New Insights on Cytoskeleton Proteins in Protozoan Parasites

Topic Information

Dear Colleagues,

In most unicellular parasites, as in other eukaryotic cells, the cytoskeleton forms a complex and dynamic network composed of actin filaments, microtubules and intermediate filaments. These different components work together to contribute to a multitude of cellular functions including maintenance of shape, integrity and internal organization, scaffold for the development of the progenies and cytokinesis, mechanical support for cell motility (gliding, cilia and flagella beating), endocytosis, exocytosis and internal transport.

The cell cytoskeleton is therefore at the centre of cell biology and this is particularly true in unicellular parasites that adapt to different environments during their life cycle and often differentiate from one stage to another with profound changes of their cytoskeleton. While molecular motors (myosins, dyneins and kinesins) are directly involved in directed movement important for intracellular transport, contraction and cell motility, other cytoskeletal and cytoskeleton-associated proteins regulate the assembly/disassembly of the networks and form parasite-specific essential structures.

Reviews and original research manuscripts on new insights on cytoskeleton and cytoskeleton-associated proteins in protozoan parasites will be considered. The objective of this Special Issue is to expand the knowledge on the cytoskeleton composition, biogenesis and function in protozoan parasites with an emphasis on their specificities.

Dr. Mélanie Bonhivers
Dr. Karine Frenal
Topic Editors

Keywords

Participating Journals

Journal Name	Impact Factor	CiteScore	Launched Year	First Decision (median)	APC
Microorganisms microorganisms	4.5	6.4	2013	15.1 Days	CHF 2700
International Journal of Molecular Sciences ijms	5.6	7.8	2000	16.3 Days	CHF 2900

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Published Papers (4 papers)

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All Microorganisms IJMS

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Open AccessArticle

The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network

by Luis Vigetti, Tatiana Labouré, Chloé Roumégous, Dominique Cannella, Bastien Touquet, Claudine Mayer, Yohann Couté, Karine Frénal, Isabelle Tardieux and Patricia Renesto

Int. J. Mol. Sci. 2022, 23(11), 5995; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23115995 - 26 May 2022

Cited by 3 | Viewed by 2161

Abstract

T. gondii is a eukaryotic parasite that has evolved a stage called tachyzoite which multiplies in host cells by producing two daughter cells internally. These nascent tachyzoites bud off their mother and repeat the division process until the expanding progenies escape to settle [...] Read more.

T. gondii is a eukaryotic parasite that has evolved a stage called tachyzoite which multiplies in host cells by producing two daughter cells internally. These nascent tachyzoites bud off their mother and repeat the division process until the expanding progenies escape to settle and multiply in other host cells. Over these intra- and extra-cellular phases, the tachyzoite maintains an essential apicobasal polarity that emerges through a unique bidirectional budding process of the elongating cells. This process requires the assembly of several molecular complexes that, at the nascent pole, encompass structural and myosin motor elements. To characterize a recently identified basal pole marker named BCC7 with respect to the posterior myosin J and myosin C motors, we used conventional biochemistry as well as advanced proteomic and in silico analysis in conjunction with live and super resolution microscopy of transgenic fluorescent tachyzoites. We document that BCC7 forms a ribbed ring below which myosin C motor entities distribute regularly. In addition, we identified—among 13 BCC7 putative partners—two novel and five known members of the inner membrane complex (IMC) family which ends at the apical side of the ring. Therefore, BCC7 could assist the stabilization of the IMC plaques and contribute to the parasite biomechanical properties. Full article

(This article belongs to the Topic New Insights on Cytoskeleton Proteins in Protozoan Parasites)

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24 pages, 5276 KiB  

Open AccessArticle

Bhalin, an Essential Cytoskeleton-Associated Protein of Trypanosoma brucei Linking TbBILBO1 of the Flagellar Pocket Collar with the Hook Complex

by Christine E. Broster Reix, Célia Florimond, Anne Cayrel, Amélie Mailhé, Corentin Agnero-Rigot, Nicolas Landrein, Denis Dacheux, Katharina Havlicek, Mélanie Bonhivers, Brooke Morriswood and Derrick R. Robinson

Microorganisms 2021, 9(11), 2334; https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms9112334 - 11 Nov 2021

Cited by 4 | Viewed by 2084

Abstract

Background: In most trypanosomes, endo and exocytosis only occur at a unique organelle called the flagellar pocket (FP) and the flagellum exits the cell via the FP. Investigations of essential cytoskeleton-associated structures located at this site have revealed a number of essential proteins. [...] Read more.

Background: In most trypanosomes, endo and exocytosis only occur at a unique organelle called the flagellar pocket (FP) and the flagellum exits the cell via the FP. Investigations of essential cytoskeleton-associated structures located at this site have revealed a number of essential proteins. The protein TbBILBO1 is located at the neck of the FP in a structure called the flagellar pocket collar (FPC) and is essential for biogenesis of the FPC and parasite survival. TbMORN1 is a protein that is present on a closely linked structure called the hook complex (HC) and is located anterior to and overlapping the collar. TbMORN1 is essential in the bloodstream form of T. brucei. We now describe the location and function of BHALIN, an essential, new FPC-HC protein. Methodology/Principal Findings: Here, we show that a newly characterised protein, BHALIN (BILBO1 Hook Associated LINker protein), is localised to both the FPC and HC and has a TbBILBO1 binding domain, which was confirmed in vitro. Knockdown of BHALIN by RNAi in the bloodstream form parasites led to cell death, indicating an essential role in cell viability. Conclusions/Significance: Our results demonstrate the essential role of a newly characterised hook complex protein, BHALIN, that influences flagellar pocket organisation and function in bloodstream form T. brucei parasites. Full article

(This article belongs to the Topic New Insights on Cytoskeleton Proteins in Protozoan Parasites)

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17 pages, 2911 KiB  

Open AccessArticle

Novel Cytoskeleton-Associated Proteins in Trypanosoma brucei Are Essential for Cell Morphogenesis and Cytokinesis

by Marina Schock, Steffen Schmidt and Klaus Ersfeld

Microorganisms 2021, 9(11), 2234; https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms9112234 - 27 Oct 2021

Cited by 4 | Viewed by 1918

Abstract

Trypanosome brucei, the causative agent of African sleeping sickness, harbours a highly ordered, subpellicular microtubule cytoskeleton that defines many aspects of morphology, motility and virulence. This array of microtubules is associated with a large number of proteins involved in its regulation. Employing [...] Read more.

Trypanosome brucei, the causative agent of African sleeping sickness, harbours a highly ordered, subpellicular microtubule cytoskeleton that defines many aspects of morphology, motility and virulence. This array of microtubules is associated with a large number of proteins involved in its regulation. Employing proximity-dependent biotinylation assay (BioID) using the well characterised cytoskeleton-associated protein CAP5.5 as a probe, we identified CAP50 (Tb927.11.2610). This protein colocalises with the subpellicular cytoskeleton microtubules but not with the flagellum. Depletion by RNAi results in defects in cytokinesis, morphology and partial disorganisation of microtubule arrays. Published proteomics data indicate a possible association of CAP50 with two other, yet uncharacterised, cytoskeletal proteins, CAP52 (Tb927.6.5070) and CAP42 (Tb927.4.1300), which were therefore included in our analysis. We show that their depletion causes phenotypes similar to those described for CAP50 and that they are essential for cellular integrity. Full article

(This article belongs to the Topic New Insights on Cytoskeleton Proteins in Protozoan Parasites)

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15 pages, 4295 KiB  

Open AccessArticle

Unique Tubulin-Based Structures in the Zoonotic Apicomplexan Parasite Cryptosporidium parvum

by Chenchen Wang, Dongqiang Wang, Jiawen Nie, Xin Gao, Jigang Yin and Guan Zhu

Microorganisms 2021, 9(9), 1921; https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms9091921 - 10 Sep 2021

Cited by 6 | Viewed by 2130

Abstract

Cryptosporidium parasites are known to be highly divergent from other apicomplexan species at evolutionary and biological levels. Here we provide evidence showing that the zoonotic Cryptosporidium parvum also differs from other apicomplexans, such as Toxoplasma gondii, by possessing only two tubulin-based filamentous [...] Read more.

Cryptosporidium parasites are known to be highly divergent from other apicomplexan species at evolutionary and biological levels. Here we provide evidence showing that the zoonotic Cryptosporidium parvum also differs from other apicomplexans, such as Toxoplasma gondii, by possessing only two tubulin-based filamentous structures, rather than an array of subpellicular microtubules. Using an affinity-purified polyclonal antibody against C. parvum β-tubulin (CpTubB), we observed a long and a short microtubule that are rigid and stable in the sporozoites and restructured during the intracellular parasite development. In asexual development (merogony), the two restructuring microtubules are present in pairs (one pair per nucleus or merozoites). In sexual developmental stages, tubulin-based structures are detectable only in microgametes, but undetectable in macrogametes. These observations indicate that C. parvum parasites use unique microtubule structures that differ from other apicomplexans as part of their cytoskeletal elements. Full article

(This article belongs to the Topic New Insights on Cytoskeleton Proteins in Protozoan Parasites)

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