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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 47 (2000), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Anti-centrin monoclonal antibodies 20H5 and 11B2 produced against Chlamydomonas centrin decorated the group of basal bodies as well as very closely attached structures in all trichomonads studied and in the devescovinids Foaina and Devescovina. Moreover, these antibodies decorated the undulating membrane in Trichomonas vaginalis, Trichomitus batrachorum, and Tritrichomonas foetus, and the cresta in Foaina. Centrin was not demonstrated in the dividing spindle and paradesmosis. Immunogold labeling, both in pre- and post-embedding, confirmed that centrin is associated with the basal body cylinder and is a component of the nine anchoring arms between the terminal plate of flagellar bases and the plasma-membrane. Centrin is also associated with the hook-shaped fibers attached to basal bodies (F1, F3), the X-fiber, and along sigmoid fibers (F2) at the pelta-axostyle junction, which is the microtubule organizing center for pelta-axostyle microtubules. There was no labeling on the striated costa and parabasal fibers nor on microtubular pelta-axostyle, but the fibrous structure inside the undulating membrane was labeled in T. vaginalis. Two proteins of 22–20 kDa corresponding to the centrin molecular mass were recognized by immunoblotting using these antibodies in the three trichomonad species examined.By screening a T. vaginalis cDNA library with 20H5 antibody, two genes encoding identical protein sequences were found. The sequence comprises the 4 typical EF-hand Ca++ -binding domains present in every known centrin. Trichomonad centrin is closer to the green algal cluster (70% identity) than to the yeast Cdc31 cluster (55% identity) or the Alveolata cluster (46% identity).
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 153 (1997), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The parasitic protozoan Trichomonas vaginalis is known to contain the ubiquitous and highly conserved protein actin. A genomic library and a cDNA library have been screened to identify and clone the actin gene(s) of T. vaginalis. The nucleotide sequence of one gene and its flanking regions have been determined. The open reading frame encodes a protein of 376 amino acids. The sequence is not interrupted by any introns and the promoter could be represented by a 10 bp motif close to a consensus motif also found upstream of most sequenced T. vaginalis genes. The five different clones isolated from the cDNA library have similar sequences and encode three actin proteins differing only by one or two amino acids. A phylogenetic analysis of 31 actin sequences by distance matrix and parsimony methods, using centractin as outgroup, gives congruent trees with Parabasala branching above Diplomonadida.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1615-6102
    Keywords: Amphiesma ; Ecdysis ; Euglena acus ; Glenodinium foliaceum ; Pellicle ; Thecal development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ultrastructure and development of the amphiesma of the dinoflagellateGlenodinium foliaceum was studied using conventional electron microscopy and immunocytochemistry. Ecdysis (shedding of the flagella, the outer two membranes of the cell, and the thecal plates) was induced by centrifugation. The cells were resuspended and the thickening of the pellicle and the development of the new thecal vesicles and plates was studied over a 9 h period. After ecdysis, the thin pellicle which underlay the thecal plates in the motile cells thickens to form a complex structure of four distinct layers: an outer layer of randomly oriented fibrils, a 50 nm layer of fibrils oriented perpendicular to the dense layer, the dense layer which has a trilaminate structure, and a wide inner homogeneous layer. The new thecal vesicles form in these pelliculate cells by the migration of electron translucent amphisomal vesicles over the layer of peripheral microtubules to a position directly under the plasmalemma. The thecal vesicles then flatten and elongate. A discontinuous pellicular layer appears within them. Subsequently, the thecal vesicles widen and are filled with a fibrillogranular substance overlying the pelliculate layer. The thecal plates form on top of this fibrillogranular material. By this time, most cells have escaped from the pellicle and are motile. At first, the outer thecal vesicle membrane is continuous with the inner thecal vesicle membrane at the sutures, but when this connection is broken, the dense pelliculate layers become continuous across the suture as does the inner thecal vesicle membrane. At ecdysis, this membrane becomes the new plasmalemma of the cell. Cells at each stage of pellicle thickening and thecal development were labelled with a polydonal antiserum raised against the 70 kDa epiplasmic protein ofEuglena acus. This antiserum labelled both the thecal plates of the motile cells and the inner homogeneous layer of the pellicle of ecdysed non-motile cells. No other amphiesmal structure was labelled, nor was any intracellular compartment.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Parasitology research 86 (2000), S. 30-35 
    ISSN: 1432-1955
    Keywords: Key words Malic enzyme ; Succinyl-CoA synthetase ; Adhesin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Three monoclonal antibodies specific for malic enzyme and for the α- and β- subunits, respectively, of the succinyl-coenzyme A (CoA) synthetase of Trichomonas vaginalis were used to immunolocalize these proteins in the cell. All antibodies labeled the hydrogenosome matrix as determined both by immunofluorescence and by immunogold staining. There was no labeling on the cell surface or in any other cell compartment. These results support the idea that these proteins are restricted to a hydrogenosomal function and do not play a role as adhesins at the plasma membrane surface.
    Type of Medium: Electronic Resource
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