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8. Construction of scFv Antibodies against the Outer Loops of the Microsporidium Nosema bombycis ATP/ADP-Transporters and Selection of the Fragment Efficiently Inhibiting Parasite Growth

Author

Dolgikh, Viacheslav V., primary, Senderskiy, Igor V., additional, Timofeev, Sergej A., additional, Zhuravlyov, Vladimir S., additional, Dolgikh, Alexandra V., additional, Seliverstova, Elena V., additional, Ismatullaeva, Diloram A., additional, and Mirzakhodjaev, Bakhtiyar A., additional

Published
2022
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15. Efficacy of a Plant-Microbe System: Pisum sativum (L.) Cadmium-Tolerant Mutant and Rhizobium leguminosarum Strains, Expressing Pea Metallothionein Genes PsMT1 and PsMT2, for Cadmium Phytoremediation

Author

Tsyganov, Viktor E., primary, Tsyganova, Anna V., additional, Gorshkov, Artemii P., additional, Seliverstova, Elena V., additional, Kim, Viktoria E., additional, Chizhevskaya, Elena P., additional, Belimov, Andrey A., additional, Serova, Tatiana A., additional, Ivanova, Kira A., additional, Kulaeva, Olga A., additional, Kusakin, Pyotr G., additional, Kitaeva, Anna B., additional, and Tikhonovich, Igor A., additional

Published
2020
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16. Protein Reabsorption in The Amphibian Kidney : Comparative and Evolutionary Aspects

Author

Seliverstova, Elena V.

Subjects
Science / Life Sciences / Microbiology
Abstract

Protein reabsorption in the renal proximal tubule (PT) is a vitally important process which prevents the loss of filtered proteins and provides their participation in subsequent metabolism. Despite considerable changes in renal structure and function in the process of evolution, very little is known about the functional similarities or specifics of tubular protein reabsorption in the kidney of lower vertebrates compared with the mammalian and human kidney. This article presents an overview of our recent studies on protein reabsorption in the kidney of amphibians, which are used as one of the main animal models for current biological and biomedical research. In frogs, newts, and rats, the absorption capacity of epithelial PT cells was studied after the introduction of green fluorescent protein (GFP), yellow fluorescent protein (YFP), and lysozyme. Molecular mechanisms of receptor-mediated protein endocytosis were also investigated by immunohisto- and immunocytochemistry, electron, fluorescent, and laser scanning confocal microscopy.

Published
2018

18. Evolutionary Physiology and Biochemistry - Advances and Perspectives

Author

Knyazev, Alexander N., primary, Avrova, Natalia F., additional, Vlasova, Yulia A., additional, Alekseeva, Olga Sergeevna, additional, Krivchenko, Alexander Ivanovich, additional, Demchenko, Ivan Timofeyevich, additional, Belekhova, Margarita G., additional, Kenigfest, Natalia B., additional, Belostotskaya, Galina B., additional, Golovanova, Tatyana A., additional, Nerubatskaya, Irina V., additional, Galagudza, Michael M., additional, Shpakov, Alexander O., additional, Derkach, Kira Viktorovna, additional, (Tsaparina), Diana M. Guillemard, additional, Tsitseroshin, Michail N., additional, Shepovalnikov, Alexandr N., additional, Galperina, Elizaveta I., additional, Panasevich, Ekaterina A., additional, Kats, Ekaterina E., additional, Zaytseva, Larisa G., additional, Kruchinina, Olga V., additional, Kuznetsov, Sergey Vladimirovich, additional, Vdovichenko, Natalia D., additional, Dmitrieva, Ludmila E., additional, Kuznetsova, Natalia N., additional, Sizonov, Vladimir A., additional, Terpilowski, Maksim A., additional, Timofeeva, Olga P., additional, Levchenko, Vladimir F., additional, Kazansky, Alexander B., additional, Sabirov, Marat A., additional, Savostyanov, Gennady A., additional, Seliverstova, Elena V., additional, Prutskova, Natalya P., additional, Shpakov, Alexander Olegovich, additional, Spirov, Alexander V., additional, Holloway, David M., additional, Tikhonov, Denis B., additional, Zhorov, Boris S., additional, Zhuravin, Igor А., additional, Dubrovskaya, Nadezhda M., additional, Tumanova, Natalia L., additional, Vasilev, Dmitrii S., additional, Nalivaeva, Natalia N., additional, and Orbeli, Leon A., additional

Published
2018
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25. Analogs of the Golgi complex in microsporidia: structure and avesicular mechanisms of function

Author

Beznoussenko, Galina V., primary, Dolgikh, Viacheslav V., additional, Seliverstova, Elena V., additional, Semenov, Petr B., additional, Tokarev, Yuri S., additional, Trucco, Alvar, additional, Micaroni, Massimo, additional, Di Giandomenico, Daniele, additional, Auinger, Peter, additional, Senderskiy, Igor V., additional, Skarlato, Sergei O., additional, Snigirevskaya, Ekaterina S., additional, Komissarchik, Yan Yu., additional, Pavelka, Margit, additional, De Matteis, Maria A., additional, Luini, Alberto, additional, Sokolova, Yuliya Ya., additional, and Mironov, Alexander A., additional

Published
2007
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26. Secretion of Antonospora (Paranosema) locustae Proteins into Infected Cells Suggests an Active Role of Microsporidia in the Control of Host Programs and Metabolic Processes.

Author

Senderskiy, Igor V., Timofeev, Sergey A., Seliverstova, Elena V., Pavlova, Olga A., and Dolgikh, Viacheslav V.

Subjects
PROTEIN synthesis, INTRACELLULAR pathogens, PROTOZOAN diseases, MICROSPORIDIA, HOST-parasite relationships, METABOLIC regulation, WESTERN immunoblotting
Abstract

Molecular tools of the intracellular protozoan pathogens Apicomplexa and Kinetoplastida for manipulation of host cell machinery have been the focus of investigation for approximately two decades. Microsporidia, fungi-related microorganisms forming another large group of obligate intracellular parasites, are characterized by development in direct contact with host cytoplasm (the majority of species), strong minimization of cell machinery, and acquisition of unique transporters to exploit host metabolic system. All the aforementioned features are suggestive of the ability of microsporidia to modify host metabolic and regulatory pathways. Seven proteins of the microsporidium Antonospora (Paranosema) locustae with predicted signal peptides but without transmembrane domains were overexpressed in Escherichia coli. Western-blot analysis with antibodies against recombinant products showed secretion of parasite proteins from different functional categories into the infected host cell. Secretion of parasite hexokinase and α/β-hydrolase was confirmed by immunofluorescence microscopy. In addition, this method showed specific accumulation of A. locustae hexokinase in host nuclei. Expression of hexokinase, trehalase, and two leucine-rich repeat proteins without any exogenous signal peptide led to their secretion in the yeast Pichia pastoris. In contrast, α/β-hydrolase was not found in the culture medium, though a significant amount of this enzyme accumulated in the yeast membrane fraction. These results suggest that microsporidia possess a broad set of enzymes and regulatory proteins secreted into infected cells to control host metabolic processes and molecular programs. [ABSTRACT FROM AUTHOR]

Published
2014
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27. Heterologous expression of pyruvate dehydrogenase E1 subunits of the microsporidium Paranosema ( Antonospora) locustae and immunolocalization of the mitochondrial protein in amitochondrial cells.

Author

Dolgikh, Viacheslav V., Seliverstova, Elena V., Naumov, Anton M., Senderskiy, Igor V., Pavlova, Olga A., and Beznoussenko, Galina V.

Subjects
*MICROSPORIDA, *INTRACELLULAR pathogens, *FUNGI, *METABOLISM, *GENES, *MITOCHONDRIA, *GLYCOLYSIS, *PYRUVATES, *DEHYDROGENASES, *ESCHERICHIA coli
Abstract

Microsporidia, a large group of fungi-related intracellular parasites, are characterized by drastically reduced metabolism. They possess genes encoding glycolysis components, and the glycerol–phosphate shuttle, but lack mitochondria, Krebs cycle, respiratory chain and pyruvate-converting enzymes, except α and β subunits of E1 enzyme of pyruvate dehydrogenase (PDH) complex. Here, we have expressed PDH subunits from the microsporidum Paranosema ( Antonospora) locustae in Escherichia coli. Western blot analysis with antibodies raised against recombinant proteins has revealed their specific accumulation in mature spores of P. locustae but not in the intracellular development stages. Two subunits were coprecipitated as a single heterooligomeric complex by anti-α or anti-β PDH antibodies. Ultracentrifugation of spore homogenate has shown the presence of PDH in the soluble fraction. Relocalization of the mitochondrial protein in microsporidial spore cytoplasm was confirmed by immunoelectron microscopy of ultrathin cryosections with affinity-purified anti-α PDH antibodies. On cryosections, parasite enzyme was found partly associated with the cytoplasmic side of ER and other intraspore membranes, suggesting that electrons might be transferred to any membrane acceptor and finally to oxygen in the parasite cell. [ABSTRACT FROM AUTHOR]

Published
2009
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28. Analogs of the Golgi complex in microsporidia: Structure and avesicular mechanisms of function

Author

Yuliya Y. Sokolova, Maria Antonietta De Matteis, Alberto Luini, Peter Auinger, Daniele Di Giandomenico, Alexander A. Mironov, Alvar Trucco, Viacheslav V. Dolgikh, Yuri S. Tokarev, P. B. Semenov, Sergei Skarlato, Igor V. Senderskiy, Margit Pavelka, Galina V. Beznoussenko, Massimo Micaroni, Elena V. Seliverstova, E. S. Snigirevskaya, Yan Yu. Komissarchik, Beznoussenko, Galina V., Dolgikh, Viacheslav V., Seliverstova, Elena V., Semenov, Petr B., Tokarev, Yuri S., Trucco, Alvar, Micaroni, Massimo, Di Giandomenico, Daniele, Auinger, Peter, Senderskly, Igor V., Skarlato, Sergei O., Snigirevskaya, Ekaterina S., Komissarchik, Yan Y. u., Pavelka, Margit, DE MATTEIS, Maria Antonietta, Luini, Alberto, Sokolova, Yuliya Y. a., and Mironov, Alexander A.

Subjects
Fat Body, Golgi Apparatus, Golgi Apparatu, Biology, Endoplasmic Reticulum, Gryllidae, symbols.namesake, Imaging, Three-Dimensional, Species Specificity, Microsporidiosis, Golgi, Image Processing, Computer-Assisted, Animals, Microsporidiosi, Secretory pathway, Life Cycle Stages, Host cell cytosol, Animal, Endoplasmic reticulum, Vesicle, fungi, Cell Membrane, Cell Biology, COP-Coated Vesicles, Golgi apparatus, COP-I vesicle, Cell biology, Life Cycle Stage, Secretory protein, Microsporidia, Polar tube, symbols, Intracellular transport, COP-Coated Vesicle
Abstract

Microsporidia are obligatory intracellular parasites, most species of which live in the host cell cytosol. They synthesize and then transport secretory proteins from the endoplasmic reticulum to the plasma membrane for formation of the spore wall and the polar tube for cell invasion. However, microsporidia do not have a typical Golgi complex. Here, using quick-freezing cryosubstitution and chemical fixation, we demonstrate that the Golgi analogs of the microsporidia Paranosema (Antonospora) grylli and Paranosema locustae appear as 300-nm networks of thin (25- to 40-nm diameter), branching or varicose tubules that display histochemical features of a Golgi, but that do not have vesicles. Vesicles are not formed even if membrane fusion is inhibited. These tubular networks are connected to the endoplasmic reticulum, the plasma membrane and the forming polar tube, and are positive for Sec13, γCOP and analogs of giantin and GM130. The spore-wall and polar-tube proteins are transported from the endoplasmic reticulum to the target membranes through these tubular networks, within which they undergo concentration and glycosylation. We suggest that the intracellular transport of secreted proteins in microsporidia occurs by a progression mechanism that does not involve the participation of vesicles generated by coat proteins I and II.

Published
2007

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