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  • 1
    Online Resource
    Online Resource
    Cham : Springer
    Keywords: Cytology ; Evolution (Biology) ; Eukaryotic Microbiology ; Microbiology ; Biochemistry ; Evolutionary biology. ; Cell biology. ; Mitochondria ; Organelles
    Description / Table of Contents: Chapter 1: Introduction -- Chapter 2: The evolution of oxygen independent energy metabolism in eukaryotes with hydrogenosomes and mitosomes -- Chapter 3: Protein Import into Hydrogenosomes and Mitosomes -- Chapter 4: Structure of the Hydrogenosome -- Chapter 5: Hydrogenosomes of Anaerobic Ciliates -- Chapter 6: Metabolism of Trichomonad Hydrogenosomes -- Chapter 7: Hydrogenosomes of Anaerobic Fungi: an Alternative Way to Adapt to Anaerobic Environments -- Chapter 8: The proteome of T. vaginalis hydrogenosomes -- Chapter 9: Mitosomes in parasitic protists -- Chapter 10: The Mitochondrion-Related Organelles of Crypto-sporidium species -- Chapter 11: The Mitochondrion-Related Organelles of Blastocystis -- Chapter 12: Mitochondrion-related organelles in free-living protists -- Chapter 13: Protists without mitochondria, how it may happen?
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource (VIII, 326 p. 52 illus., 17 illus. in color)
    Edition: 2nd ed. 2019
    ISBN: 9783030179410
    Series Statement: Microbiology Monographs 9
    Language: English
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  • 2
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Cell organelles. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (298 pages)
    Edition: 1st ed.
    ISBN: 9783540767336
    Series Statement: Microbiology Monographs ; v.9
    DDC: 571.6
    Language: English
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  • 3
    Online Resource
    Online Resource
    Cham :Springer International Publishing AG,
    Keywords: Mitochondria. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (332 pages)
    Edition: 2nd ed.
    ISBN: 9783030179410
    Series Statement: Microbiology Monographs ; v.9
    Language: English
    Note: Intro -- Preface -- Contents -- The Hydrogenosome Is Born: In Memoriam Donald G. Lindmark -- References -- The Evolution of Oxygen-Independent Energy Metabolism in Eukaryotes with Hydrogenosomes and Mitosomes -- 1 Introduction -- 2 Motivation and a Thirteenfold Insight About O2 -- 3 Older Views of How and Why the Mitochondrion Become Established -- 4 Anoxic and Sulfidic Oceans up to ~450 Million Years Ago -- 5 Anoxic Oceans Give Anaerobic Eukaryotes Room to Breathe -- 6 Conclusion -- References -- Protein Import into Hydrogenosomes and Mitosomes -- 1 Introduction -- 2 Protein Trafficking in Eukaryotes -- 2.1 The Nucleus -- 2.2 The Endoplasmic Reticulum -- 2.3 The Mitochondrion -- 3 The Evolution of the Mitochondrial Protein Import Machinery -- 4 Studying Hydrogenosomal and Mitosomal Protein Import -- 4.1 Laboratory Techniques and Tools -- 4.2 Mining Genome Sequence Data -- 5 Organellar Targeting Signals -- 5.1 Mitochondrial Targeting Signals -- 5.2 Signals on Precursors of Soluble Hydrogenosomal and Mitosomal Proteins -- 5.2.1 Trichomonas Hydrogenosomes -- 5.2.2 Neocallimastix Hydrogenosomes -- 5.2.3 Cryptosporidium Mitosomes -- 5.2.4 Entamoeba Mitosomes -- 5.2.5 Giardia Mitosomes -- 5.2.6 Microsporidia Mitosomes -- 5.3 Signals on Hydrogenosomal and Mitosomal Membrane Proteins -- 6 Crossing the Organellar Membranes -- 6.1 The Outer Membrane -- 6.1.1 Translocase of the Outer Membrane (TOM Complex) -- 6.1.2 Sorting and Assembling β-Barrel Proteins: The SAM Complex -- 6.2 The Intermembrane Space Chaperones -- 6.3 The Inner Membrane -- 6.3.1 The TIM22 Complex -- 6.3.2 The TIM23 Complex -- 7 The Protein Import Motor -- 8 Preprotein Processing Peptidases -- 8.1 The Mitochondrial Processing Peptidase (MPP) -- 8.2 The Inner Membrane Protease -- 9 Folding Newly Imported Soluble Proteins -- 10 Perspectives -- References -- Structure of the Hydrogenosome. , 1 Introduction -- 2 Where Are Hydrogenosomes Found? -- 3 The Hydrogenosome Shape -- 4 Hydrogenosome Size -- 5 Hydrogenosome Components -- 5.1 The Hydrogenosomes Envelope -- 5.2 The Peripheral Vesicle -- 5.3 The Matrix of the Hydrogenosome -- 6 Fungal Hydrogenosomes -- 7 Proximity with Other Cellular Structures -- 7.1 Hydrogenosomes and Endoplasmic Reticulum -- 8 Hydrogenosome Autophagy -- 9 Hydrogenosome Division -- 10 Hydrogenosome Behavior in the Cell Cycle -- 11 Hydrogenosomes Connection to Microtubules -- 12 Immunolabeling -- References -- Hydrogenosomes of Anaerobic Ciliates -- 1 Introduction -- 2 Nyctotherus ovalis -- 2.1 The Energy Metabolism of N. ovalis -- 2.2 In Silico Reconstruction of the Basal Hydrogenosomal Metabolism of N. ovalis -- 3 The Hydrogenosomes of Other Ciliates -- 4 Can the Methanogenic Symbionts Tell Us More About the Origin and Function of Ciliate Hydrogenosomes -- 5 Evolutionary Aspects -- References -- Metabolism of Trichomonad Hydrogenosomes -- 1 Introduction -- 2 The Hydrogenosomal Membrane -- 3 Energy Metabolism -- 4 Proteins of the Core Catabolic Pathway -- 4.1 Pyruvate:Ferredoxin Oxidoreductase -- 4.2 Ferredoxin -- 4.3 Hydrogenase -- 4.4 Malic Enzyme -- 4.5 NADH Dehydrogenase -- 4.6 Succinyl-CoA:Acetate CoA Transferase -- 4.7 Succinyl-CoA Synthetase -- 4.8 Adenylate Kinase -- 5 Interaction with Oxygen and Reactive Oxygen Species -- 6 Iron-Sulfur Cluster Assembly Machinery -- 7 Amino Acid and Polyamine Metabolism -- 7.1 Serine Hydroxymethyltransferase and the Case of Glycine Decarboxylase Complex -- 7.2 Polyamine Metabolism -- 8 Concluding Remarks -- References -- Hydrogenosomes of Anaerobic Fungi: An Alternative Way to Adapt to Anaerobic Environments -- 1 Introduction -- 2 Mitochondria Versus Hydrogenosomes -- 3 Anaerobic Fungi Possess Hydrogenosomes and Perform a (Bacterial-Type) Mixed Acid Fermentation. , 4 Hydrogenosomal Metabolism of Piromyces and Neocallimastix -- 5 The Role of the Hydrogenosomes in the Energy Metabolism of Piromyces sp. E2 -- 6 The Mitochondrial Origin of the Hydrogenosomes in Anaerobic Fungi -- References -- The Proteome of T. vaginalis Hydrogenosomes -- 1 Introduction -- 2 Experimental Procedures -- 3 In Silico Predictions -- 4 The Proteome of Trichomonas vaginalis Hydrogenosomes -- 4.1 Energy Metabolism -- 4.2 Iron-Sulfur Cluster Assembly -- 4.3 Reactive Oxygen Species Defense -- 4.4 Amino Acid Metabolism -- 4.5 Protein Import -- 4.6 Carriers of the Hydrogenosomal Inner Membrane -- 4.7 C-Tail-Anchored Proteins -- 4.8 Contaminants or Surface-Associated Proteins? -- 5 Quantitative Analysis of the Proteome: Iron-Induced Changes -- 6 The Proteome of Pentatrichomonas hominis Hydrogenosome -- 7 Concluding Remarks -- References -- Mitosomes in Parasitic Protists -- 1 Introduction -- 2 Discovery of Mitosomes -- 3 Morphology -- 4 Biogenesis -- 4.1 The Genome -- 4.2 Protein Targeting, Translocation, and Maturation -- 4.3 Replication -- 4.3.1 Division -- 4.3.2 Segregation -- 5 Physiological Functions -- 5.1 Iron-Sulfur Cluster Assembly Machinery -- 5.1.1 The Mitochondrial Model -- 5.1.2 The Role of Mitochondria in the Maturation of Extramitochondrial Fe-S Proteins -- 5.1.3 Fe-S Cluster Assembly in Mitosomes -- Giardia intestinalis and Other Diplomonads -- Microsporidia -- Cryptosporidium spp. -- Mikrocytos mackini -- Entamoeba histolytica and Related Organisms -- 5.2 Requirements for ATP, Membrane Potential and Electron Transport -- 5.3 Sulfate Activation and Other Mitosomal Functions -- 6 Perspectives -- References -- The Mitochondrion-Related Organelles of Cryptosporidium Species -- 1 Introduction -- 2 Ultrastructure Morphology -- 2.1 Intracellular Location -- 2.2 Subcellular (Internal) Organization -- 2.3 Variations in Cristae. , 3 Mitochondrial Cell Biology -- 3.1 Association of the Mitochondrion with the RER -- 3.2 Iron-Sulphur Cluster (ISC) Biosynthesis -- 3.3 Mitochondrial Protein Import -- 4 Carbohydrate Metabolism -- 4.1 Pyruvate:NADP+ Oxidoreductase (PNO) -- 4.2 Predicted End Products of Glycolysis -- 5 Energy Metabolism -- 6 The Crystalloid Body -- 6.1 Ultrastructural Morphology -- 6.2 Putative Functions -- 7 Diversity of Mitochondria Within the Clade -- 8 Concluding Remarks and Future Perspectives -- References -- The Mitochondrion-Related Organelles of Blastocystis -- 1 Introduction -- 2 Blastocystis Genome, Adaptations and Lateral Gene Transfer -- 3 Blastocystis Mitochondrial DNA -- 4 Cell Biology and Functions -- 4.1 Adaptations to Oxygen -- 4.2 Fe-S Cluster Assembly Biosynthesis -- 4.3 Mitochondrial Protein Import -- 4.4 Glycolysis -- 5 Energy Metabolism: Biochemistry -- 6 Morphology -- 7 Role of Blastocystis Mitochondria in Cell Death -- 8 Concluding Remarks and Future Perspectives -- References -- Mitochondrion-Related Organelles in Free-Living Protists -- 1 Introduction -- 2 Fornicata -- 2.1 Iron-Sulfur Cluster Assembly -- 2.2 Pyruvate Metabolism and Energy Generation -- 2.3 Protein Import -- 2.4 Glycine Cleavage System -- 2.5 Hydrogen Production Coupled with GCS -- 2.6 Overall Characteristics and Evolution of MROs in Ancestrally Free-Living Fornicata -- 3 Trepomonas sp. -- 4 Other Taxa -- 4.1 Jakobida -- 4.2 Heterolobosea -- 4.3 Stramenopila -- 4.4 Rhizaria -- 4.5 Alveolata -- 4.6 Breviatea -- 4.7 Amoebozoa -- 5 Conclusions -- References -- Organisms Without Mitochondria, How It May Happen? -- 1 Mitochondria in Anaerobes Are Reduced but Typically Not Lost -- 2 Oxymonads: Protists Without Mitochondria -- 3 Prerequisites and Consequences of Mitochondrial Loss -- 4 Why Should We Be Interested in Amitochondriate Protists? -- References -- Index.
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  • 4
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Ferredoxin, Fd, is often deficient in metronidazole-resistant strains of Trichomonas vaginalis and is thought to be necessary for drug activation. To directly test whether Fd is essential for metronidazole susceptibility, gene replacement technology has been developed for T. vaginalis. The selectable marker gene neomycin phosphotransferase (NEO) flanked by ∼2.6 and ∼2.0 kBp of the Fd 5′ and 3′ flanking regions (pKO-FD-NEO) was introduced into cells on linear DNA and selected for NEO gene expression. Stable transformants were shown to contain the NEO gene in the Fd locus and to have completely lost the Fd gene. Northern and immunoblot analyses confirm the loss of Fd mRNA and protein in pKO-FD-NEO cells. Analyses of the activity of hydrogenosomal proteins in Fd KO cells show a fourfold increase in hydrogenase activity and a 95% decrease in pyruvate/ferredoxin oxidoreductase (PFO) activity. In contrast, PFO and hydrogenase mRNA levels are unchanged. Surprisingly, Fd KO cells are not resistant to metronidazole under aerobic or anaerobic conditions. These cells are capable of producing molecular hydrogen, albeit at 50% the level of the parental strain, demonstrating that the Fd gene product eliminated in KO cells is neither necessary for hydrogen production nor metronidazole activation. Together these data indicate the presence of unidentified Fds or flavodoxins capable of drug activation or an unidentified mechanism that does not require either PFO or Fd for metronidazole activation.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Giardia intestinalis (syn. lamblia) is one of the most widespread intestinal protozoan pathogens worldwide, causing hundreds of thousands of cases of diarrhoea each year. Giardia is a member of the diplomonads, often described as an ancient protist group whose primitive nature is suggested by ...
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Hydrogenosomes are double-membraned ATP-producing and hydrogen-producing organelles of diverse anaerobic eukaryotes. In some versions of endosymbiotic theory they are suggested to be homologues of mitochondria, but alternative views suggest they arose from an anaerobic bacterium that was ...
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . A number of reports suggest that the sexually transmitted pathogen of cattle, Tritrichomonas foetus, and a gastrointestinal commensal of pigs, Tritrichomonas suis, are very similar and may be co-specific. A conclusive review of the taxonomic and nomenclatural status of these species has not been presented so far. Toward this end, we reexamined and compared porcine and bovine trichomonads with regard to their morphology, pathogenic potential, and DNA polymorphism. Using light and electron microscopy, no distinguishing features between T. foetus and T. suis strains were found in size, general morphology, and karyomastigont structure. Both bovine and porcine trichomonads showed pathogenic potential in the subcutaneous mouse assays and did not separate into distinct groups according to strain virulence. Three DNA fingerprinting methods (i.e. RFLP, RAPD, and PCR-based analysis of variable-length DNA repeats) that produce species-specific DNA fragment patterns did not distinguish between the bovine and porcine strains. Sequencing of a variable 502-bp DNA fragment as well as comparison of 16S rRNA gene sequences did not reveal species-specific differences between the cattle and porcine strains. Therefore, we conclude that T. foetus and T. suis belong to the same species. To prevent confusion that may arise from T. foetus-T. suis synonymy, we propose to suppress the older name suis and maintain its accustomed junior synonym foetus as a nomen protection for both cattle and porcine trichomonads. The case has been submitted to the International Commision on Zoological Nomenclature for ruling under its plenary power.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 44 (1997), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . The random amplified polymorphic DNA (RAPD) technique was used for phylogenetic analysis of trichomonads, for intraspecies genealogical study of Trichomonas vaginalis strains, and for assessment of intrastrain polymorphism in Trichomonas vaginalis. The phylogenetic tree for 12 trichomonad species showed certain discrepancies with current models of trichomonad evolution. However, it shows that RAPD traits retain phylogenetically relevant information. The results of intraspecies analyses of 18 Trichomonas vaginalis strains suggested some concordance between the genetic relationship of strains and their geographic origin. They also suggested a concordance between the strain genetic relationships and the resistance to metronidazole. A concordance was also found with respect to the severity of disease observed in donor patients but not with the results of laboratory virulence assays. No concordance was found between genetic relationship of strains and strain infection with a dsRNA Trichomonas vaginalis virus (TVV). The latter suggests that TVV might be transmitted horizontally among Trichomonas vaginalis populations. The identity of RAPD patterns of clones isolated from in vitro cultures and those of the cultures reisolated independently from the same patient within a period of six weeks suggests that individual Trichomonas vaginalis strains are not polymorphic and that the RAPD patterns are stable. Therefore, the RAPD technique seems useful for addressing various clinically relevant issues.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 40 (1993), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Resitance to metronidazole detectable under anaerobic conditions was induced in two Trichomonas vaginalis strains (TV 10-02 and MRP-2) by cultivation at gradually increasing pressure of the drug (1-100 μ/ml) for 12 to 21 months. the resistant derivatives reproduced in anaerobic trypticase-yeast-extract-maltose medium at 100 μ/ml metronidazole and showed very high values of minimal lethal concentration for metronidazole in anaerobic in vitro assays (556-1,600 μ/ml at 48-h exposure to the drug). Stepwise selection was necessary to develop the resistance in either strain. Attempts to induce resistance by prolonged maintenance of trichomonads with constant, low or moderate drug concentrations (3-10 μ/ml) were unsuccessful. Freshly developed resistance to high concentrations of metronidazole was unstable in absence of drug pressure as well as after cryopreservation. Development of stable resistance required further cultivation at 100 μ/ml metronidazole. Unstable substrains did not revert to original susceptibility. They retained a moderate level of resistance, being able to grow at 10 μ/ml metronidazole. the strains with fully developed resistance had no activity of the hydrogenosomal enzymes pyruvate: ferredoxin oxidoreductase and hydrogenase and ceased uptake of [14C]-metronidazole. These findings indicate that the pyruvate oxidizing pathway responsible for metronidazole activation was inactivated and metabolism of the drug stopped.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Parasitology research 85 (1999), S. 692-699 
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The ability of a microbial invader to acquire iron from its vertebrate host has been recognized as an important virulence mechanism in some pathogenic bacteria. We examined the involvement of similar mechanisms in an experimental infection of mice by a protozoan pathogen of cattle, Tritrichomonasfoetus. In a series of experiments, outbred ICR mice were inoculated intraperitoneally with two strains of T. foetus, the moderately virulent KV-1 (∼5% mortality rate) and the highly virulent LUB-1MIP (∼80% mortality rate). Treatment of mice with ferric ammonium citrate (FeAC) (100 mg/kg per day intraperitoneally) increased the mortality rate caused by the KV-1 infection up to the level determined for the highly virulent strain. The treatment effect was dose dependent and required early administration of FeAC after inoculation of parasites and its continued supply for at least 3 subsequent days. Daily sampling of peritoneal exudate showed that the infection-enhancing effect of iron overload was associated with a stimulation of parasite multiplication, which in the case of KV-1 infection was strongly suppressed in untreated mice. Consistent with these findings, the strain of lower virulence (KV-1) showed considerably lower efficiency accumulating radiolabeled iron from transferrin and a low-molecular source [Fe(III)nitrilotriacetic acid] in vitro. The results indicate an involvement of iron uptake mechanisms by the parasite as a virulence factor in T. foetus infection.
    Type of Medium: Electronic Resource
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