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In addition, images obtained with the use of the high-resolution backscattered electrons (BSE) detector provided a powerful tool for immunocytochemical analysis of biological material. In this work, we show the contribution of the FESEM to the detailed description of cytoskeletal structures of the protozoan parasites Herpetomonas megaseliae, Trypanosoma brucei and Giardia lamblia. High-resolution images of detergent extracted H. megaseliae and T. brucei showed the profile of the cortical microtubules, also known as sub-pellicular microtubules (SPMT), and protein bridges cross-linking them. Also, it was possible to visualize fine details of the filaments that form the lattice-like structure of the paraflagellar rod (PFR) and its connection with the axoneme. In G. lamblia, it was possible to observe the intricate structure of the adhesive disk, funis (a microtubular array) and other cytoskeletal structures poorly described previously. Since most of the stable cytoskeletal structures of this protozoan rely on tubulin, we used the BSE images to accurately map immunolabeled tubulin in its cytoskeleton. Our results suggest that the observation of detergent extracted parasites using FESEM associated to backscattered analysis of immunolabeled specimens represents a new approach for the study of parasite cytoskeletal elements and their protein associations.","author":[{"@context":"https://schema.org","@type":"Person","name":"Daniela Lourenço"}],"contributor":[],"dateCreated":"2015-01-20","datePublished":"2005-01-01","headline":"Improvement on the visualization of cytoskeletal structures of protozoan parasites using high-resolution field emission scanning electron microscopy (FESEM","image":"https://attachments.academia-assets.com/47468226/thumbnails/1.jpg","inLanguage":"en","keywords":["Scanning Electron Microscopy","Cytoskeleton","Parasites","Flagella","High Resolution","Trypanosoma brucei","Trypanosoma brucei brucei","Secondary Electron","Field Emission Scanning Electron Microscopy"],"publication":"Histochemistry and Cell Biology","publisher":{"@context":"https://schema.org","@type":"Organization","name":null},"sourceOrganization":[{"@context":"https://schema.org","@type":"EducationalOrganization","name":null}],"thumbnailUrl":"https://attachments.academia-assets.com/47468226/thumbnails/1.jpg","url":"https://www.academia.edu/10250933/Improvement_on_the_visualization_of_cytoskeletal_structures_of_protozoan_parasites_using_high_resolution_field_emission_scanning_electron_microscopy_FESEM"}</script><link rel="stylesheet" media="all" href="//a.academia-assets.com/assets/single_work_page/loswp-4e3d039261950d4b4b1a4aa831b9fce420f969e92cf016bd1a7151245032ceae.css" /><link rel="stylesheet" media="all" href="//a.academia-assets.com/assets/design_system/body-8d679e925718b5e8e4b18e9a4fab37f7eaa99e43386459376559080ac8f2856a.css" /><link rel="stylesheet" media="all" href="//a.academia-assets.com/assets/design_system/button-3cea6e0ad4715ed965c49bfb15dedfc632787b32ff6d8c3a474182b231146ab7.css" /><link rel="stylesheet" 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contrast and in the generation of high-resolution images. In addition, images obtained with the use of the high-resolution backscattered electrons (BSE) detector provided a powerful tool for immunocytochemical analysis of biological material. In this work, we show the contribution of the FESEM to the detailed description of cytoskeletal structures of the protozoan parasites Herpetomonas megaseliae, Trypanosoma brucei and Giardia lamblia. High-resolution images of detergent extracted H. megaseliae and T. brucei showed the profile of the cortical microtubules, also known as sub-pellicular microtubules (SPMT), and protein bridges cross-linking them. Also, it was possible to visualize fine details of the filaments that form the lattice-like structure of the paraflagellar rod (PFR) and its connection with the axoneme. In G. lamblia, it was possible to observe the intricate structure of the adhesive disk, funis (a microtubular array) and other cytoskeletal structures poorly described previously. Since most of the stable cytoskeletal structures of this protozoan rely on tubulin, we used the BSE images to accurately map immunolabeled tubulin in its cytoskeleton. Our results suggest that the observation of detergent extracted parasites using FESEM associated to backscattered analysis of immunolabeled specimens represents a new approach for the study of parasite cytoskeletal elements and their protein associations.","ai_title_tag":"Enhanced FESEM Imaging of Protozoan Parasite Cytoskeletons","publication_date":"2005,,","publication_name":"Histochemistry and Cell Biology"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"high","language":"en","title":"Improvement on the visualization of cytoskeletal structures of protozoan parasites using high-resolution field emission scanning electron microscopy (FESEM","broadcastable":false,"draft":null,"has_indexable_attachment":true,"indexable":true}}["work"]; window.loswp.workCoauthors = [25093107]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "full_page_mobile_sutd_modal"; 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In addition, images obtained with the use of the high-resolution backscattered electrons (BSE) detector provided a powerful tool for immunocytochemical analysis of biological material. In this work, we show the contribution of the FESEM to the detailed description of cytoskeletal structures of the protozoan parasites Herpetomonas megaseliae, Trypanosoma brucei and Giardia lamblia. High-resolution images of detergent extracted H. megaseliae and T. brucei showed the profile of the cortical microtubules, also known as sub-pellicular microtubules (SPMT), and protein bridges cross-linking them. Also, it was possible to visualize fine details of the filaments that form the lattice-like structure of the paraflagellar rod (PFR) and its connection with the axoneme. In G. lamblia, it was possible to observe the intricate structure of the adhesive disk, funis (a microtubular array) and other cytoskeletal structures poorly described previously. Since most of the stable cytoskeletal structures of this protozoan rely on tubulin, we used the BSE images to accurately map immunolabeled tubulin in its cytoskeleton. Our results suggest that the observation of detergent extracted parasites using FESEM associated to backscattered analysis of immunolabeled specimens represents a new approach for the study of parasite cytoskeletal elements and their protein associations.</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":47468226,"attachmentType":"pdf","workUrl":"https://www.academia.edu/10250933/Improvement_on_the_visualization_of_cytoskeletal_structures_of_protozoan_parasites_using_high_resolution_field_emission_scanning_electron_microscopy_FESEM"}">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":47468226,"attachmentType":"pdf","workUrl":"https://www.academia.edu/10250933/Improvement_on_the_visualization_of_cytoskeletal_structures_of_protozoan_parasites_using_high_resolution_field_emission_scanning_electron_microscopy_FESEM"}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div></div><div data-auto_select="false" data-client_id="331998490334-rsn3chp12mbkiqhl6e7lu2q0mlbu0f1b" data-doc_id="47468226" data-landing_url="https://www.academia.edu/10250933/Improvement_on_the_visualization_of_cytoskeletal_structures_of_protozoan_parasites_using_high_resolution_field_emission_scanning_electron_microscopy_FESEM" data-login_uri="https://www.academia.edu/registrations/google_one_tap" data-moment_callback="onGoogleOneTapEvent" id="g_id_onload"></div><div class="ds-top-related-works--grid-container"><div class="ds-related-content--container ds-top-related-works--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="0" data-entity-id="18156024" 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/18156024/Subpellicular_microtubules_associate_with_an_intramembranous_particle_lattice_in_the_protozoan_parasite_Toxoplasma_gondii">Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii</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="38120897" href="https://independent.academia.edu/NaomiMorrissette">Naomi Morrissette</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of cell science, 1997</p><p class="ds-related-work--abstract ds2-5-body-sm">Application of Fourier analysis techniques to images of isolated, frozen-hydrated subpellicular microtubules from the protozoan parasite Toxoplasma gondii demonstrates a distinctive 32 nm periodicity along the length of the microtubules. A 32 nm longitudinal repeat is also observed in the double rows of intramembranous particles seen in freeze-fracture images of the parasite&#39;s pellicle; these rows are thought to overlie the subpellicular microtubules. Remarkably, the 32 nm intramembranous particle periodicity is carried over laterally to the single rows of particles that lie between the microtubule-associated double rows. This creates a two-dimensional particle lattice, with the second dimension at an angle of approximately 75 degrees to the longitudinal rows (depending on position along the length of the parasite). Drugs that disrupt known cytoskeletal components fail to destroy the integrity of the particle lattice. This intramembranous particle organization suggests the exist...</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":"Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii","attachmentId":42078223,"attachmentType":"pdf","work_url":"https://www.academia.edu/18156024/Subpellicular_microtubules_associate_with_an_intramembranous_particle_lattice_in_the_protozoan_parasite_Toxoplasma_gondii","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/18156024/Subpellicular_microtubules_associate_with_an_intramembranous_particle_lattice_in_the_protozoan_parasite_Toxoplasma_gondii"><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="74635916" 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/74635916/High_resolution_scanning_electron_microscopy_of_the_cytoskeleton_of_Tritrichomonas_foetus">High-resolution scanning electron microscopy of the cytoskeleton of Tritrichomonas foetus</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="212927311" href="https://independent.academia.edu/IvoneRosa3">Ivone Rosa</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Structural Biology, 2013</p><p class="ds-related-work--abstract ds2-5-body-sm">Tritrichomonas foetus is a pathogenic protozoan that causes bovine trichomoniasis. In addition to its importance in veterinary medicine, this parasite is also a good representative of one the earliest eukaryotic cells available for study. T. foetus contains organelles that are common to all eukaryotic cells as well as uncommon cell structures such as hydrogenosomes and a complex and elaborate cytoskeleton that constitutes the mastigont system. The mastigont system is mainly formed by several proteinaceous structures that are associated with basal bodies, the pelta-axostylar complex and the costa. Although the structural organization of trichomonad cytoskeletons has been analyzed using several techniques, observation using a new generation of scanning electron microscopes with a resolution of 0.8 nm has allowed more detailed visualization of the three-dimensional organization of the mastigont system. Moreover, this study revealed the presence of new structures, such as the costa accessory filament, and the presence of two groups of microtubules that form the pelta-axostylar system.</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":"High-resolution scanning electron microscopy of the cytoskeleton of Tritrichomonas foetus","attachmentId":82717848,"attachmentType":"pdf","work_url":"https://www.academia.edu/74635916/High_resolution_scanning_electron_microscopy_of_the_cytoskeleton_of_Tritrichomonas_foetus","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/74635916/High_resolution_scanning_electron_microscopy_of_the_cytoskeleton_of_Tritrichomonas_foetus"><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="23320900" 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/23320900/Cytochemical_techniques_and_energy_filtering_transmission_electron_microscopy_applied_to_the_study_of_parasitic_protozoa">Cytochemical techniques and energy-filtering transmission electron microscopy applied to the study of parasitic protozoa</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="32331583" href="https://independent.academia.edu/MarcosVannierSantos">Marcos Vannier-Santos</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biological Procedures Online, 2001</p><p class="ds-related-work--abstract ds2-5-body-sm">The study of parasitic protozoa plays a major role in cell biology, biochemistry and molecular biology. Numerous cytochemical techniques have been developed in order to unequivocally identify the nature of subcellular compartments. Enzyme and immuno-cytochemistry allow the detection of, respectively, enzymatic activity products and antigens in particular sites within the cell. Energy-filtering transmission electron microscopy permits the detection of specific elements within such compartments. These approaches are particularly useful for studies employing antimicrobial agents where cellular compartments may be destroyed or remarkably altered and thus hardly identified by standard methods of observation. In this regard cytochemical and spectroscopic techniques provide valuable data allowing the determination of the mechanisms of action of such compounds.</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":"Cytochemical techniques and energy-filtering transmission electron microscopy applied to the study of parasitic protozoa","attachmentId":43780340,"attachmentType":"pdf","work_url":"https://www.academia.edu/23320900/Cytochemical_techniques_and_energy_filtering_transmission_electron_microscopy_applied_to_the_study_of_parasitic_protozoa","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/23320900/Cytochemical_techniques_and_energy_filtering_transmission_electron_microscopy_applied_to_the_study_of_parasitic_protozoa"><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="116927342" 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/116927342/Visualization_of_the_cytostome_inTrypanosoma_cruziby_high_resolution_field_emission_scanning_electron_microscopy_using_secondary_and_backscattered_electron_imaging">Visualization of the cytostome inTrypanosoma cruziby high resolution field emission scanning electron microscopy using secondary and backscattered electron imaging</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">FEMS Microbiology Letters, 2005</p><p class="ds-related-work--abstract ds2-5-body-sm">High resolution scanning electron microscopy was used to analyze the surface of epimastigote, amastigote and trypomastigote forms of Trypanosoma cruzi. Significant differences were observed between these forms and in different areas of the same cell. The cytostome found in amastigote and epimastigote forms could be easily visualized in images, which resemble those obtained only using the freeze-fracture technique. In contrast to other areas of the cell surface, the region of the cytostome, localized close to the flagellar pocket, showed a rugous surface and an opening with a diameter of 90 nm. Gold-labeled concanavalin A binds to the whole cell surface. However, the extent of binding was much higher in the region of the cytostome. The results obtained show that high resolution scanning electron microscopy is a powerful technique for analyzing the surface of protozoa.</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":"Visualization of the cytostome inTrypanosoma cruziby high resolution field emission scanning electron microscopy using secondary and backscattered electron imaging","attachmentId":112921188,"attachmentType":"pdf","work_url":"https://www.academia.edu/116927342/Visualization_of_the_cytostome_inTrypanosoma_cruziby_high_resolution_field_emission_scanning_electron_microscopy_using_secondary_and_backscattered_electron_imaging","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/116927342/Visualization_of_the_cytostome_inTrypanosoma_cruziby_high_resolution_field_emission_scanning_electron_microscopy_using_secondary_and_backscattered_electron_imaging"><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="23156475" 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/23156475/Visualization_of_the_funis_of_Giardia_lamblia_by_high_resolution_field_emission_scanning_electron_microscopy_new_insights">Visualization of the funis of Giardia lamblia by high-resolution field emission scanning electron microscopy—new insights</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="32987749" href="https://independent.academia.edu/MarleneBenchimol">Marlene Benchimol</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Structural Biology, 2004</p><p class="ds-related-work--abstract ds2-5-body-sm">Giardia lamblia is a multiflagellar parasite and one of the earliest diverging eukaryotic cells. It possesses a cytoskeleton made of several microtubular structures-an adhesive disc, four pairs of flagella, median body, and funis. This protozoan displays different types of movements, including a lateral and dorso-ventral dislocation of its posterior region, which has not been completely elucidated. In the present study, high-resolution field emission scanning electron microscopy was used to analyze the funis structure of G. lamblia trophozoites. It was shown that the funis is made of short arrays of microtubules emanating from the axonemes of the caudal flagella, which are anchored to dense rods that run parallel to the posterior-lateral flagella. After emergence of the posteriorlateral flagella, funis microtubules are anchored to the epiplasm, a fibrous layer that underlies the portion of membrane that presents tail contractility. Based on these observations a model for the tail flexion of G. lamblia is proposed.</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":"Visualization of the funis of Giardia lamblia by high-resolution field emission scanning electron microscopy—new insights","attachmentId":43640923,"attachmentType":"pdf","work_url":"https://www.academia.edu/23156475/Visualization_of_the_funis_of_Giardia_lamblia_by_high_resolution_field_emission_scanning_electron_microscopy_new_insights","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/23156475/Visualization_of_the_funis_of_Giardia_lamblia_by_high_resolution_field_emission_scanning_electron_microscopy_new_insights"><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="18156019" 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/18156019/Cytoskeleton_of_Apicomplexan_Parasites">Cytoskeleton of Apicomplexan Parasites</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="38120897" href="https://independent.academia.edu/NaomiMorrissette">Naomi Morrissette</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Microbiology and Molecular Biology Reviews, 2002</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":"Cytoskeleton of Apicomplexan Parasites","attachmentId":39905180,"attachmentType":"pdf","work_url":"https://www.academia.edu/18156019/Cytoskeleton_of_Apicomplexan_Parasites","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/18156019/Cytoskeleton_of_Apicomplexan_Parasites"><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="106490000" 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/106490000/What_about_the_Cytoskeletal_and_Related_Proteins_of_Tapeworms_in_the_Host_s_Immune_Response_An_Integrative_Overview">What about the Cytoskeletal and Related Proteins of Tapeworms in the Host’s Immune Response? An Integrative Overview</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="36697270" href="https://independent.academia.edu/JulioCarrero1">Julio Carrero</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Pathogens</p><p class="ds-related-work--abstract ds2-5-body-sm">Recent advances have increased our understanding of the molecular machinery in the cytoskeleton of mammalian cells, in contrast to the case of tapeworm parasites, where cytoskeleton remains poorly characterized. The pertinence of a better knowledge of the tapeworm cytoskeleton is linked to the medical importance of these parasitic diseases in humans and animal stock. Moreover, its study could offer new possibilities for the development of more effective anti-parasitic drugs, as well as better strategies for their surveillance, prevention, and control. In the present review, we compile the results of recent experiments on the cytoskeleton of these parasites and analyze how these novel findings might trigger the development of new drugs or the redesign of those currently used in addition to supporting their use as biomarkers in cutting-edge diagnostic tests.</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":"What about the Cytoskeletal and Related Proteins of Tapeworms in the Host’s Immune Response? An Integrative Overview","attachmentId":105673337,"attachmentType":"pdf","work_url":"https://www.academia.edu/106490000/What_about_the_Cytoskeletal_and_Related_Proteins_of_Tapeworms_in_the_Host_s_Immune_Response_An_Integrative_Overview","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/106490000/What_about_the_Cytoskeletal_and_Related_Proteins_of_Tapeworms_in_the_Host_s_Immune_Response_An_Integrative_Overview"><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="21585528" 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/21585528/Characterization_of_Putative_Cytoskeletal_Proteins_from_a_Trypanosomatid_and_Their_Comparative_Binding_to_Microtubules_and_Soluble_Tubulin">Characterization of Putative Cytoskeletal Proteins from a Trypanosomatid and Their Comparative Binding to Microtubules and Soluble Tubulin</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="42618660" href="https://independent.academia.edu/SulieChang">Sulie Chang</a></div><p class="ds-related-work--metadata ds2-5-body-xs">2008</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":"Characterization of Putative Cytoskeletal Proteins from a Trypanosomatid and Their Comparative Binding to Microtubules and Soluble Tubulin","attachmentId":42136468,"attachmentType":"pdf","work_url":"https://www.academia.edu/21585528/Characterization_of_Putative_Cytoskeletal_Proteins_from_a_Trypanosomatid_and_Their_Comparative_Binding_to_Microtubules_and_Soluble_Tubulin","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/21585528/Characterization_of_Putative_Cytoskeletal_Proteins_from_a_Trypanosomatid_and_Their_Comparative_Binding_to_Microtubules_and_Soluble_Tubulin"><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="111238532" 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/111238532/Cellular_electron_tomography_of_the_apical_complex_in_the_apicomplexan_parasite_Eimeria_tenella_shows_a_highly_organised_gateway_for_regulated_secretion">Cellular electron tomography of the apical complex in the apicomplexan parasite Eimeria tenella shows a highly organised gateway for regulated secretion</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="37540157" href="https://independent.academia.edu/DavidFerguson25">David Ferguson</a></div><p class="ds-related-work--metadata ds2-5-body-xs">2021</p><p class="ds-related-work--abstract ds2-5-body-sm">The apical complex of apicomplexan parasites is essential for host cell invasion and intracellular survival and as the site of regulated exocytosis from specialised secretory organelles called rhoptries and micronemes. Despite its importance, there is little data on the three-dimensional organisation and quantification of these organelles within the apical complex or how they are trafficked to this specialised region of plasma membrane for exocytosis. In coccidian apicomplexans there is an additional tubulin-containing hollow barrel structure, the conoid, which provides a structural gateway for this specialised secretion. Using a combination of cellular electron tomography and serial block face-scanning electron microscopy (SBF-SEM) we have reconstructed the entire apical end of Eimeria tenella sporozoites. We discovered that conoid fibre number varied, but there was a fixed spacing between fibres, leading to conoids of different sizes. Associated apical structures varied in size to...</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":"Cellular electron tomography of the apical complex in the apicomplexan parasite Eimeria tenella shows a highly organised gateway for regulated secretion","attachmentId":108828957,"attachmentType":"pdf","work_url":"https://www.academia.edu/111238532/Cellular_electron_tomography_of_the_apical_complex_in_the_apicomplexan_parasite_Eimeria_tenella_shows_a_highly_organised_gateway_for_regulated_secretion","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/111238532/Cellular_electron_tomography_of_the_apical_complex_in_the_apicomplexan_parasite_Eimeria_tenella_shows_a_highly_organised_gateway_for_regulated_secretion"><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="26334023" 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/26334023/Analysis_of_microtubule_cytoskeleton_distribution_using_a_fluorescent_taxoid_in_two_trichomonadid_protozoa_Trichomonas_gallinae_and_Tritrichomonas_foetus">Analysis of microtubule cytoskeleton distribution using a fluorescent taxoid in two trichomonadid protozoa: Trichomonas gallinae and Tritrichomonas foetus</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="50258656" href="https://pucrs.academia.edu/AnneLarre">Anne Larre</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Experimental Parasitology, 2008</p><p class="ds-related-work--abstract ds2-5-body-sm">Trichomonas gallinae and Tritrichomonas foetus are flagellated parasitic protozoa of the upper digestive tract of birds and the urogenital tract of cattle, respectively. Both of these species are important in the veterinary field, due to the fact that they cause significant economic losses. Therefore, we investigated the morphology of these parasites by studying microtubule cytoskeleton organization. FLUTAX-2, an active fluorescent derivative of Taxol, was used in this study. This fluorescent taxoid binds to polymerized ab-tubulin dimers. Our results showed that FLUTAX-2 was able to bind to and stabilize microtubules of intact T. gallinae and T. foetus trophozoites, allowing the microtubular cytoskeleton to be easily observed by fluorescence microscopy. T. foetus and T. gallinae had no differences in their FLUTAX-2 binding profiles. Further studies may allow this technique to be improved, and it may possibly be used as a routine laboratory method for the diagnosis of avian and bovine trichomonosis.</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":"Analysis of microtubule cytoskeleton distribution using a fluorescent taxoid in two trichomonadid protozoa: Trichomonas gallinae and Tritrichomonas foetus","attachmentId":46644628,"attachmentType":"pdf","work_url":"https://www.academia.edu/26334023/Analysis_of_microtubule_cytoskeleton_distribution_using_a_fluorescent_taxoid_in_two_trichomonadid_protozoa_Trichomonas_gallinae_and_Tritrichomonas_foetus","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/26334023/Analysis_of_microtubule_cytoskeleton_distribution_using_a_fluorescent_taxoid_in_two_trichomonadid_protozoa_Trichomonas_gallinae_and_Tritrichomonas_foetus"><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":47468226,"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":47468226,"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_47468226" 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. You can download the paper by clicking the button above.</p></div></div></div></div><div class="ds-sidebar--container js-work-sidebar"><div class="ds-related-content--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="0" data-entity-id="8791252" 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/8791252/Novel_filamentous_bundles_in_the_cytoplasm_of_a_unicellular_eukaryote_Crithidia_fasciculata">Novel filamentous bundles in the cytoplasm of a unicellular eukaryote, Crithidia fasciculata</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="18998562" href="https://royalholloway.academia.edu/johnlagnado">john lagnado</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Protoplasma, 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style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="1" data-entity-id="112857285" 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/112857285/Immunocytochemical_differentiation_of_microtubules_in_the_cytoskeleton_of_Giardia_lamblia_using_monoclonal_antibodies_to_%CE%B1_tubulin_and_polyclonal_antibodies_to_associated_low_molecular_weight_proteins">Immunocytochemical differentiation of microtubules in the cytoskeleton of Giardia lamblia using monoclonal antibodies to α-tubulin and polyclonal antibodies to associated low molecular weight proteins</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="10721217" href="https://independent.academia.edu/richardcrossley">richard crossley</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Cell Science, 1986</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":"Immunocytochemical differentiation of microtubules in the cytoskeleton of Giardia lamblia using monoclonal antibodies to α-tubulin and polyclonal antibodies to associated low molecular weight proteins","attachmentId":109959757,"attachmentType":"pdf","work_url":"https://www.academia.edu/112857285/Immunocytochemical_differentiation_of_microtubules_in_the_cytoskeleton_of_Giardia_lamblia_using_monoclonal_antibodies_to_%CE%B1_tubulin_and_polyclonal_antibodies_to_associated_low_molecular_weight_proteins","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/112857285/Immunocytochemical_differentiation_of_microtubules_in_the_cytoskeleton_of_Giardia_lamblia_using_monoclonal_antibodies_to_%CE%B1_tubulin_and_polyclonal_antibodies_to_associated_low_molecular_weight_proteins"><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-related-work-sidebar-card" data-collection-position="2" data-entity-id="97977789" 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/97977789/Characterization_of_proteins_from_the_cytoskeleton_of_Giardia_lamblia">Characterization of proteins from the cytoskeleton of Giardia lamblia</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="10721217" href="https://independent.academia.edu/richardcrossley">richard crossley</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Cell Science, 1983</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":"Characterization of proteins from the cytoskeleton of Giardia lamblia","attachmentId":99454402,"attachmentType":"pdf","work_url":"https://www.academia.edu/97977789/Characterization_of_proteins_from_the_cytoskeleton_of_Giardia_lamblia","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" 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Cell, 1996</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 deep-etch study of the cytoskeleton of Giardia duodenalis","attachmentId":43239696,"attachmentType":"pdf","work_url":"https://www.academia.edu/15386567/A_deep_etch_study_of_the_cytoskeleton_of_Giardia_duodenalis","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/15386567/A_deep_etch_study_of_the_cytoskeleton_of_Giardia_duodenalis"><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-related-work-sidebar-card" data-collection-position="4" data-entity-id="18993487" 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/18993487/Novel_Thioredoxin_Like_Proteins_Are_Components_of_a_Protein_Complex_Coating_the_Cortical_Microtubules_of_Toxoplasma_gondii">Novel Thioredoxin-Like Proteins Are Components of a Protein Complex Coating the Cortical Microtubules of Toxoplasma gondii</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="39141737" href="https://independent.academia.edu/WetzelLaura">Laura Wetzel</a><span>, </span><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="39488344" href="https://independent.academia.edu/KHu2">K. Hu</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Eukaryotic Cell, 2013</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":"Novel Thioredoxin-Like Proteins Are Components of a Protein Complex Coating the Cortical Microtubules of Toxoplasma gondii","attachmentId":40371163,"attachmentType":"pdf","work_url":"https://www.academia.edu/18993487/Novel_Thioredoxin_Like_Proteins_Are_Components_of_a_Protein_Complex_Coating_the_Cortical_Microtubules_of_Toxoplasma_gondii","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" 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class="ds-related-work--metadata ds2-5-body-xs">Cell Host & Microbe, 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":"Role of the Parasite and Host Cytoskeleton in Apicomplexa Parasitism","attachmentId":46006158,"attachmentType":"pdf","work_url":"https://www.academia.edu/12688159/Role_of_the_Parasite_and_Host_Cytoskeleton_in_Apicomplexa_Parasitism","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/12688159/Role_of_the_Parasite_and_Host_Cytoskeleton_in_Apicomplexa_Parasitism"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" 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ds2-5-body-link" data-author-id="37778346" href="https://independent.academia.edu/ArturoGonz%C3%A1lezrobles">Arturo González-robles</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Parasitology Research, 2007</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":"Ultrastructure of cyst differentiation in parasitic protozoa","attachmentId":44675298,"attachmentType":"pdf","work_url":"https://www.academia.edu/14039521/Ultrastructure_of_cyst_differentiation_in_parasitic_protozoa","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" 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js-related-work-sidebar-card" data-collection-position="8" data-entity-id="43237007" 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/43237007/Extracellular_Vesicles_from_Parasitic_Helminths_Contain_Specific_Excretory_Secretory_Proteins_and_Are_Internalized_in_Intestinal_Host_Cells">Extracellular Vesicles from Parasitic Helminths Contain Specific Excretory/Secretory Proteins and Are Internalized in Intestinal Host Cells</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="159932579" href="https://independent.academia.edu/dfdfdfdfd24">dfdf dfdfd</a></div><p class="ds-related-work--metadata ds2-5-body-xs">PLoS ONE, 2012</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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