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The effects of these ESA on the host cell function may participate in the establishment of a successful infection, in which the parasite persists for a sufficient period of time to complete its life cycle. A number of regulatory components or processes originating from the parasite that control or regulate the metabolism and the growth of host cell have been identified. The purpose of the present review is to analyze some of the current data related to the parasite ESA that interfere with the host cell physiology. Special attention is given to members of conserved protein families demonstrating remarkable diversity and plasticity of function (ie, glutathione S-transferases and related molecules; members of the trans-sialidase and mucin family; and members of the ribosomal protein family). 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window.loginModal.appleClientId = 'edu.academia.applesignon';</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":48583885,"attachmentType":"pdf"}"><img alt="First page of “Host Cell Phenotypic Variability Induced by Trypanosomatid-Parasite-Released Immunomodulatory Factors: Physiopathological Implications”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/48583885/mini_magick20190203-9956-bofiv3.png?1549199376" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/images/single_work_splash/adobe_icon.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">Host Cell Phenotypic Variability Induced by Trypanosomatid-Parasite-Released Immunomodulatory Factors: Physiopathological Implications</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="12324004" href="https://independent.academia.edu/JoanaTavares2"><img alt="Profile image of Joana Tavares" class="ds-work-card--author-avatar" src="https://0.academia-photos.com/12324004/4968739/5706584/s65_joana.tavares.jpg" />Joana Tavares</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">2004, Journal of Biomedicine and Biotechnology</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">9 pages</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 7143032; const worksViewsPath = "/v0/works/views?subdomain_param=api&work_ids%5B%5D=7143032"; const getWorkViews = async (workId) => { const response = await fetch(worksViewsPath); if (!response.ok) { throw new Error('Failed to load work views'); } const data = await response.json(); return data.views[workId]; }; // Get the view count for the work - we send this immediately rather than waiting for // the DOM to load, so it can be available as soon as possible (but without holding up // the backend or other resource requests, because it's a bit expensive and not critical). const viewCount = await getWorkViews(workId); const updateViewCount = (viewCount) => { try { const viewCountNumber = parseInt(viewCount, 10); if (viewCountNumber === 0) { // Remove the whole views element if there are zero views. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); return; } const commaizedViewCount = viewCountNumber.toLocaleString(); const viewCountBody = document.getElementById('work-metadata-view-count'); if (!viewCountBody) { throw new Error('Failed to find work views element'); } viewCountBody.textContent = `${commaizedViewCount} views`; } catch (error) { // Remove the whole views element if there was some issue parsing. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); throw new Error(`Failed to parse view count: ${viewCount}`, error); } }; // If the DOM is still loading, wait for it to be ready before updating the view count. if (document.readyState === "loading") { document.addEventListener('DOMContentLoaded', () => { updateViewCount(viewCount); }); // Otherwise, just update it immediately. } else { updateViewCount(viewCount); } })();</script></div><p class="ds-work-card--work-abstract ds-work-card--detail ds2-5-body-md">The parasitic protozoa Trypanosoma cruzi and Leishmania sp release a variety of molecules into their mammalian hosts (ESA: excretory-secretory products). The effects of these ESA on the host cell function may participate in the establishment of a successful infection, in which the parasite persists for a sufficient period of time to complete its life cycle. A number of regulatory components or processes originating from the parasite that control or regulate the metabolism and the growth of host cell have been identified. The purpose of the present review is to analyze some of the current data related to the parasite ESA that interfere with the host cell physiology. Special attention is given to members of conserved protein families demonstrating remarkable diversity and plasticity of function (ie, glutathione S-transferases and related molecules; members of the trans-sialidase and mucin family; and members of the ribosomal protein family). The identification of parasite target molecules and the elucidation of their mode of action toward the host cell represents a step forward in efforts aimed at an immunotherapeutic or pharmacological control of parasitic infection.</p><div class="ds-work-card--button-container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--work-card","attachmentId":48583885,"attachmentType":"pdf","workUrl":"https://www.academia.edu/7143032/Host_Cell_Phenotypic_Variability_Induced_by_Trypanosomatid_Parasite_Released_Immunomodulatory_Factors_Physiopathological_Implications"}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--work-card","attachmentId":48583885,"attachmentType":"pdf","workUrl":"https://www.academia.edu/7143032/Host_Cell_Phenotypic_Variability_Induced_by_Trypanosomatid_Parasite_Released_Immunomodulatory_Factors_Physiopathological_Implications"}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div><div class="ds-signup-banner-trigger-container"><div class="ds-signup-banner-trigger"></div></div><div class="ds-signup-banner"><div id="ds-signup-banner-close-button"><button class="ds2-5-button ds2-5-button--secondary ds2-5-button--inverse"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">close</span></button></div><div class="ds-signup-banner-ctas"><img src="//a.academia-assets.com/images/academia-logo-capital-white.svg" /><h4 class="ds2-5-heading-serif-sm">Sign up for access to the world's latest research.</h4><button class="ds2-5-button ds2-5-button--inverse ds2-5-button--full-width js-swp-download-button" data-signup-modal="{"location":"signup-banner"}">Sign up for free</button></div><div class="ds-signup-banner-divider"></div><div class="ds-signup-banner-reasons"><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Get notified about relevant papers</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Save papers to use in your research</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Join the discussion with peers</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Track your impact</span></div></div></div><script>(() => { // Set up signup banner show/hide behavior: // 1. 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T. cruzi trypomastigotes (Ty), the classical infective stage, interact with the extracellular matrix (ECM), an obligatory step before invasion of almost all mammalian cells in different tissues. Here we have characterized the proteome and phosphoproteome of T. cruzi trypomastigotes upon interaction with ECM (MTy) and the data are available via ProteomeXchange with identifier PXD010970. Proteins involved with metabolic processes (such as the glycolytic pathway), kinases, flagellum and microtubule related proteins, transport-associated proteins and RNA/DNA binding elements are highly represented in the pool of proteins modified by phosphorylation. Further, important metabolic switches triggered by this interaction with ECM were indicated by decreases in the phosphorylation of hexokinase, phosphofructokinase, fructose-2,6-bisphosphatase, phosphoglucomutase, phosphoglycerate kinase in MTy. Concomitantly, a decrease in the pyruvate and lactate and an increase of glucose and succinate contents were detected by GC-MS. These observations led us to focus on the changes in the glycolytic pathway upon binding of the parasite to the ECM. Inhibition of hexokinase, pyruvate kinase and lactate dehydrogenase activities in MTy were observed and this correlated with the phosphorylation levels of the respective enzymes. Putative kinases involved in protein phosphorylation altered upon parasite incubation with ECM were suggested by in silico analysis. Taken together, our results show that in addition to cytoskeletal changes and protease activation, a reprogramming of the trypomastigote metabolism is triggered by the interaction of the parasite with the ECM prior to cell invasion and differentiation into amastigotes, the multiplicative intracellular stage of T. cruzi in the vertebrate host.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Reprogramming of Trypanosoma cruzi metabolism triggered by parasite interaction with the host cell extracellular matrix","attachmentId":80965433,"attachmentType":"pdf","work_url":"https://www.academia.edu/71751642/Reprogramming_of_Trypanosoma_cruzi_metabolism_triggered_by_parasite_interaction_with_the_host_cell_extracellular_matrix","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/71751642/Reprogramming_of_Trypanosoma_cruzi_metabolism_triggered_by_parasite_interaction_with_the_host_cell_extracellular_matrix"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="1" data-entity-id="123807187" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/123807187/Trypanosoma_cruziglutathione_binding_proteins_immunogenicity_during_human_and_experimental_Chagas_disease">Trypanosoma cruziglutathione-binding proteins: immunogenicity during human and experimental Chagas' disease</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="284618179" href="https://independent.academia.edu/AliTaibi6">Ali Taibi</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Parasitology, 1992</p><p class="ds-related-work--abstract ds2-5-body-sm">SUMMARYFollowing purification by affinity chromatography, three glutathione-binding proteins (TcGBP) of 45, 30, and 25 kDa were co-purified fromTrypanosoma cruziepimastigotes. Using 1-chloro-2,4 dinitrobenzene as substrate, a glutathione S-transferase activity of 70 nmol/min/mg of proteins was detected in the GSH binding fraction. An increased expression of TcGBP and total GST activity was observed upon incubation of parasites with phenobarbital, which is an inducer of GST synthesis. Immunofluorescence and electron microscopic experiments demonstrated that TcGBP were expressed by all developmental stages of the parasite, including infective forms. The expression of these proteins by intracellular dividing amastigotes could be in favour of a potential defensive role of these molecules against host attack. Results obtained by immunoprecipitation ofin vitrotranslation products using anti-TcGBP antisera suggested that these three polypeptides are not glycosylated. In addition, antibodie...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Trypanosoma cruziglutathione-binding proteins: immunogenicity during human and experimental Chagas' disease","attachmentId":118154084,"attachmentType":"pdf","work_url":"https://www.academia.edu/123807187/Trypanosoma_cruziglutathione_binding_proteins_immunogenicity_during_human_and_experimental_Chagas_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/123807187/Trypanosoma_cruziglutathione_binding_proteins_immunogenicity_during_human_and_experimental_Chagas_disease"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="2" data-entity-id="56260048" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/56260048/The_Dialogue_of_the_Host_Parasite_Relationship_Leishmania_spp_and_Trypanosoma_cruzi_Infection">The Dialogue of the Host-Parasite Relationship: Leishmania spp. and Trypanosoma cruzi Infection</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="119226744" href="https://independent.academia.edu/PatriciaDutra8">Patricia Dutra</a></div><p class="ds-related-work--metadata ds2-5-body-xs">BioMed Research International, 2015</p><p class="ds-related-work--abstract ds2-5-body-sm">The intracellular protozoaLeishmaniaspp. andTrypanosoma cruziand the causative agents of Leishmaniasis and Chagas disease, respectively, belong to the Trypanosomatidae family. Together, these two neglected tropical diseases affect approximately 25 million people worldwide. Whether the host can control the infection or develops disease depends on the complex interaction between parasite and host. Parasite surface and secreted molecules are involved in triggering specific signaling pathways essential for parasite entry and intracellular survival. The recognition of the parasite antigens by host immune cells generates a specific immune response.Leishmaniaspp. andT. cruzihave a multifaceted repertoire of strategies to evade or subvert the immune system by interfering with a range of signal transduction pathways in host cells, which causes the inhibition of the protective response and contributes to their persistence in the host. The current therapeutic strategies in leishmaniasis and tr...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"The Dialogue of the Host-Parasite Relationship: Leishmania spp. and Trypanosoma cruzi Infection","attachmentId":71733517,"attachmentType":"pdf","work_url":"https://www.academia.edu/56260048/The_Dialogue_of_the_Host_Parasite_Relationship_Leishmania_spp_and_Trypanosoma_cruzi_Infection","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/56260048/The_Dialogue_of_the_Host_Parasite_Relationship_Leishmania_spp_and_Trypanosoma_cruzi_Infection"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="3" data-entity-id="2551832" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/2551832/Enolase_a_key_player_in_the_metabolism_and_a_probable_virulence_factor_of_trypanosomatid_parasites_perspectives_for_its_use_as_a_therapeutic_target">Enolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="3311773" href="https://ula.academia.edu/WilfredoQui%C3%B1ones">Wilfredo Quiñones</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Enzyme research, 2011</p><p class="ds-related-work--abstract ds2-5-body-sm">Glycolysis and glyconeogenesis play crucial roles in the ATP supply and synthesis of glycoconjugates, important for the viability and virulence, respectively, of the human-pathogenic stages of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp. These pathways are, therefore, candidate targets for antiparasite drugs. The glycolytic/gluconeogenic enzyme enolase is generally highly conserved, with similar overall fold and identical catalytic residues in all organisms. Nonetheless, potentially important differences exist between the trypanosomatid and host enzymes, with three unique, reactive residues close to the active site of the former that might be exploited for the development of new drugs. In addition, enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. This location and possible function of enolase offer additional perspectives for both drug discovery and vaccination.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Enolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target","attachmentId":50571593,"attachmentType":"pdf","work_url":"https://www.academia.edu/2551832/Enolase_a_key_player_in_the_metabolism_and_a_probable_virulence_factor_of_trypanosomatid_parasites_perspectives_for_its_use_as_a_therapeutic_target","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/2551832/Enolase_a_key_player_in_the_metabolism_and_a_probable_virulence_factor_of_trypanosomatid_parasites_perspectives_for_its_use_as_a_therapeutic_target"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="4" data-entity-id="24693435" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/24693435/Trypanosoma_cruzi_Leishmania_donovani_and_L_mexicana_Extract_factor_that_lyses_mammalian_cells">Trypanosoma cruzi, Leishmania donovani, and L. mexicana: Extract factor that lyses mammalian cells</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="47597816" href="https://independent.academia.edu/JODaly">J. O'Daly</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="48090379" href="https://usb.academia.edu/PedroAso">Pedro Aso</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="51688985" href="https://independent.academia.edu/JoseODaly">Jose O'Daly</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Experimental Parasitology, 1979</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Trypanosoma cruzi, Leishmania donovani, and L. mexicana: Extract factor that lyses mammalian cells","attachmentId":45024047,"attachmentType":"pdf","work_url":"https://www.academia.edu/24693435/Trypanosoma_cruzi_Leishmania_donovani_and_L_mexicana_Extract_factor_that_lyses_mammalian_cells","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/24693435/Trypanosoma_cruzi_Leishmania_donovani_and_L_mexicana_Extract_factor_that_lyses_mammalian_cells"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="5" data-entity-id="103960751" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/103960751/From_the_cell_biology_to_the_development_of_new_chemotherapeutic_approaches_against_trypanosomatids_dreams_and_reality">From the cell biology to the development of new chemotherapeutic approaches against trypanosomatids: dreams and reality</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="31729059" href="https://independent.academia.edu/SouzaWanderleyde">Wanderley de Souza</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Kinetoplastid Biology and Disease, 2002</p><p class="ds-related-work--abstract ds2-5-body-sm">Members of the Trypanosomatidae family comprise a large number of species that are causative agents of important diseases such as sleeping sickness, Chagas' disease and Leishmaniasis. These organisms are also of biological interest since they are able to change the morphology according to the environment where they live, through a process of reversible cell transformation, and possess structures and organelles that are not found in mammalian cells. This review analyses the process of transformation, which takes place during the life cycle of Trypanosoma cruzi in the vertebrate and invertebrate hosts. Special attention is given to the interaction of the parasite with vertebrate cells. In addition, the present knowledge of structures and organelles such as the nucleus, the plasma membrane, the sub-pellicular microtubules, the flagellum, the kinetoplast-mitochondrion complex, the peroxisome (glycosome), the acidocalcisome and the structures and organelles involved in the endocytic pathway, is reviewed from a cell biology perspective. The possible use of available data for the development of new anti parasite drugs is also discussed.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"From the cell biology to the development of new chemotherapeutic approaches against trypanosomatids: dreams and reality","attachmentId":103819718,"attachmentType":"pdf","work_url":"https://www.academia.edu/103960751/From_the_cell_biology_to_the_development_of_new_chemotherapeutic_approaches_against_trypanosomatids_dreams_and_reality","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/103960751/From_the_cell_biology_to_the_development_of_new_chemotherapeutic_approaches_against_trypanosomatids_dreams_and_reality"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="6" data-entity-id="11301625" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/11301625/Trypanosoma_cruzi_Induced_Host_Immune_System_Dysfunction_A_Rationale_for_Parasite_Immunosuppressive_Factor_s_Encoding_Gene_Targeting">Trypanosoma cruzi-Induced Host Immune System Dysfunction: A Rationale for Parasite Immunosuppressive Factor(s) Encoding Gene Targeting</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="27327835" href="https://requimte.academia.edu/MargaridaBorges">Margarida Borges</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of biomedicine & biotechnology, 2001</p><p class="ds-related-work--abstract ds2-5-body-sm">An intense suppression of T cell proliferation to mitogens and to antigens is observed in a large number of parasitic infections. The impairment of T cell proliferation also occurred during the acute phase of Chagas' disease, caused by the intracellular protozoan parasite Trypanosoma cruzi. A wealth of evidence has accumulated that illustrates the ability of T. cruzi released molecules to influence directly a variety of diverse immunological functions. In this paper, we review the data concerning the immunoregulatory effects of T. cruzi Tc24 (a B cell activator antigen) and Tc52 (an immunosuppressive protein) released molecules on the host immune system. The gene targeting approach developed to further explore the biological function(s) of Tc52 molecule, revealed interesting unexpected functional properties. Indeed, in addition to its immunusuppressive activity a direct or indirect involvement of Tc52 gene product alone or in combination with other cellular components in T. cruzi differentiation control mechanisms have been evidenced. Moreover, targeted Tc52 replacement allowed the obtention of parasite mutants exhibiting low virulence in vitro and in vivo. Thus, the generation of a complete deficiency state of virulence factors by gene targeting should provide a means to assess the importance of these factors in the pathophysiological processes and disease progression. It is hoped that such approaches might allow rational design of tools to control T. cruzi infections.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Trypanosoma cruzi-Induced Host Immune System Dysfunction: A Rationale for Parasite Immunosuppressive Factor(s) Encoding Gene Targeting","attachmentId":46766487,"attachmentType":"pdf","work_url":"https://www.academia.edu/11301625/Trypanosoma_cruzi_Induced_Host_Immune_System_Dysfunction_A_Rationale_for_Parasite_Immunosuppressive_Factor_s_Encoding_Gene_Targeting","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/11301625/Trypanosoma_cruzi_Induced_Host_Immune_System_Dysfunction_A_Rationale_for_Parasite_Immunosuppressive_Factor_s_Encoding_Gene_Targeting"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="7030488" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/7030488/A_century_of_research_what_have_we_learned_about_the_interaction_of_Trypanosoma_cruzi_with_host_cells">A century of research: what have we learned about the interaction of Trypanosoma cruzi with host cells</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="11993025" href="https://unifesp.academia.edu/RMortara">Renato Mortara</a></div><p class="ds-related-work--abstract ds2-5-body-sm">Key words: Trypanosoma cruzi -cellular invasion -trypomastigotes -amastigotes -parasitophorous vacuole escape -phylogenetic lineages with mouse macrophages in vitro. Infect Immun 33: 54�-554. Carvalho TM, De Souza W 198�. Infectivity of amastigotes of Trypanosoma cruzi. Rev Inst Med Trop Sao Paulo 28: 205-212. Carvalho TM, De Souza W 1989. Early events related with the behavior of Trypanosoma cruzi within an endocytic vacuole in mouse peritoneal macrophages. Cell Struct Funct 14: �8�-�92. Carvalho TM, Ferreira �G, Coimbra ES, Rosestolato CT, De Souza W 1999. Distribution of cytoskeletal structures and organelles of the host cell during evolution of the intracellular parasitism by Trypanosoma cruzi. J Submicrosc Cytol Pathol 31: �25-��. Chagas C 1909. Nova tripanozomíase humana. Estudos sobre a morfologia e o ciclo evolutivo do Schizotrypanum n.gen, n. sp., agente etiológico de nova entidade mórbida do homem. Mem Inst Oswaldo Cruz 1: 159-218. Chagas C 1911. Nova entidade morbida do homem. Resumo geral de estudos etiologicos e clínicos. Mem Inst Oswaldo Cruz 3: 219-2�5. Chaves LB, Briones MRS, Schenkman S 199�. Trans-sialidase from Trypanosoma cruzi epimastigotes is expressed at the stationary phase and is different from the enzyme expressed in trypomastigotes. Mol Biochem Parasitol 61: 9�-10�. Chuenkova M, Pereira ME� 1995. Trypanosoma cruzi trans-sialidase: enhancement of virulence in a murine model of Chagas' disease. J Exp Med 181: 1�9�-1�0�. Chuenkova MV, Pereira M� 2001. The T. cruzi trans-sialidase induces PC12 cell differentiation via M�PK/ERK pathway. Neuroreport 12: ��15-��18. Coimbra VC, Yamamoto D, Khusal KG, �tayde VD, Fernandes MC, Mortara R�, Yoshida N, �lves MJ, Rabinovitch M 200�. Enucleated L929 cells support invasion, differentiation and multiplication of Trypanosoma cruzi parasites. Infect Immun 75: ��00-��0�. Colli W 1984. Interiorization of Trypanosoma cruzi into mammalian host cells in the light of the parasite membrane chemical composition. Mem Inst Oswaldo Cruz 79: 45-50. Colli W 199�. Trans-sialidase: a unique enzyme activity discovered in the protozoan Trypanosoma cruzi. FASEB J 7: 125�-12�4. Cortez M, �tayde V, Yoshida N 200�. Host cell invasion mediated by Trypanosoma cruzi surface molecule gp82 is associated with Factin disassembly and is inhibited by enteroinvasive Escherichia coli. Microbes Infect 8: 1502-1512. Couto �S, De Lederkremer RM, Colli W, �lves MJM 199�. The glycosylphosphatidylinositol anchor of the trypomastigote-specific Tc-85 glycoprotein from Trypanosoma cruzi--metabolic-labeling and structural studies. Eur J Biochem 217: 59�-�02. Couto �S, Gonçalves MF, Colli W, Lederkremer RM 1990. The N-linked carbohydrate chain of the 85-kilodalton glycoprotein from Trypanosoma cruzi trypomastigotes contains sialyl, fucosyl and galactosyl (alpha 1-�) galactose units. Mol Biochem Parasitol 39: 101-10�. Cross G�M, Takle GB 199�. The surface trans-sialidase family of Trypanosoma cruzi. Annu Rev Microbiol 47: �85-411. da Silva CV, Kawashita SY, Probst CM, Dallagiovanna B, Cruz MC, Silva E�, Souto-Padrón T, Krieger M�, Goldenberg S, Briones MRS, �ndrews NW, Mortara R� 2009. Characterization of a 21 kDa protein from Trypanosoma cruzi associated with mammalian cell invasion. Microbes Infect, in press. de Lederkremer RM, Casal OL, �lves MJ, Colli W 1980. Evidence for the presence of D-galactofuranose in the lipopeptidophosphoglycan from Trypanosome cruzi. Modification and tritium labeling. FEBS Lett 116: 25-29. de Lederkremer RM, Colli W 1995. Galactofuranose-containing glycoconjugates in trypanosomatids. Glycobiology 5: 54�-552. De Meis J, Ferreira LM, Guillermo LV, Silva EM, Dosreis G�, Lopes MF 2008. �poptosis differentially regulates mesenteric and subcutaneous lymph node immune responses to Trypanosoma cruzi. Eur J Immunol 38: 1�9-14�. De Souza W 1984. Cell biology of Trypanosoma cruzi. Int Rev Cell Biol 86: 19�-28�. De Souza W 2000. O parasito e sua interação com os hospedeiros. In Trypanosoma cruzi e doença de Chagas. Z Brener, Z� �ndrade, M Barral-Netto (eds.), Guanabara Koogan, Rio de Janeiro, p. 88-12�. De Souza W 2002. Basic cell biology of Trypanosoma cruzi. Curr Pharm Des 8: 2�9-285. De Souza W 2005. Microscopy and cytochemistry of the biogenesis of the parasitophorous vacuole. Histochem Cell Biol 123: 1-18. De Souza W 2008. Electron microscopy of trypanosomes -a historical view. Mem Inst Oswaldo Cruz 103: �1�-�25. de Titto EH, �raujo FG 198�. Mechanism of cell invasion by Trypanosoma cruzi: importance of sialidase activity. Acta Trop 44: 2��-282. Devera R, Fernandes O, Coura JR 200�. Should Trypanosoma cruzi be called �cruzi" complex? � review of the parasite diversity and the potential of selecting population after in vitro culturing and mice infection. Mem Inst Oswaldo Cruz 98: 1-12. Dias WB, Fajardo FD, Graca-Souza �V, Freire-de-Lima L, Vieira F, Girard MF, Bouteille B, Previato JO, Mendonca-Previato L, Todeschini �R 2008. Endothelial cell signalling induced by transsialidase from Trypanosoma cruzi. Cell Microbiol 10: 88-99. Docampo R, Scott D�, Vercesi �E, Moreno SNJ 1995. Intracellular Ca 2+ storage in acidocalcisomes of Trypanosoma cruzi. Biochem J 310: 1005-1012. Dorta ML, Ferreira �T, Oshiro MEM, Yoshida N 1995. Ca 2+ signal induced by Trypanosoma cruzi metacyclic trypomastigote surface molecules implicated in mammalian cell invasion. Mol Biochem Parasitol 73: 285-289. Dvorak J�, Howe CL 19��. The attraction of Trypanosoma cruzi to vertebrate cells in vitro. J Protozool 23: 5�4-5��. Dvorak J�, Hyde TP 19��. Trypanosoma cruzi: interaction with vertebrate cells in vitro. Individual interactions at the cellular and subcellular levels. Exp Parasitol 34: 2�8-28�. Eakin �E, Mills ��, Harth G, McKerrow JH, Craik CS 1992. The sequence, organization and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi. J Biol Chem 267: �411-�420. CM, Stuart KD, �ndersson B 2005a. The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease. Science 309: 409-415. Hudson L, Snary D, Morgan SJ 1984. Trypanosoma cruzi: continuous cultivation with murine cell lines. Parasitology 88: 28�-294. Junqueira �C, Degrave W, Brandao � 2005. Minicircle organization and diversity in Trypanosoma cruzi populations. Trends Parasitol 21: 2�0-2�2. Kahn S, Kahn M, Van Voorhis WC, Goshorn �, Strand �, Hoagland N, Eisen H, Pennathur S 199�. S�85-1 proteins of Trypanosoma cruzi lack sialidase activity. Mol Biochem Parasitol 60: 149-152. Kahn S, Wleklinski M, �ruffo �, Farr �, Coder D, Kahn M 1995. Trypanosoma cruzi amastigote adhesion to macrophages is facilitated by the mannose receptor. J Exp Med 182: 124�-1258. Kahn SJ, Wleklinski M, Ezekowitz R�, Coder D, �ruffo �, Farr � 199�. The major surface glycoprotein of Trypanosoma cruzi amastigotes are ligands of the human serum mannose-binding protein. Infect Immun 64: 2�49-2�5�.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"A century of research: what have we learned about the interaction of Trypanosoma cruzi with host cells","attachmentId":33687039,"attachmentType":"pdf","work_url":"https://www.academia.edu/7030488/A_century_of_research_what_have_we_learned_about_the_interaction_of_Trypanosoma_cruzi_with_host_cells","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/7030488/A_century_of_research_what_have_we_learned_about_the_interaction_of_Trypanosoma_cruzi_with_host_cells"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="8" data-entity-id="10560006" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/10560006/Heterologous_Expression_of_Trypanosoma_cruzi_trans_Sialidase_in_Leishmania_major_Enhances_Virulence">Heterologous Expression of Trypanosoma cruzi trans-Sialidase in Leishmania major Enhances Virulence</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="25848792" href="https://independent.academia.edu/WendaGao">Wenda Gao</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Infection and Immunity, 2000</p><p class="ds-related-work--abstract ds2-5-body-sm">Earlier studies showed that mice primed for a few hours with the trans-sialidase (TS) of Trypanosoma cruzi, the agent of Chagas' disease, become highly susceptible to trypanosomal infection. These studies suggest that TS affects parasite virulence independent of antigenic stimulation. Potentially, TS could enhance or reduce the virulence of heterologous microbes depending on the mechanism of TS action and on the type of immune response elicited by the particular parasite. We tested this hypothesis by expressing heterologous TS in Leishmania major, a protozoan parasite that causes cutaneous leishmaniasis and lacks TS and the TS product ␣2-3-linked sialic acid. Leishmania cells transfected with a T. cruzi TS expression construct made high levels of active enzyme, which was present in the promastigotes and shed into the extracellular milieu. TS expression did not affect L. major binding to and entry into cultured macrophages or its tropism for macrophage infection in vivo. However, TS-expressing L. major exhibited elevated virulence in BALB/c mice, as determined by lesion progression, parasite numbers, and macro-and microscopic examination of cutaneous lesions. Several genetic tests proved that the enhanced virulence was directly attributable to TS expression. The results are consistent with TS functioning to sabotage the mouse immune system to confer a growth advantage on T. cruzi and transgenic L. major. These data suggest that heterologous expression of T. cruzi virulence factors in Leishmania may provide a new approach for dissecting their function in vivo.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Heterologous Expression of Trypanosoma cruzi trans-Sialidase in Leishmania major Enhances Virulence","attachmentId":47303781,"attachmentType":"pdf","work_url":"https://www.academia.edu/10560006/Heterologous_Expression_of_Trypanosoma_cruzi_trans_Sialidase_in_Leishmania_major_Enhances_Virulence","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/10560006/Heterologous_Expression_of_Trypanosoma_cruzi_trans_Sialidase_in_Leishmania_major_Enhances_Virulence"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="9" data-entity-id="55080980" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/55080980/Mice_infected_with_Trypanosoma_cruzi_produce_antibodies_against_the_enzymatic_domain_of_trans_sialidase_that_inhibit_its_activity">Mice infected with Trypanosoma cruzi produce antibodies against the enzymatic domain of trans-sialidase that inhibit its activity</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="44406175" href="https://independent.academia.edu/OscarCampetella">Oscar Campetella</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Infection and immunity, 1994</p><p class="ds-related-work--abstract ds2-5-body-sm">trans-Sialidase (TS) is an enzymatic activity described only for trypanosomes that is involved in the invasion of host cells by Trypanosoma cruzi. The enzyme that is shed by the parasite is made of two domains, the C-terminal region containing immunodominant amino acid repeats that define the SAPA antigen and the N-terminal domain that contains the putative region for enzymatic activity. The SAPA antigen induces a strong humoral response detected shortly after infection, both in humans and in mice. This response is directed to the immunodominant domain but is irrelevant in terms of neutralization of TS activity. We now show that TS activity can be detected in sera from acutely infected mice. However, mice infected with a T. cruzi strain whose growth can be controlled by the host did not have detectable levels of TS activity in sera. In fact, sera from these mice were able to abolish TS activity. This inhibition was due to the presence of specific antibodies directed against the enzy...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Mice infected with Trypanosoma cruzi produce antibodies against the enzymatic domain of trans-sialidase that inhibit its activity","attachmentId":71126191,"attachmentType":"pdf","work_url":"https://www.academia.edu/55080980/Mice_infected_with_Trypanosoma_cruzi_produce_antibodies_against_the_enzymatic_domain_of_trans_sialidase_that_inhibit_its_activity","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/55080980/Mice_infected_with_Trypanosoma_cruzi_produce_antibodies_against_the_enzymatic_domain_of_trans_sialidase_that_inhibit_its_activity"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div></div></div><div class="ds-sticky-ctas--wrapper js-loswp-sticky-ctas hidden"><div class="ds-sticky-ctas--grid-container"><div class="ds-sticky-ctas--container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--sticky-ctas","attachmentId":48583885,"attachmentType":"pdf","workUrl":null}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--sticky-ctas","attachmentId":48583885,"attachmentType":"pdf","workUrl":null}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div><div class="ds-below-fold--grid-container"><div class="ds-work--container js-loswp-embedded-document"><div class="attachment_preview" data-attachment="Attachment_48583885" style="display: none"><div class="js-scribd-document-container"><div class="scribd--document-loading js-scribd-document-loader" style="display: block;"><img alt="Loading..." src="//a.academia-assets.com/images/loaders/paper-load.gif" /><p>Loading Preview</p></div></div><div style="text-align: center;"><div class="scribd--no-preview-alert js-preview-unavailable"><p>Sorry, preview is currently unavailable. 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class="ds-related-work--metadata ds2-5-body-xs">The Journal of Infectious Diseases, 2011</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Host Cell Lipid Bodies Triggered by Trypanosoma cruzi Infection and Enhanced by the Uptake of Apoptotic Cells Are Associated With Prostaglandin E2 Generation and Increased Parasite Growth","attachmentId":119552576,"attachmentType":"pdf","work_url":"https://www.academia.edu/125525725/Host_Cell_Lipid_Bodies_Triggered_by_Trypanosoma_cruzi_Infection_and_Enhanced_by_the_Uptake_of_Apoptotic_Cells_Are_Associated_With_Prostaglandin_E2_Generation_and_Increased_Parasite_Growth","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link 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ds2-5-body-xs">Molecular and Biochemical Parasitology, 2009</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Functional characterization of stage-specific aminotransferases from trypanosomatids","attachmentId":100879440,"attachmentType":"pdf","work_url":"https://www.academia.edu/99917750/Functional_characterization_of_stage_specific_aminotransferases_from_trypanosomatids","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/99917750/Functional_characterization_of_stage_specific_aminotransferases_from_trypanosomatids"><span class="ds2-5-text-link__content">View PDF</span><span 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data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/70439702/Defective_transport_of_pyrazolopyrimidine_ribosides_in_insensitive_trypanosoma_cruzi_wild_strains_is_a_parasite_stage_specific_and_reversible_characteristic">Defective transport of pyrazolopyrimidine ribosides in insensitive trypanosoma cruzi wild strains is a parasite-stage specific and reversible characteristic</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="16621441" href="https://independent.academia.edu/AngelaAvila2">Angela Avila</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1987</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" 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