Localization by Indirect Immunofluorescence of Tetrin, Actin, and Centrin to the Oral Apparatus and Buccal Cavity of the Macrostomal Form of <i>Tetrahymena vorax</i>

McLaughlin, Neil; Buhse, Howard E.

doi:10.1111/j.1550-7408.2004.tb00556.x

Cited by 5 publications

(7 citation statements)

References 32 publications

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“…Centrin is universally found in basal bodies and centrosomes but its localization to additional structures is not unusual. For example, in T. thermophila, centrin localizes to the oral crescent that lines the cystosome, in Trypanosoma brucei centrin 2 localizes to an additional bi-lobed structure near the Golgi apparatus, and Paramecium centrin localizes to the infraciliary lattice (Madeddu et al, 1996; Moudjou et al, 1996; McLaughlin and Buhse, 2004; He et al, 2005), suggesting that centrin may have species-specific functions.…”

Section: Resultsmentioning

confidence: 99%

Mining the Giardia genome and proteome for conserved and unique basal body proteins

Lauwaet

Smith

Reiner

et al. 2011

International Journal for Parasitology

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Giardia lamblia is a flagellated protozoan parasite and a major cause of diarrhea in humans. Its microtubular cytoskeleton mediates trophozoite motility, attachment and cytokinesis, and is characterized by an attachment disk and eight flagella that are each nucleated in a basal body. To date, only 10 giardial basal body proteins have been identified, including universal signaling proteins that are important for regulating mitosis or differentiation. In this study, we have exploited bioinformatics and proteomic approaches to identify new Giardia basal body proteins and confocal microscopy to confirm their localization in interphase trophozoites. This approach identified 75 homologs of conserved basal body proteins in the genome including 65 not previously known to be associated with Giardia basal bodies. Thirteen proteins were confirmed to co-localize with centrin to the Giardia basal bodies. We also demonstrate that most basal body proteins localize to additional cytoskeletal structures in interphase trophozoites. This might help to explain the roles of the four pairs of flagella and Giardia-specific organelles in motility and differentiation. A deeper understanding of the composition of the Giardia basal bodies will contribute insights into the complex signaling pathways that regulate its unique cytoskeleton and the biological divergence of these conserved organelles.

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Section: Resultsmentioning

confidence: 99%

Mining the Giardia genome and proteome for conserved and unique basal body proteins

Lauwaet

Smith

Reiner

et al. 2011

International Journal for Parasitology

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“…The residual structures we see may represent one of these proteins performing this linking role. Kloetzel and Horich (unpubl. data) support one such possibility: the reaction of the perikinetosomal sheaths in our THS preparations with monoclonal antibody 20H5 (Baron et al 1992) by immunoEM indicates that they contain the contractile, calcium-binding protein centrin (see also Guerra et al 2003;Lemullois et al 2004;McLaughlin and Buhse 2004;Pearson and Winey 2009).…”

mentioning

confidence: 56%

“…Thus, the current available evidence indicates that cagein is a novel protein, adding to the extensive cortical protein collection previously identified in ciliates, such as centrins (Lemullois et al. ; McLaughlin and Buhse ), tetrins (Brimmer and Weber ; Honts and Williams ), epiplasmins (Damaj et al. ; Pomol et al.…”

Section: Discussionmentioning

confidence: 85%

“…Other cytoskeletal proteins identified as important elements of the ciliate pellicle do not have the distribution, molecular masses nor immunolocalizations matching those of cagein. Thus, the current available evidence indicates that cagein is a novel protein, adding to the extensive cortical protein collection previously identified in ciliates, such as centrins (Lemullois et al 2004;McLaughlin and Buhse 2004), tetrins (Brimmer and Weber 2000;Honts and Williams 1990), epiplasmins (Damaj et al 2009;Pomol et al 2006), articulins (Huttenlauch et al 1998), alveolins (Gould et al 2008), and the Tetrahymena epiplasmic proteins (Bouchard et al 2001;Williams 2004). Certainly, many of the crucial components of the ciliate pellicle remain as yet undescribed.…”

Section: Kloetzel and Brann-basal-body Cages In Euplotesmentioning

confidence: 90%

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Structure and Protein Composition of a Basal‐Body Scaffold (“Cage”) in the Hypotrich Ciliate Euplotes

Kloetzel

Brann

2012

J Eukaryotic Microbiology

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Cilia on the ventral surface of the hypotrich ciliate Euplotes are clustered into polykinetids or compound ciliary organelles, such as cirri or oral membranelles, used in locomotion and prey capture. A single polykinetid may contain more than 150 individual cilia; these emerge from basal bodies held in a closely spaced array within a scaffold or framework structure that has been referred to as a basal-body "cage". Cage structures were isolated free of cilia and basal bodies; the predominant component of such cages was found on polyacrylamide gels to be a 45-kDa polypeptide. Antisera were raised against this protein band and used for immunolocalizations at the light and electron microscope levels. Indirect immunofluorescence revealed the 45-kDa polypeptide to be localized exclusively to the bases of the ventral polykinetids. Immunogold staining of thin sections of intact cells further localized this reactivity to filaments of a double-layered dense lattice that appears to link adjoining basal bodies into ordered arrays within each polykinetid. Scanning electron microscopy of isolated cages reveals the lower or "basal" cage layer to be a fine lacey meshwork supporting the basal bodies at their proximal ends; adjoining basal bodies are held at their characteristic spacing by filaments of an upper or "medial" cage layer. The isolated cage thus resembles a miniature test-tube rack, able to accommodate varying arrangements of basal-body rows, depending on the particular type of polykinetid. Because of its clear and specific localization to the basal-body cages in Euplotes, we have termed this novel 45-kDa protein "cagein".

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“…This technique provides a rational basis on which the morphologists can make conclusions about different cell components. This approach can be extended by the simple general-biological interpolations to the Protozoa morphology not only because immunofluorescence staining methods are applicable for protistological / protozoological studies from 1960 till now (Zaman, 1965;Zaman, 1966;Dzbenski, 1966;Hauser, 1980;Kovac, 1980;Ohba, 1986;Brugerolle, 1988;Olins, 1989;Allen, 1990;Turkewitz, 1992;Dohra, 1994;Hanyu, 1995;Hanyu, 1996;Clerot, 2001;Santangelo, 2001;Strzyzewska-Jówko, 2003;McLaughlin, 2004;Itabashi, 2004;Kissmehl, 2004;Ramoino, 2004), but also because the simplest inorganic staining agents may be used for visualization of several compartments and constituents of the Protozoa cells (even without the antibodyome agents (Mohebbi, 2009;Zhu, 2013)). Notwithstanding, there is no case of determination of the different "omics" characteristics using inorganic dyes.…”

Section: Requirements On the Protistological "Omics"mentioning

confidence: 99%

Is it possible to consider «kinetomics» and «argyromics» as novel trends of functional morphology and systems biology of parasitic and nonparasitic protozoa? a brief analytical review

Градов¹

2016

Journal of Biomedical Technologies

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Abstract. This paper considers argyrophilic (i.e. stained by the silver nitrate) fibrils visualized by the well-known Klein method and later called neuroformative system of Protozoa, or neuroformium. Klein described the excitation wave propagation and coordination of the cilia moving by this network, as well as the main role in localization of the peristomes and the ciliar apparatus on the topographic microanatomy map of Protozoa before and after the cell division. However, in early 1930-th the advanced staining techniques revealed two components in the above mentioned fibrill network with the similar morphobiochemical parameters (within the limits of the silver nitrate staining selectivity), one of which provides the mechanical stabilization of the Protozoa body (a number of Paramecium species were found to possess even a third selectivelystained fiber system). This resulted in the introduction of the term "argyrome" by Chatton in 1936 for the complex of the argentophilic fibrils and a term "cinetome" for the subpellicular infraciliature. It is therefore more appropriate to speak about "kinetomics" and "argyromics" rather than of a single "omics" for all the intracellular networks of Protozoa. We consider the principles of introduction of the novel "-omics" in modern science and from the above standpoint discuss whether it is possible to consider "kinetomics" and "argyromics" as the novel trends of functional morphology and systems biology of Protozoa.

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Localization by Indirect Immunofluorescence of Tetrin, Actin, and Centrin to the Oral Apparatus and Buccal Cavity of the Macrostomal Form of Tetrahymena vorax

Cited by 5 publications

References 32 publications

Mining the Giardia genome and proteome for conserved and unique basal body proteins

Mining the Giardia genome and proteome for conserved and unique basal body proteins

Structure and Protein Composition of a Basal‐Body Scaffold (“Cage”) in the Hypotrich Ciliate Euplotes

Is it possible to consider «kinetomics» and «argyromics» as novel trends of functional morphology and systems biology of parasitic and nonparasitic protozoa? a brief analytical review

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