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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Davydova A., Vorobyeva M., Krasitskaya V., Vorobjev P., Tupikin A., Kabilov M., Frank L., Venyaminova A.
Заглавие : 2 '-Modified RNA aptamers specific to photoprotein obelin as a platform for new bioluminescent biosensors
Колич.характеристики :2 с
Коллективы : Russian Science Foundation [16-14-10296]
Место публикации : FEBS Open Bio: WILEY, 2018. - Vol. 8. - С. 115-116. - ISSN 2211-5463
Примечания : Cited References:0. - The work is supported by Russian Science Foundation (Grant No. 16-14-10296).
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Borisova V.V., Pyshnaya I.A., Pyshnyi D.V., Frank L.A.
Заглавие : A Highly Sensitive and Rapid Method for the Detection of DNA Fragments Using the Photoprotein Obelin as a Reporter
Колич.характеристики :7 с
Коллективы :
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2008. - Vol. 34, Is. 6. - С. 709-715. - ISSN 1068-1620, DOI 10.1134/S1068162008060101
Примечания : Cited References: 13. - This work was supported the program Molecular and Cellular Biology (project no. 10.6), integration grants of the Siberian Division of the Russian Academy of Sciences (73 and 55), CRDF, and the Russian Foundation for Basic Research (project nos. 06-04-49263-a and 06-04-08076-ofi).
Предметные рубрики: BIOLUMINESCENT IMMUNOASSAY
Ключевые слова (''Своб.индексиров.''): obelin--bioluminescent hybridization assay--pcr
Аннотация: The recombinant Ca(2+)-activated photoprotein obelin was used as a reporter protein in a solid-phase bioluminescent hybridization DNA assay. Oligonucleotide probes were immobilized on the surface of polymer methacrylate beads or microbiological plates of different types. A 30-mer oligonucleotide or its derivative with the biotin residue on the 3'-terminus, as well as a denatured double-stranded PCR fragment of the hepatitis C virus with the sequence of the 30-mer oligonucleotide was used as a DNA template. The probe in the hybridization complex was labeled by the elongation of the chain using a Taq DNA polymerase in the presence of biotinylated deoxyuridine triphosphate. The results of the bioluminescent assay were compared with the results of colorimetric analysis obtained with alkaline phosphatase as a reporter protein. It was shown that the use of the bioluminescent obelin label substantially accelerates the DNA detection procedure, provides a high sensitivity of the assay (no less than 10(-15) mol of DNA template), and ensures a quantitative determination of the amount of DNA template in the tested sample.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Antipina L.Y., Tomilin F.N., Vysotskii E.S., Ovchinnikov S.G.
Заглавие : A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN
Колич.характеристики :6 с
Место публикации : J. Struct. Chem.: SPRINGER, 2011. - Vol. 52, Is. 5. - С. 870-875. - ISSN 0022-4766
Примечания : Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213).
Предметные рубрики: CALCIUM-DISCHARGED OBELIN
SEMIEMPIRICAL METHODS
1.7 ANGSTROM
OPTIMIZATION
PARAMETERS
MECHANISM
FLUORESCENCE
ELEMENTS
PROTEIN
EMITTER
Ключевые слова (''Своб.индексиров.''): coelenterazine--2-hydroperoxy-coelenterazine--obelia longissima--renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Borisova V.V., Vereshchagina T.A., Fomenko E.V., Anshits A.G., Gitelson I.I.
Заглавие : Affine magnetic sorbents supported on coal ash microspheres for recombinant protein isolation
Место публикации : Applied Biochemistry and Microbiology. - 2009. - Vol. 45, Is. 2. - С. 215-220. - ISSN 00036838 (ISSN) , DOI 10.1134/S0003683809020173
Ключевые слова (''Своб.индексиров.''): clytia gregaria--obelia longissima
Аннотация: The results of the development and utilization of an affine magnetic sorbent with Ni2+ ions immobilized on coal ash microspheres are reported. The applicability of the material in the isolation of Histag proteins is demonstrated by examples of the recombinant green fluorescent protein from Clytia gregaria and the Ca2+ regulated photoprotein obelin from Obelia longissima. The specific sorption capacity of the sorbent was 2-7 mg/cm3 for medium-size proteins (20-30 kDa). The particles are suitable for chromatography with the presence of chaotropic agents and EDTA. They are easy to manipulate as isolation of a target protein takes 30-35 min. On the one hand, the elevated affinity of the sorbent to proteins rich in native histidines may result in a high degree of irreversible sorption; on the other hand, it allows isolation of such proteins without the introduction of artificial polyhistidine fragments. В© 2009 Pleiades Publishing, Ltd.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Natashin P. V., Malikova N. P., Niu F., Pu M., Vysotski E. S., Liu Z.-J.
Заглавие : All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin
Место публикации : J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - С. 57-66. - ISSN 10111344 (ISSN) , DOI 10.1016/j.jphotobiol.2015.11.012
Ключевые слова (''Своб.индексиров.''): aequorin--bioluminescence--calcium--coelenterazine--obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Vysotski E.S., Markova S.V., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin
Колич.характеристики :13 с
Место публикации : Protein Sci.: COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, 2005. - Vol. 14, Is. 3. - С. 663-675. - ISSN 0961-8368, DOI 10.1110/ps.041142905
Примечания : Cited References: 46
Предметные рубрики: RAY CRYSTALLOGRAPHIC ANALYSIS
ANGSTROM RESOLUTION
SEQUENCE-ANALYSIS
CA2+-REGULATED PHOTOPROTEINS
CA2+-DISCHARGED PHOTOPROTEIN
LUMINESCENT PROTEIN
MODULATED PROTEINS
ELECTRON-DENSITY
CLONING
CDNA
Ключевые слова (''Своб.индексиров.''): bioluminescence--ef-hand--fluorescent protein--proton relay--calcium-binding loops--aequorin--obelin--diffraction
Аннотация: The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7 Angstrom and 2.2 Angstrom. respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-proteins retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hydroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these subtle shifts are the basis of the ability of these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.
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Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Frank, Ludmila A., Krasitskaya, Vasilisa V.
Заглавие : Application of Enzyme Bioluminescence for Medical Diagnostics
Колич.характеристики :23 с
Место публикации : Adv. Biochem. Eng. Biotechnol.: SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - С. 175-197. - (Advances in Biochemical Engineering-Biotechnology). - , DOI 10.1007/978-3-662-43385-0_6
Примечания : Cited References:63
Предметные рубрики: RESONANCE ENERGY-TRANSFER
POLYMERASE-CHAIN-REACTION
LUCIFERASE
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-regulated photoprotein--diagnostics--immunoassay--luciferase--nucleic acid hybridization assay
Аннотация: Nowadays luciferases are effectively used as analytical instruments in a great variety of research fields. Of special interest are the studies dealing with elaboration of novel analytical systems for the purposes of medical diagnostics. The ever-expanding spectrum of clinically important analytes accounts for the increasing demand for new techniques for their detection. In this chapter we have made an attempt to summarize the results on applications of luciferases as reporters in binding assays including immunoassay, nucleic acid hybridization assay, and so on. The data over the last 15 years have been analyzed and clearly show that luciferase-based assays, due to extremely high sensitivity, low cost, and the lack of need for skilled personnel, hold much promise for clinical diagnostics.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Vysotski E.S., Deng L..., Lee J..., Rose J..., Wang B.C.
Заглавие : Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine
Колич.характеристики :7 с
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2003. - Vol. 311, Is. 2. - С. 433-439. - ISSN 0006-291X, DOI 10.1016/j.bbrc.2003.09.231
Примечания : Cited References: 29
Предметные рубрики: CRYSTAL-STRUCTURE
BIOLUMINESCENT PROTEIN
VIOLET BIOLUMINESCENCE
PHOTOPROTEIN AEQUORIN
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
W92F OBELIN
PURIFICATION
REFINEMENT
EXPRESSION
Ключевые слова (''Своб.индексиров.''): photoprotein--bioluminescence--atomic resolution--ef-hand
Аннотация: The spatial structure of the Ca2+-regulated photoprotein obelin has been solved to resolution of 1.1 Angstrom. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73 Angstrom resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca2+, the electron densities of both oxygen atoms became equally intense. In addition, one Ca2+ was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms. (C) 2003 Elsevier Inc. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : LETUNOV V.N., VYSOTZKII E.S.
Заглавие : BIOLUMINESCENCE ACTIVITY AND CONTENT OF CA-2+-DEPENDENT PHOTOPROTEIN IN OBELIA-LONGISSIMA (PALLAS) HYDROID COLONIES
Колич.характеристики :7 с
Место публикации : Zhurnal Obshchei Biol.: MEZHDUNARODNAYA KNIGA, 1988. - Vol. 49, Is. 3. - P381-387. - ISSN 0044-4596
Примечания : Cited References: 14
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva, Elena V., Vysotski, Eugene S.
Заглавие : Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin
Колич.характеристики :9 с
Коллективы : Russian Academy of Sciences [03562016-0712, 0356-2015-0103]; RFBR [17-04-00764]
Место публикации : J. Photochem. Photobiol. B-Biol.: ELSEVIER SCIENCE SA, 2017. - Vol. 174. - С. 97-105. - ISSN 1011-1344, DOI 10.1016/j.jphotobio1.2017.07.021
Примечания : Cited References:54. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 03562016-0712 and 0356-2015-0103) and the RFBR grant 17-04-00764.
Предметные рубрики: SEQUENCE-ANALYSIS
APO-OBELIN
INTRINSIC FLUORESCENCE
COELENTERAZINE
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--photoprotein--coelenteramide--cysteine--serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or p-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coil, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild -type aequorin. In contrast, Cys-free obelin retains only 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a "fast" component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 0.2 and 44.6 0.4 C for aequorin and Cys-free aequorin, and 49.1 0.1 and 28.8 0.3 C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E. V., Vysotski E. S.
Заглавие : Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin
Место публикации : J. Photochem. Photobiol. B Biol.: Elsevier B.V., 2017. - Vol. 174. - С. 97-105. - ISSN 10111344 (ISSN) , DOI 10.1016/j.jphotobiol.2017.07.021
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenteramide--coelenterazine--cysteine--photoprotein--serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or ?-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coli, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild-type aequorin. In contrast, Cys-free obelin retains only ~ 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a “fast” component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 ± 0.2 and 44.6 ± 0.4 °C for aequorin and Cys-free aequorin, and 49.1 ± 0.1 and 28.8 ± 0.3 °C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield. © 2017 Elsevier B.V.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Frank L.A., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin
Колич.характеристики :9 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2013. - Vol. 12, Is. 6. - С. 1016-1024. - ISSN 1474-905X, DOI 10.1039/c3pp00002h
Примечания : Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
CA2+-BINDING PHOTOPROTEIN
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
MNEMIOPSIS-LEIDYI
LIGHT-EMISSION
W92F OBELIN
CLONING
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya, Vasilisa V., Chaukina, Valentina V., Abroskina, Maria V., Vorobyeva, Maria A., Ilminskaya, Aleksandra A., Kabilov, Marsel R., Prokopenko, Semyon V., Nevinsky, Georgy A., Venyaminova, Alya G., Frank, Ludmila A.
Заглавие : Bioluminescent aptamer-based sandwich-type assay of anti-myelin basic protein autoantibodies associated with multiple sclerosis
Колич.характеристики :7 с
Коллективы : Russian Foundation for Basic Research (RFBR), Russia [17-315-50027]; Russian State [AAAA-A17-117013050026-4, AAAA-A17-117020210021-7]
Место публикации : Anal. Chim. Acta: ELSEVIER SCIENCE BV, 2019. - Vol. 1064. - С. 112-118. - ISSN 0003-2670, DOI 10.1016/j.aca.2019.03.015. - ISSN 1873-4324(eISSN)
Примечания : Cited References:29. - This work was supported by the Russian Foundation for Basic Research (RFBR), Russia, under the grant No 17-315-50027; Russian State funded budget projects No. AAAA-A17-117013050026-4 and AAAA-A17-117020210021-7.
Предметные рубрики: ANTIBODIES
BIOMARKERS
RNA
Ключевые слова (''Своб.индексиров.''): bioluminescent microassay--rna aptamers--autoantibodies to myelin basic--protein--multiple sclerosis
Аннотация: Bioluminescent solid-phase sandwich-type microassay was developed to detect multiple sclerosis (MS)-associated autoantibodies in human sera. The assay is based on two different 2'-F-Py RNA aptamers against the target autoantibodies as biospecific elements, and Ca2+-regulated photoprotein obelin as a reporter. The paper describes elaboration of the assay and its application to 91 serum samples from patients with clinically definite MS and 86 ones from individuals healthy in terms of MS. Based on the receiver-operator curve (ROC) analysis, the chosen threshold value as clinical decision limit offers sensitivity of 63.7% and specificity of 94.2%. The area under the ROC curve (AUC) value of 0.87 shows a good difference between the groups under investigation. The likelihood ratio of 10.97 proves the diagnostic value of the assay and its potential as one of the laboratory MS-tests. (C) 2019 Elsevier B.V. All rights reserved.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bashmakova, Eugenia E., Krasitskaya, Vasilisa V., Zamay, Galina S., Zamay, Tatiana N., Frank, Ludmila A.
Заглавие : Bioluminescent aptamer-based solid-phase microassay to detect lung tumor cells in plasma
Колич.характеристики :5 с
Коллективы : Russian Academy of Sciences [0356-2017-0017]
Место публикации : Talanta: ELSEVIER SCIENCE BV, 2019. - Vol. 199. - С. 674-678. - ISSN 0039-9140, DOI 10.1016/j.talanta.2019.03.030. - ISSN 1873-3573(eISSN)
Примечания : Cited References:19. - The authors are grateful to the staff of Krasnoyarsk regional clinical oncology center named after A.I. Kryzhanovsky and particularly doctor Alexey V. Krat for the experimental material provided. This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, project No. 0356-2017-0017.
Предметные рубрики: CONJUGATED NANOPARTICLES
CANCER
COLLECTION
LIGANDS
PROBES
Ключевые слова (''Своб.индексиров.''): dna aptamers--lung tumor--bioluminescent solid-phase microassay
Аннотация: Two high-affinity DNA aptamers for lung tumor cells were applied as biospecific elements in bioluminescent assay of patient blood. The oligonucleotide complementary to the 5' end of both aptamers carrying either biotin or Ca2+-regulated photoprotein obelin was used to form a sandwich-type analytical complex on the surfaces of magnetic streptavidin-activated microspherical particles. Clinical blood samples from cases of morphologically confirmed lung cancer and control samples were analyzed applying the developed assay. From the receiver operator curve (ROC) analysis, the chosen threshold value as clinical decision limit offers the sensitivity of 91.5% and the specificity of 75% (p 0.001). The area under ROC curve with the value of 0.901 distinguishes well between the two groups under investigation.
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15.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Frank L.A., Vysotski E.S.
Заглавие : Bioluminescent immunoassay of alphafetoprotein with Ca2+-activated photoprotein obelin
Место публикации : BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS: JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - С. 439-442. - 4. - ISBN 0-471-97502-8
Примечания : Cited References: 0
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Petunin A.I., Vysotski E.S.
Заглавие : Bioluminescent immunoassay of thyrotropin and thyroxine using obelin as a label
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2004. - Vol. 325, Is. 2. - С. 240-246. - ISSN 0003-2697, DOI 10.1016/j.ab.2003.11.003
Примечания : Cited References: 16
Предметные рубрики: AEQUORIN
PURIFICATION
PROTEIN
CDNA
Ключевые слова (''Своб.индексиров.''): obelin--human thyrotropin--thyroxine--immunoassay--bioluminescence
Аннотация: Solid-phase bioluminescent immunoassay of thyroid hormones, human thyrotropin (hTSH) and two forms of thyroxine (T4), whose determinations are vitally important for diagnostics of thyroid diseases and the efficiency of treatment, is described. The recombinant obelin, a Ca2+-regulated photoprotein originally derived from the luminous marine hydroid Obelia longissima, is employed as a bioluminescent label. To produce obelin conjugates with anti-hTSH, anti-T4 immunoglobulins (IgG), and T4, additional SH groups are introduced into the obelin molecule using Traut's reagent (2-iminothiolane) and then obelin possessing extra SH groups is conjugated with succinimidyl 4-(N-maleimidomethyl)-cyclohexane-1-carboxylate-activated IgGs or T4. The total yield of obelin conjugates determined by luminescent activity is 60-65% after all chemical and purification procedures. The obtained conjugates are stable to lyophilization and in solution for at least 9 months at 4 degreesC, with loss of activity not exceeding 10%. The application of obelin conjugates for determination of the hTSH, total T4, and free T4 in standard, control, and patient sera displays high sensitivity and reproducibility of results. The results of bioluminescent immunoassays are closely comparable to those obtained by the radioimmunoassay method (R = 0.95-0.99). (C) 2003 Elsevier Inc. All rights reserved.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gealageas R..., Malikova N.P., Picaud S..., Borgdorff A.J., Burakova L.P., Brulet P..., Vysotski E.S., Dodd R.H.
Заглавие : Bioluminescent properties of obelin and aequorin with novel coelenterazine analogues
Колич.характеристики :13 с
Коллективы : ICSN; CNRS Physics, Chemistry and Biology interface grant; RFBR [12-04-00131]; Government of Russian Federation [11.G34.31.0058]; ANR
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2014. - Vol. 406, Is. 11. - С. 2695-2707. - ISSN 1618-2642, DOI 10.1007/s00216-014-7656-4. - ISSN 1618-2650
Примечания : Cited References: 57. - R.G. acknowledges the ICSN for a fellowship. We are grateful for the ANR grant to P.B. and a CNRS Physics, Chemistry and Biology interface grant to R.H.D. and P.B.; N.P.M, L.P.B., and E.S.V. acknowledge the RFBR grant 12-04-00131 and the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant 11.G34.31.0058). P.B. and A.J.B. are indebted to Eric Karplus from Science Wares Inc. for helping with single-photon imaging software.
Предметные рубрики: PHOTOPROTEIN OBELIN
CRYSTAL-STRUCTURE
CA2+-REGULATED PHOTOPROTEINS
CA2+-ACTIVATED PHOTOPROTEIN
SEMISYNTHETIC AEQUORINS
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
BINDING PROTEIN
CALCIUM-BINDING
CA2+ DYNAMICS
Ключевые слова (''Своб.индексиров.''): bioluminescence--luciferase--photoprotein--coelenterazine
Аннотация: The main analytical use of Ca2+-regulated photoproteins from luminous coelenterates is for real-time non-invasive visualization of intracellular calcium concentration ([Ca2+](i)) dynamics in cells and whole organisms. A limitation of this approach for in vivo deep tissue imaging is the fact that blue light emitted by the photoprotein is highly absorbed by tissue. Seven novel coelenterazine analogues were synthesized and their effects on the bioluminescent properties of recombinant obelin from Obelia longissima and aequorin from Aequorea victoria were evaluated. Only analogues having electron-donating groups (m-OCH3 and m-OH) on the C6 phenol moiety or an extended resonance system at the C8 position (1-naphthyl and alpha-styryl analogues) showed a significant red shift of light emission. Of these, only the alpha-styryl analogue displayed a sufficiently high light intensity to allow eventual tissue penetration. The possible suitability of this compound for in vivo assays was corroborated by studies with aequorin which allowed the monitoring of [Ca2+](i) dynamics in cultured CHO cells and in hippocampal brain slices. Thus, the alpha-styryl coelenterazine analogue might be potentially useful for non-invasive, in vivo bioluminescence imaging in deep tissues of small animals.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva, Elena, V, Jiang, Tianyu, Malikova, Natalia P., Li, Minyong, Vysotski, Eugene S.
Заглавие : Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents
Колич.характеристики :21 с
Коллективы : RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 15. - Ст.5446. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21155446
Примечания : Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.).
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.
WOS
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E. V., Jiang T., Malikova N. P., Li M., Vysotski E. S.
Заглавие : Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 15. - Ст.5446. - С. 1-21. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21155446
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V.V., Burakova L.P., Pyshnaya I.A., Frank L.A.
Заглавие : Bioluminescent reporters for identification of gene allelic variants
Колич.характеристики :8 с
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2012. - Vol. 38, Is. 3. - С. 298-305. - ISSN 1068-1620, DOI 10.1134/S1068162012030090
Примечания : Cited References: 13. - The authors thank the staff of Hematology Research Center (Krasnoyarsk Branch of Russian Academy of Medical Sciences) for providing DNA samples. The work was supported by the Integration Interdisciplinary Project of Siberian Branch of the Russian Academy of Sciences No. 76 and the Krasno yarsk Regional Fund for the support of scientific and technological activities.
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
RENILLA-MUELLERI
LUCIFERASE
PURIFICATION
SUBSTRATE
CLONING
CDNA
Ключевые слова (''Своб.индексиров.''): snp--pext reaction--obelin--luciferase--bioluminescent microassay
Аннотация: A method for single nucleotide polymorphism identification was developed, which was based on the primer extension reaction (PEXT) followed by bioluminescent solid-phase microassay. Recombinant Ca2+-regulated photoprotein obelin and coelenterazine-dependent Renilla muelleri luciferase were used as reporters. The study was performed as an example of SNP genotyping of the human F5 gene encoding human Factor V Leiden polymorphism 1691 G - A (R506Q). Genomic DNA was amplified by PCR using primers flanking polymorphic site of 140 base pairs. PCR products were used as templates for two PEXT reactions using two primers containing 3'-terminal nucleotides, which were complementary to either normal or mutant alleles. If the template and allele-specific primer were completely complementary, the latter was elongated with DNA polymerase. The resulting extension product contained biotin residue due to the presence of biotinylated deoxyuridine triphosphate (B-dUTP) in the reaction mixture. The products were analyzed using obelin-streptavidin conjugates. The optimal PEXT-reaction conditions were found, which ensured a high reliability of SNP genotyping. A new approach to simultaneously revealing both alleles in one well was developed using two bioluminescent reporters. The efficiency of the proposed approach was shown in the study of clinical DNA samples.
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