The Expression and Distribution of Dense Granule Proteins in the Enteric (Coccidian) Forms ofToxoplasma gondiiin the Small Intestine of the Cat

Ferguson, David J. P.; Cesbron-Delauw, M.-F.; Dubremetz, Jean François; Sibley, L. David; Joiner, Keith A.; Wright, Steve

doi:10.1006/expr.1998.4384

Cited by 60 publications

(41 citation statements)

References 28 publications

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“…Localization of RON4 to the Rhoptry Necks by Immunoelectron Microscopy-Lung and peritoneal exudate from T. gondii acutely infected mice containing tachyzoites and brain from chronically infected mice containing bradyzoites were processed for immunoelectron microscopy as described previously (32). Thin sections were cut and mounted on Formvar-coated nickel grids.…”

Section: Methodsmentioning

confidence: 99%

Proteomic Analysis of Rhoptry Organelles Reveals Many Novel Constituents for Host-Parasite Interactions in Toxoplasma gondii

Bradley

Ward

Cheng

et al. 2005

Journal of Biological Chemistry

349

346

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Rhoptries are specialized secretory organelles that are uniquely present within protozoan parasites of the phylum Apicomplexa. These obligate intracellular parasites comprise some of the most important parasites of humans and animals, including the causative agents of malaria (Plasmodium spp.) and chicken coccidiosis (Eimeria spp.). The contents of the rhoptries are released into the nascent parasitophorous vacuole during invasion into the host cell, and the resulting proteins often represent the literal interface between host and pathogen. We have developed a method for highly efficient purification of rhoptries from one of the best studied Apicomplexa, Toxoplasma gondii, and we carried out a detailed proteomic analysis using mass spectrometry that has identified 38 novel proteins. To confirm their rhoptry origin, antibodies were raised to synthetic peptides and/or recombinant protein. Eleven of 12 of these yielded antibody that showed strong rhoptry staining by immunofluorescence within the rhoptry necks and/or their bulbous base. Hemagglutinin epitope tagging confirmed one additional novel protein as from the rhoptry bulb. Previously identified rhoptry proteins from Toxoplasma and Plasmodium were unique to one or the other organism, but our elucidation of the Toxoplasma rhoptry proteome revealed homologues that are common to both. This study also identified the first Toxoplasma genes encoding rhoptry neck proteins, which we named RONs, demonstrated that toxofilin and Rab11 are rhoptry proteins, and identified novel kinases, phosphatases, and proteases that are likely to play a key role in the ability of the parasite to invade and co-opt the host cell for its own survival and growth.

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Section: Methodsmentioning

confidence: 99%

Proteomic Analysis of Rhoptry Organelles Reveals Many Novel Constituents for Host-Parasite Interactions in Toxoplasma gondii

Bradley

Ward

Cheng

et al. 2005

Journal of Biological Chemistry

349

346

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“…(i) T. gondii. The coccidian stages of T. gondii were examined in the small intestines of cats as described previously (9).…”

Section: Methodsmentioning

confidence: 99%

MORN1 Has a Conserved Role in Asexual and Sexual Development across the Apicomplexa

et al. 2008

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The gene encoding the membrane occupation and recognition nexus protein MORN1 is conserved across the Apicomplexa. In Toxoplasma gondii, MORN1 is associated with the spindle poles, the anterior and posterior rings of the inner membrane complex (IMC). The present study examines the localization of MORN1 during the coccidian development of T. gondii and three Eimeria species (in the definitive host) and erythrocytic schizogony of Plasmodium falciparum. During asexual proliferation, MORN1 is associated with the posterior ring of the IMCs of the multiple daughters forming during T. gondii endopolygeny and schizogony in Eimeria and P. falciparum. Furthermore, the expression of P. falciparum MORN1 protein peaked in late schizogony. These data fit a model with a conserved role for MORN1 during IMC assembly in all variations of asexual development. An important new observation is the reactivity of MORN1 antibody with certain sexual stages in T. gondii and Eimeria species. Here MORN1 is organized as a ring-like structure where the microgametes bud from the microgametocyte while in mature microgametes it is present near the flagellar basal bodies and mitochondrion. These observations suggest a conserved role for MORN1 in both asexual and sexual development across the Apicomplexa.

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“…After washing samples were rapidly dehydrated in ethanol, embedded in LR White resin and processed. 19 Sections were placed on grids, incubated with NA24 (undiluted) or Clone 376 (1:80), and a secondary antibody (10nm gold particles), counterstained and examined in a Joel 1200EX transmission electron microscope (Joel UK Ltd, Welwyn Garden City, UK) at 80 kV.…”

Section: Immunoelectron Microscopymentioning

confidence: 99%

Can cytoplasmic nucleophosmin be detected by immunocytochemical staining of cell smears in acute myeloid leukemia?

et al. 2009

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IntroductionApproximately one-third of cases of de novo acute myeloid leukemia (AML) carry mutations in the C-terminal region of the nucleophosmin (NPM1) gene.1-2 AML with mutated NPM1 shows distinctive biological and clinical features, including female gender, monocytoid morphology, CD34-negativity and a unique gene expression profile.3 These features are irrespective of whether NPM1-mutated AML carries a normal karyotype (about 85% of cases) or secondary chromosomal aberrations (about 15%), thus reinforcing the view that NPM1 mutation is a founder genetic lesion. 4 In the absence of FLT3-ITD mutations, AML with a normal karyotype and NPM1 mutation confers a significantly better prognosis than other AML cases with a normal karyotype.5-8 A recent study indicates that these prognostic considerations also apply to NPM1-mutated AML patients carrying secondary chromosomal aberrations.4 Frame-shift NPM1 mutations create a new leucine-rich sequence at the protein's C-terminus which serves as a nuclear export signal. This, accompanied by loss of tryptophan residues, is responsible for the increased nuclear export and aberrant cytoplasmic accumulation of the NPM1 leukemic mutants. 9NPM1 mutations were initially detected following the observation that in B5-fixed/EDTA decalcified bone marrow trephine (BMT) biopsies, NPM protein was aberrantly expressed in the cytoplasm of leukemic cells of about onethird of AML patients.1 This anomalous staining pattern is closely correlated with the presence of mutated NPM1.9 As BMT biopsies are not always performed at diagnosis of AML, the ability to detect cNPM on cell smears would be advantageous. We have established a technique to assess NPM expression in routine hematologic smear samples and assessed its correlation with NPM1 mutation status. Design and Methods SamplesCell lines FL18 and L428 were cultured with recommended media and OCI-AML3 (DSMZ, Braunschweig, Germany) as described else-

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The Expression and Distribution of Dense Granule Proteins in the Enteric (Coccidian) Forms ofToxoplasma gondiiin the Small Intestine of the Cat

Cited by 60 publications

References 28 publications

Proteomic Analysis of Rhoptry Organelles Reveals Many Novel Constituents for Host-Parasite Interactions in Toxoplasma gondii

Proteomic Analysis of Rhoptry Organelles Reveals Many Novel Constituents for Host-Parasite Interactions in Toxoplasma gondii

MORN1 Has a Conserved Role in Asexual and Sexual Development across the Apicomplexa

Can cytoplasmic nucleophosmin be detected by immunocytochemical staining of cell smears in acute myeloid leukemia?

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