the FYVE or PIK domain. The FYVE-PIK architecture is only present in trypanosomatids and in virus such as Acanthamoeba mimivirus, suggesting a horizontal acquisition. Our Bayesian phylogenetic inference supports this hypothesis. The exact functions of this FYVE-PIK gene are unknown, but the presence of FYVE domain suggests a role in membranous compartments, such as endosome. Taken together, the data presented here strengthen the possibility that trypanosomatids are characterized by extensive genomic plasticity that may be considered in designing drugs and vaccines for prevention of Chagas disease.
    MeSH term(s) Bayes Theorem ; Chagas Disease/epidemiology ; Evolution, Molecular ; Gene Transfer, Horizontal ; Genome, Protozoan ; Humans ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Phylogeny ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Trypanosoma cruzi/classification ; Trypanosoma cruzi/enzymology ; Trypanosoma cruzi/genetics
    Chemical Substances Protozoan Proteins ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
    Language English
    Publishing date 2014-07
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2037068-4
    ISSN 1567-7257 ; 1567-1348
    ISSN (online) 1567-7257
    ISSN 1567-1348
    DOI 10.1016/j.meegid.2014.03.022
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  9. Article ; Online: Proteomic analysis of Trypanosoma cruzi secretome: characterization of two populations of extracellular vesicles and soluble proteins.

    Bayer-Santos, Ethel / Aguilar-Bonavides, Clemente / Rodrigues, Silas Pessini / Cordero, Esteban Maurício / Marques, Alexandre Ferreira / Varela-Ramirez, Armando / Choi, Hyungwon / Yoshida, Nobuko / da Silveira, José Franco / Almeida, Igor C

    Journal of proteome research

    2013  Volume 12, Issue 2, Page(s) 883–897

    Abstract: Microorganisms use specialized systems to export virulence factors into host cells. Secretion of effector proteins into the extracellular environment has been described in Trypanosoma cruzi; however, a comprehensive proteomic analysis of the secretome ... ...

    Abstract Microorganisms use specialized systems to export virulence factors into host cells. Secretion of effector proteins into the extracellular environment has been described in Trypanosoma cruzi; however, a comprehensive proteomic analysis of the secretome and the secretion mechanisms involved remain elusive. Here, we present evidence that T. cruzi releases proteins associated with vesicles that are formed by at least two different mechanisms. Transmission electron microscopy showed larger vesicles budding from the plasma membrane of noninfective epimastigotes and infective metacyclic trypomastigotes, as well as smaller vesicles within the flagellar pocket of both forms. Parasite conditioned culture supernatant was fractionated and characterized by morphological, immunochemical, and proteomic analyses. Three fractions were obtained by differential ultracentrifugation: the first enriched in larger vesicles resembling ectosomes, the second enriched in smaller vesicles resembling exosomes, and a third fraction enriched in soluble proteins not associated with extracellular vesicles. Label-free quantitative proteomic analysis revealed a rich collection of proteins involved in metabolism, signaling, nucleic acid binding, and parasite survival and virulence. These findings support the notion that T. cruzi uses different secretion pathways to excrete/secrete proteins. Moreover, our results suggest that metacyclic forms may use extracellular vesicles to deliver cargo into host cells.
    MeSH term(s) Animals ; Biological Transport ; Cell Membrane/metabolism ; Cells, Cultured ; Chromatography, Liquid ; Culture Media, Conditioned/chemistry ; Flagella/metabolism ; Life Cycle Stages/physiology ; Mice ; Microscopy, Electron, Transmission ; Proteomics ; Protozoan Proteins/isolation & purification ; Protozoan Proteins/metabolism ; Secretory Vesicles ; Tandem Mass Spectrometry ; Trypanosoma cruzi/physiology ; Ultracentrifugation ; Virulence Factors/isolation & purification
    Chemical Substances Culture Media, Conditioned ; Protozoan Proteins ; Virulence Factors
    Language English
    Publishing date 2013-01-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/pr300947g
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  10. Article ; Online: Posttranscriptional mechanisms involved in the control of expression of the stage-specific GP82 surface glycoprotein in Trypanosoma cruzi.

    Gentil, Luciana Girotto / Cordero, Esteban Maurício / do Carmo, Mirian Silva / dos Santos, Márcia Regina Machado / da Silveira, José Franco

    Acta tropica

    2009  Volume 109, Issue 2, Page(s) 152–158

    Abstract: Trypanosoma cruzi metacyclic trypomastigotes express the developmentally regulated GP82 glycoprotein, which is implicated in host cell invasion. Although GP82 mRNA and protein are not present and the mRNAs barely detectable in epimastigotes, nuclear run- ... ...

    Abstract Trypanosoma cruzi metacyclic trypomastigotes express the developmentally regulated GP82 glycoprotein, which is implicated in host cell invasion. Although GP82 mRNA and protein are not present and the mRNAs barely detectable in epimastigotes, nuclear run-on analysis showed that it is transcribed in both stages. This result indicates that accumulation of transcripts in metacyclic forms is not due to increased transcription of the GP82 gene. To investigate whether mRNA stability may be responsible for the differences in the steady-state levels of this mRNA, parasites were treated with actinomycin D or cycloheximide. When treated with actinomycin D, the half-lives estimated for GP82 transcripts were about 6h in metacyclic trypomastigotes and 0.5h in epimastigotes. In the presence of cycloheximide, the levels of GP82 mRNA decayed slightly after 8h in metacyclic trypomastigotes, whereas in epimastigotes the levels of this mRNA increased. This effect suggests a stabilizing mechanism acting in metacyclic trypomastigotes and a destabilizing mechanism in epimastigotes which could be mediated by an element present in the 3'-UTR of the transcripts. Consistent with this finding, northern blot analysis showed that GP82 mRNAs were mobilized to polysomes and consequently translated, but only in metacyclic trypomastigotes.
    MeSH term(s) 3' Untranslated Regions ; Animals ; Gene Expression Regulation ; Polyribosomes/metabolism ; Protein Biosynthesis ; Protozoan Proteins/biosynthesis ; RNA Stability ; Trypanosoma cruzi/genetics ; Trypanosoma cruzi/physiology ; Variant Surface Glycoproteins, Trypanosoma/biosynthesis
    Chemical Substances 3' Untranslated Regions ; Protozoan Proteins ; Variant Surface Glycoproteins, Trypanosoma ; glycoprotein GP82, Trypanosoma cruzi
    Language English
    Publishing date 2009-02
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 210415-5
    ISSN 1873-6254 ; 0001-706X
    ISSN (online) 1873-6254
    ISSN 0001-706X
    DOI 10.1016/j.actatropica.2008.10.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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