Moscow University Biological Sciences Bulletin最新文献

{"title":"Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation","authors":"T. B. Stanishneva-Konovalova, E. B. Pichkur, S. S. Kudryavtseva, I. A. Yaroshevich, A. N. Semenov, E. G. Maksimov, A. V. Moiseenko, O. I. Volokh, V. I. Muronets","doi":"10.3103/s0096392523700219","DOIUrl":"https://doi.org/10.3103/s0096392523700219","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"137 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cryo-Electron Microscopy of Enveloped Viruses Using an Upgraded Transmission Electron Microscope: Influenza Type A and B Viruses and SARS-CoV-2","authors":"L. V. Kordyukova, A. V. Moiseenko, T. A. Timofeeva, I. T. Fedyakina","doi":"10.3103/s0096392523700153","DOIUrl":"https://doi.org/10.3103/s0096392523700153","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Cryo-electron microscopy (cryo-EM) is indispensable for the structural studies of enveloped viruses: dangerous pathogens of humans and animals. Yet, it requires highly specialized equipment as well as careful sample preparation. In this work, the capabilities of a JEOL JEM-2100 transmission electron microscope equipped with a cryo-transfer holder are used, and preliminary cryo-EM data for influenza A and B virus strains and SARS-CoV-2 inactivated with beta-propiolactone are presented. Image analysis allows us to (1) distinguish “empty” viral particles from “full” ones (containing nucleocapsid); (2) visualize the lipid bilayer of the viral envelope; (3) identify influenza virus surface antigens and the M1 protein layer combined with the inner lipid monolayer; and (4) distinguish different morphology of S-spikes on the surface of inactivated SARS-CoV-2 virions. The developed approach provides good image quality for both fundamental and applied research.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"16 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097501","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Condensed DNA Structure in Bacteria Subjected to Various Types of Stress","authors":"Y. F. Krupyanskii, N.G. Loiko, V. V. Kovalenko, A. A. Generalova, E. V. Tereshkin, A. V. Moiseenko, K. B. Tereshkina, A. N. Popov, O. S. Sokolova","doi":"10.3103/s0096392523700207","DOIUrl":"https://doi.org/10.3103/s0096392523700207","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The architecture of DNA in the dormant cells was studied by synchrotron radiation diffraction and transmission electron microscopy. Diffraction experiments indicate the appearance of a periodic ordered organization of DNA. Transmission electron microscopy made it possible to visualize information about the type of DNA condensation. Intracellular nanocrystalline, liquid-crystalline and folded nucleosome-like structures of DNA have been found. Next, we studied changes in DNA architecture under stress of exposure to a chemical analogue of the anabiosis autoinducer (4-hexylresorcinol). Studies of the DNA architecture in the anabiotic and mummified states show the identity of the DNA structure in the anabiotic state and in the dormant state under starvation stress. The architecture of DNA in a mummified state is very different from that of DNA in an anabiotic state.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"33 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097725","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peculiarities of Cytochrome c Enzymatic Activity with Cardiolipin","authors":"I. N. Levchenko, G. K. Vladimirov, I. V. Volodyaev, Y. A. Vladimirov","doi":"10.3103/s0096392523700256","DOIUrl":"https://doi.org/10.3103/s0096392523700256","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The points of enzymatic activity, quantum yields, structure, functions of luminol chemiluminescence activated by physical activators natural dyes isoquinolysine coumarins C-334 and C-525 under the action of cytochrome <i>c</i> complex with cardiolipin in aqueous medium and in nonpolar environment were considered. It is shown: (1) the enzymatic activity points and quantum yields are significantly higher in the presence of the physical activator coumarin C-525 than in the case of its own unactivated luminescence or in the case of the physical activator C-334; (2) the enzymatic activity depends not only on the concentration of cytochrome <i>c</i> but also on the percentage ratio between the native form of cytochrome <i>c</i> with cardiolipin and the partially denatured one.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"127 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097873","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Stabilization of Full-Length S-Protein of SARS-Cov-2 Coronavirus in SMA Polymer for Electron Microscopy Study","authors":"N. Yu. Mamaeva, N. I. Derkacheva, D. A. Gasanova, O. S. Sokolova, G. S. Glukhov","doi":"10.3103/s0096392523700165","DOIUrl":"https://doi.org/10.3103/s0096392523700165","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>A detergent-free protocol for purification of the coronavirus prefusion S-protein using styrene-maleic acid copolymer (SMA) was developed. Expression of the S-protein was carried out in HEK293T cells. Two solubilization methods were used to purify and prepare the S-protein for microscopy: in NP-40 detergent and as part of SMA. The resulting preparations were examined in an electron microscope, and the particles of purified S-proteins were classified. Analysis of two-dimensional projections of the particles showed that the use of lipodiscs for solubilization leads to lower mobility of the purified protein on the substrate compared to the protein in the detergent, which may further contribute to obtaining higher resolutions when studying the structure of membrane proteins.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"39 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097515","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Advances in Structural Research Using Electron Microscopy in Russia (Results of the Fourth International Conference RICCEM-2023)","authors":"O. S. Sokolova, T. B. Stanishneva-Konovalova, M. P. Kirpichnikov","doi":"10.3103/s0096392523700128","DOIUrl":"https://doi.org/10.3103/s0096392523700128","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The IV Russian International Conference on Cryo-Electron Microscopy (RICCEM-2023) was held at the Faculty of Biology of Lomonosov Moscow State University in a hybrid online and offline format and brought together more than 250 researchers from 10 countries. Following the conference, a special issue of the journal “Moscow University Biological Sciences Bulletin” was published. This article summarizes the main results of the conference and the content of the papers published in the special issue.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"35 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097729","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"How Does a Biopolymer (Protein) Fold into a Unique 3D Structure?","authors":"K. V. Shaitan","doi":"10.3103/s009639252370013x","DOIUrl":"https://doi.org/10.3103/s009639252370013x","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The current state of the protein folding problem and other biopolymers folding is discussed. The concept of a multidimensional potential energy surface and free energy surface for linear polymers is detailed, taking into account the topology of the configuration space and the presence of symmetry elements with respect to the rearrangement of identical monomer units. The presence of kinematic connections for conformational movements in a viscous medium leads to a tendency for the formation of helical structures of linear polymers. The dynamic effects of viscosity also lead to an almost uniform distribution of energy dissipation rates across the nodes of the chain. The combination of free energy surface topography and viscosity effects provides a physical basis for advancing folding theory toward interpreting a variety of experimental observations and elucidating principles of amino acid code formation for 3D protein structures. The relationship between the denaturation temperature of the folded state of the biopolymer and the energy of nonvalent interactions between monomers in the chain is analyzed.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"39 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140097732","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bacteria of the Genus Bacillus on the Russian Segment of the International Space Station","authors":"R. R. Yenikeyev, L. M. Zakharchuk","doi":"10.3103/s0096392523700062","DOIUrl":"https://doi.org/10.3103/s0096392523700062","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Pure cultures of 19 strains of spore-forming bacteria were obtained from the equipment surfaces of the Russian segment of the International Space Station. The study of morphological, cultural, and physiological-biochemical properties of these bacteria allowed the authors to attribute all strains to the genus <i>Bacillus</i>. As a result of using MALDI-TOF methods and genome-wide sequencing, it was found that six of 19 bacillus strains belong to the species <i>B. paralicheniformis</i>, four to <i>B. pumilus</i>, four to <i>B. subtilis</i>, two to <i>B. cereus</i>, and one to <i>B. amyloliquefaciens</i>. In accordance with the requirements and norms of EUCAST 2023, the resistance of bacillus strains obtained from the Russian segment of the International Space Station to such antibiotics as imipenem, meropenem, ciprofloxacin, levofloxacin, norfloxacin, vancomycin, erythromycin, clindamycin, and linezolid was studied. Resistance to erythromycin was found in 11 strains of <i>Bacillus</i>, and five strains showed resistance to clindamycin. Only one strain showed resistance to imipenem, levofloxacin, and norfloxacin, respectively. Analysis of the complete genome of bacterial strains in which resistance to erythromycin and (or) clindamycin was found made it possible to establish that resistance to these antibiotics in <i>B. paralicheniformis</i> strains SE71, SE131, SE181, SE182, and SE183 provides the <i>ermD</i> antibiotic resistance gene. In <i>B. cereus</i> SE43, resistance to erythromycin encodes the <i>mphL</i> gene.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"2 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140005436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Investigation into Anti-Inflammatory Properties of Excretory/Secretory Products from Gull-Tapeworm Dibothriocephalus dendriticus and Ligula Ligula interrupta Plerocercoids","authors":"A. N. Pavlyuchenkova, I. A. Kutyrev, A. V. Fedorov, M. A. Chelombitko, O. E. Mazur, Z. N. Dugarov","doi":"10.3103/s0096392523700049","DOIUrl":"https://doi.org/10.3103/s0096392523700049","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>In this work, the anti-inflammatory potential of secretory-excretory products (SEP) of gull-tapeworm <i>Dibothriocephalus dendriticus</i> and Ligula <i>Ligula interrupta</i> plerocercoids was studied for the first time in an in vitro model of LPS-induced activation of macrophages. A monocyte cell line derived from a patient with acute monocytic leukemia, THP-1, was used as a macrophage model. The anti-inflammatory properties of SEP were determined by the content of tumor necrosis factor (TNF) and interleukin-6 cytokines in the incubation medium using commercial kits for enzyme immunoassay. The results of our study indicated that SEP from <i>L. interrupta</i> plerocercoids have a pronounced anti-inflammatory effect, while SEP from <i>D. dendriticus</i> plerocercoids did not have such an effect. The authors next investigated the anti-inflammatory properties of <i>L. interrupta</i> SEP in a carrageenan-induced air-sac inflammation model in mice. A significant decrease in the volume of inflammatory exudate under the influence of <i>L. interrupta</i> SEP was found as well as an increase in the level of the interleukin-6 cytokine. At the same time, SEP of <i>L. interrupta</i> had no effect on the number of cells per 1 mL of exudate or the level of the proinflammatory cytokine TNF. The low molecular weight fraction of <i>L. interrupta</i> SEP also increased the level of the anti-inflammatory cytokine interleukin-10, which indicates a more pronounced anti-inflammatory effect compared to the high molecular weight fraction. The results obtained, in general, indicate the anti-inflammatory properties of the SEP of <i>L. interrupta</i> plerocercoids. However, the mechanism of anti-inflammatory action has not been elucidated and requires further research.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"20 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140005553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Why Freshwater Hydra Does Not Get Alzheimer’s Disease","authors":"A. N. Khokhlov","doi":"10.3103/s0096392523700104","DOIUrl":"https://doi.org/10.3103/s0096392523700104","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The history of research into the fundamental mechanisms of the pathogenesis of Alzheimer’s disease (AD) is briefly reviewed. Concepts in which a decisive role in the development of this disease was attributed to aluminum or free radicals are analyzed. The lack of reliable data to date to support these concepts is highlighted. The author’s point of view is stated, according to which almost all the results indicating the advisability of using antioxidants (as well as other potential drugs for AD) for the prevention and treatment of AD were obtained in model animals with certain pathologies (for example, with severe oxidative stress), which contribute to the formation of symptoms similar to those of AD in humans. In this regard, parallels with experimental gerontological work aimed at studying the effect of calorie-restricted nutrition on aging and life span are drawn. It is noted that these studies also used animals that were either not completely normal or were in unfavorable conditions. According to the author, the lack of serious success in the development of effective geroprotectors or drugs for the prevention/treatment of AD is due to the ignorance by most specialists of the principles of classical gerontology, in particular, the definitions of aging and age-related diseases, as well as correct approaches to the selection of control objects for their studies. It is emphasized that humans, unfortunately, cannot use the freshwater hydra method to combat aging and age-related diseases. Under certain conditions, it continuously renews all cells (including nerve cells) of its body and thereby ensures its “immortality.” In humans, replacing “old” neurons can lead to loss of personality/individuality, and “repairing” these cells seems impossible today. In this regard, the author considers it advisable to conduct studies of the aging of postmitotic cells in experiments on stationary cell cultures, which can accelerate, in particular, elucidation of the mechanisms of accumulation of beta-amyloid and senile pigments, such as lipofuscin, in neurons. The need to conduct clinical studies of AD as complementary to experimental work is noted, although the former are much more expensive and time-consuming. Only confirmation in human studies of the effectiveness of drugs developed in experiments on model animals will allow them to be recommended for clinical use.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":"28 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140005441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}