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Fig. 7 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 7. (A, B) The distribution of α-tubulin in the cell after rapid axopodial contraction. (A) Low-magnification images of the cell after the induction of rapid axopodial contraction. A projection image of the whole cell constructed from 87 optical sections taken at a 0.5 µm interval (left) and the corresponding light micrograph (right). (B) High-magnification images of the same cell shown in (A). A projection image of the equatorial plane of the cell body constructed from 5 optical sections taken at a 0.5 µm interval (left), and the corresponding light micrograph (right). Note that the positive signals in the distal parts of the axopodia have a branched appearance (arrowheads). Scale bars: 20 μm (A), 10 μm (B).

Fig. 4 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 4. (A–D) Evaluation of the maintenance of the original lengths of axopodia in R. contractilis using different combinations of fixative and buffer. Cells were fixed with (A) 4% paraformaldehyde in phosphate buffer, (B) 4% paraformaldehyde in PHEM, (C) 0.2% glutaraldehyde in phosphate buffer, or (D) 0.2% glutaraldehyde in PHEM. Note that only fixation with 0.2% glutaraldehyde in PHEM maintained the axopodial length. Scale bar: 20 µm.

Fig. 1 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 1. (A, B) Rapid axopodial contraction induced by mechanical stimulation in R. contractilis. Images (A) before and (B) after rapid axopodial contraction. Arrowheads indicate kinetocysts. Note the synchronized retraction of all axopodia and the apparent increases in the widths of contracted axopodia relative to the features observed before the onset of axopodial contraction (an arrow). Scale bar: 20 µm (A, B).

Fig. 6 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 6. Confocal analysis of α-tubulin-immunolabeled extended axopodia. Fine reconstructed projection image from 161 optical sections taken at a 0.05 µm (top) and the corresponding light micrograph (bottom). Note the regions of relatively low fluorescence (arrowheads) did not correspond to the location of kinetocysts (arrows). Scale bar: 10 μm.

Fig. 5 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 5. (A, B) The distribution of α-tubulin in the cell before rapid axopodial contraction. (A) Low-magnification images of a cell without the induction of rapid axopodial contraction. A projection image of the whole cell was constructed from 192 optical sections obtained at 0.5 µm intervals (left); the corresponding light micrograph is also shown (right). (B) High-magnification images of the same cell shown in (A). A projection image of the equatorial plane of the cell body constructed from 5 optical sections taken at 0.5 µm intervals, and the corresponding light micrograph. The asterisk indicates a centroplast. Note that positive signals were detected along the fully extended axopodia. Scale bars: 20 μm (A), 10 μm (B).

Fig. 3 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 3. Schematic illustration of the experimental setup. The fixative is injected into the cell suspension via a micro flow-through chamber with a syringe pump. Next, the cells are fixed by injecting the fixative at a rate below the threshold required for inducing rapid contraction. The cells are then observed under a microscope.

Fig. 2 in Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis

Fig. 2. (A, B) Fine structures associated with axopodial microtubules. (A) Centroplast in the center of the cell. (B) Cross-section of an axopodium in the peripheral region of the cell. Note that bundles of microtubules radiate from the centroplast (arrowheads) and that the axopodium comprises six microtubules. Scale bars: 500 nm (A), 100 nm (B).

Figure 2 in Recombinant - and -tubulin from Echinococcus granulosus: expression, purification and polymerization

Figure 2. Sequence alignment of Echinococcus granulosus α9-tubulin and corresponding sequences from humans and parasites. The symbol ''*'' denotes the positions of amino acids that have a single, fully conserved amino acid residue; the symbol '':'' denotes conservation between groups of amino acids with strongly similar properties; the symbol ''.'' denotes conservation between groups of amino acids with weakly similar properties; and the symbol ''–'' denotes gaps inserted to maximize sequence alignment. EgA9, E. granulosus α9; HuA6, human alpha 6 (119578461); HmA5, H. microstoma alpha 5 (674586714); HcA, H. contortus alpha tubulin (159155); SjA1, S. japonicum alpha 1–3 (226478902); and TgA, T. gondii alpha (161937).

Figure 1 in Recombinant - and -tubulin from Echinococcus granulosus: expression, purification and polymerization

Figure 1. The cloning and expression of α9- and β4-tubulin. (a) The expression of α9- and β4-tubulin in E. coli BL21 (DE3). M: standard protein molecular weight marker, lane 1: negative control without induction, lane 2: induced control, lane 3: the supernatant after sonication, lane 4: the pellet after sonication, and lane 5: purified recombinant tubulin. (b) Western blot analysis. M: standard protein molecular weight marker, lane 1: α-tubulin, lane 2: β-tubulin.

Figure 3 in Recombinant - and -tubulin from Echinococcus granulosus: expression, purification and polymerization

Figure 3. The sequence alignment of Echinococcus granulosus β4-tubulin and corresponding sequences from humans and parasites. Symbol meanings are as in Figure 2. EgB4, E. granulosus β4-tubulin; EmB1, E. multilocularis Tub-1 gene (7838198); EmB2, E. multilocularis Tub-2 gene (7838200); EmB3, E. multilocularis Tub-3 gene (7838202); HuB3, human B3 (50592996); HuB4, human B4a (574584803); HmB2C, H. microstoma beta 2C (674589300); HcB1, H. contortus beta tubulin isotype 1 (124244617); SjB2, S. japonicum beta 2 (226467271); PfB, P. falciparum beta (160732).

Figure 5 in Recombinant - and -tubulin from Echinococcus granulosus: expression, purification and polymerization

Figure 5. The polymerization of Echinococcus granulosus α9- and β4-tubulin. (a) Spectrophotometric analysis of polymerization of E. granulosus α9- and β4-tubulin at different concentrations. (b) Confocal scanning laser micrographs of the polymerization product of recombinant tubulin showing immune reactivity to anti-α-tubulin/Alexa-Fluor 488 antibody and anti-β-tubulin/Alexa-Fluor 647 antibody. (I): Phase contrast view, (II): α-tubulin immuno-reactivity, (III): β-tubulin immune-reactivity. (c) The microtubule-like structure resulting from polymerization of pure expressed α9- and β4-tubulin under appropriate conditions in vitro.

Figure 4 in Recombinant - and -tubulin from Echinococcus granulosus: expression, purification and polymerization

Figure 4. Modelled structure of the polymerized Echinococcus granulosus α9- and β4-tubulin dimer based on PDB ID 4f6r.

Fig. 5 in Cortical Localization of α- and γ-Tubulin and the Assembly of Cortical Microtubule Cytoskeleton in Hypotrichous Ciliate Euplotes eurystomus

Fig. 5. (A–D) Projections of the optical sections passing through the ventral surface of E. eurystomus cells in mitotic phase decorated with FLUTAX. Scale: 20 μm. (A) The AZM primordium appeared at the bottom-left of old AZM in the early stage of morphogenesis. (AZMP: adoral zone of membranelles primordium; UMP: undulating membrane primordium; arrow shows the UMP originated from the right side of AZMP). (B) The pattern of FVTC primordia was 3-3-3-2-2 from left to right, shown in a box (FVTCP: frontal–ventral–transverse cirri primordium; arrows show the blastema of ALM and PLM originating from the base of FVTCPs). (C) The AZM and UM of proter inherited the olds (white arrow), and those of opisthe were generated from the AZMP (black arrows show the primordium of the left marginal cirri). (D) Some old ciliary organelles still existed until the separation of the proter and opisthe (white arrows show the neonatal ALM and PLM; black arrows show the residual ALM; some old cirri are shown in the circle).

Fig. 3 in Cortical Localization of α- and γ-Tubulin and the Assembly of Cortical Microtubule Cytoskeleton in Hypotrichous Ciliate Euplotes eurystomus

Fig. 3. (A–C) Projection of optical section passing through the ventral surface of E. eurystomus cells decorated with the FLUTAX. Scale: 20 μm. (A) All the ventral ciliary organelles, and especially their base-associated microtubules, were strongly and clearly stained by FLUTAX (ALM: anterior longitudinal microtubules; PLM: posterior longitudinal microtubules; TM: transverse microtubules; PM: peripheral microtubules). (B) The microtubules associated with the adoral ciliary organelles were also marked by FLUTAX (SMB: small membranelle bracket; hollow arrow shows the microtubule fasolculus extending from the base of SMB; white arrow shows the microtubules in the adoral rib; black arrow shows the UM ciliary base–associated microtubules). (C) The FLUTAX decorated the short microtubular bundles between the bases of TCs (arrow).

Fig. 4 in Cortical Localization of α- and γ-Tubulin and the Assembly of Cortical Microtubule Cytoskeleton in Hypotrichous Ciliate Euplotes eurystomus

Fig. 4. (A–D) Projections of the optical sections passing through the dorsal cortex of E. eurystomus cells decorated with FLUTAX. Scale: 20 μm. (A) The leptos microtubular nets covered the dorsal cortex (arrow). (B) The longitudinal microtubules in the dorsal cortex (arrow). (C) The oblique microtubules in the dorsal cortex (arrow). (D) The dargyrome was faintly stained by the FLUTAX.

Fig. 1 in Cortical Localization of α- and γ-Tubulin and the Assembly of Cortical Microtubule Cytoskeleton in Hypotrichous Ciliate Euplotes eurystomus

Fig. 1. The permutation pattern of ciliary organelles in the ventral and dorsal of E. eurystomus cells (A, B). (A) The ventral ciliary pattern of E.eurystomus, (B) the dorsal ciliary pattern of E.eurystomus. (AZM: adoral zone of membranelles, OC: oral cirri; UM: undulating membranes, FVC: frontal–ventral cirri, TC: transverse cirri, CC: caudal cirri, LMC: left marginal cirri DK: dorsal kineties).

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Figure 1 in Phylogenetic analyses suggest that Psammomitra (Ciliophora, Urostylida) should represent an urostylid family, based on small subunit rRNA and alpha-tubulin gene sequence information

Figure 1. Morphology and infraciliature of Psammomitra retractilis (F–J, from Song & Warren, 1996). A, B, F, individuals in extended states to show the typical body shapes. Arrowheads in (A) mark the long, dominant membranelles. C, lateral view of a contracted specimen. D, posterior part, to demonstrate the long dorsal cilia. E, anterior part. Arrowheads indicate the long membranelles, whereas arrows mark the dorsal cilia. G, H, dorsal and lateral views of contracted cells. I, J, ventral and dorsal views to show the infraciliature and macronuclear nodules. Scale bars: A, C, D, F = 40 Mm; E = 30 Mm.

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Figure 3 in Phylogenetic analyses suggest that Psammomitra (Ciliophora, Urostylida) should represent an urostylid family, based on small subunit rRNA and alpha-tubulin gene sequence information

Figure 3. Maximum parsimony phylogeny of small subunit rRNA genes. Psammomitra is highlighted in black, and holostichids are enclosed in rectangles. Thick branches and arrows denote position of investigated species. Numbers on branches are values generated from 1000 bootstrap replicates.