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Use of proZZ-obelin fusion protein in bioluminescent immunoassay [Text] / L. A. Frank, V. A. Illarionova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 1996. - Vol. 219, Is. 2. - P475-479, DOI 10.1006/bbrc.1996.0258. - Cited References: 21 . - 5. - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ESCHERICHIA-COLI
   EXPRESSION
   AEQUORIN
   PURIFICATION
   SYSTEM
Аннотация: Obelin is a photoprotein that emits light by Ca2+-binding. To develop a bioluminescent immunoassay based on the light emission property of obelin, we have expressed the apoobelin fusion protein with ZZ-domain of S. aureus protein A in E. coil by recombinant DNA techniques. The pro2Z-obelin expressed was purified by one-step affinity chromatography on IgG-Agarose. The purified proZZ-obelin has both the luminescent activity of obelin and the IgG-binding ability of ZZ-domain. The specific activity of fusion protein was 8.5 x 10(15) photons per mg of protein. (C) 1996 Academic Press, Inc.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Illarionova, V.A.; Vysotski, E.S.

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Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay [Text] / L. A. Frank, A. I. Petunin, E. S. Vysotski // Russ. J. Bioorg. Chem. - 2004. - Vol. 30, Is. 4. - P327-331, DOI 10.1023/B:RUBI.0000037257.80835.7a. - Cited References: 16 . - ISSN 1068-1620

РУБ Biochemistry & Molecular Biology + Chemistry, Organic
Рубрики:
ESCHERICHIA-COLI
   PURIFICATION
   AEQUORIN
   PROTEIN
   CDNA
Кл.слова (ненормированные):
bioluminescent immunoassay -- obelin -- thyroid stimulating hormone
Аннотация: An efficient procedure for obelin conjugation with immunoglobulins was developed. The possibility was shown of using the resulting conjugates instead of a radioisotope label for the immunoassay of thyroid stimulating hormone in sera; the conjugates provide a sensitivity of 0.01 muIU/ml. The results of bioluminescent immunoassay (sera of 34 patients) satisfactorily correlate with the results of radioisotope assay (R 0.99).

Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
DIAS Ltd, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Petunin, A.I.; Vysotski, E.S.

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Applications of nanodiamonds for separation and purification of proteins [Text] / V. S. Bondar', I. O. Pozdnyakova, A. P. Puzyr' // Phys. Solid State. - 2004. - Vol. 46, Is. 4. - P758-760, DOI 10.1134/1.1711468. - Cited References: 11 . - ISSN 1063-7834

РУБ Physics, Condensed Matter
Рубрики:
ESCHERICHIA-COLI
OBELIN
Аннотация: Recombinant apoobelin and recombinant luciferase are separated from bacterial cells of Escherichia coli with the use of detonation nanodiamonds. The application of nanodiamonds has a number of points in its favor, namely, (i) simplifies the procedures for purifying the proteins, (ii) decreases the time of their separation to 30-40 min, (iii) eliminates the necessity of using special chromatographic equipment, and (iv) makes it possible to prepare high-purity apoobelin and luciferase materials with protein yields of 35-45 and 45-60%, respectively. The possible mechanisms of interaction of protein molecules and nanodiamond particles are analyzed. (C) 2004 MAIK "Nauka / Interperiodica".

Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bondar', V.S.; Pozdnyakova, I.O.; Puzyr', A.P.

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A model of bacterial cell cycle duration based on DnaA dynamics and estimation of the population cost of bacterial plasmids [Text] / A. N. Shuvaev, A. V. Brilkov // Dokl. Biochem. Biophys. - 2007. - Vol. 416, Is. 01.06.2013. - P233-236, DOI 10.1134/S1607672907050018. - Cited References: 17 . - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ESCHERICHIA-COLI
   GROWTH-RATE
   PARAMETERS
   SIZE
   TIME

Держатели документа:
[Shuvaev, A. N.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Brilkov, A. V.] Krasnoyarsk Fed Univ, Krasnoyarsk 660062, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Shuvaev, A.N.; Brilkov, A.V.

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A Glucose-Utilizing Strain, Cupriavidus euthrophus B-10646: Growth Kinetics, Characterization and Synthesis of Multicomponent PHAs [Text] / T. . Volova [et al.] // PLoS One. - 2014. - Vol. 9, Is. 2. - Ст. e87551, DOI 10.1371/journal.pone.0087551. - Cited References: 64. - This study was financially supported by Project "Biotechnologies of novel biomaterials: Innovative Biopolymers and Biomedicine Devices" (Agreement No. 11.G34.31.0013 with Amendment No. 1 of 15 February 2013) in accordance with Resolution No. 220 of the Government of the Russian Federation of April 9, 2010, "On measures designed to attract leading scientists to the Russian institutions of higher learning." The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 1932-6203

РУБ Multidisciplinary Sciences
Рубрики:
RALSTONIA-EUTROPHA
   BIODEGRADABLE POLYHYDROXYALKANOATES
   AEROMONAS-HYDROPHILA
   ESCHERICHIA-COLI
   MOLECULAR-WEIGHT
   SURFACE-ENERGY
   NORTH PACIFIC
   TERPOLYESTER
   BIOSYNTHESIS
   POLY(3-HYDROXYBUTYRATE-CO-3-HYDROXYVALERATE-CO-3-HYDROXYHEXANOATE)
Аннотация: This study investigates kinetic and production parameters of a glucose-utilizing bacterial strain, C. eutrophus B-10646, and its ability to synthesize PHA terpolymers. Optimization of a number of parameters of bacterial culture (cell concentration in the inoculum, physiological activity of the inoculum, determined by the initial intracellular polymer content, and glucose concentration in the culture medium during cultivation) provided cell concentrations and PHA yields reaching 110 g/L and 80%, respectively, under two-stage batch culture conditions. Addition of precursor substrates (valerate, hexanoate, propionate, c-butyrolactone) to the culture medium enabled synthesis of PHA terpolymers, P(3HB/3HV/4HB) and P(3HB/3HV/3HHx), with different composition and different molar fractions of 3HB, 3HV, 4HB, and 3HHx. Different types of PHA terpolymers synthesized by C. eutrophus B-10646 were used to prepare films, whose physicochemical and physicalmechanical properties were investigated. The properties of PHA terpolymers were significantly different from those of the P3HB homopolymer: they had much lower degrees of crystallinity and lower melting points and thermal decomposition temperatures, with the difference between these temperatures remaining practically unchanged. Films prepared from all PHA terpolymers had higher mechanical strength and elasticity than P3HB films. In spite of dissimilar surface structures, all films prepared from PHA terpolymers facilitated attachment and proliferation of mouse fibroblast NIH 3T3 cells more effectively than polystyrene and the highly crystalline P3HB.

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Держатели документа:
[Volova, Tatiana
Kiselev, Evgeniy
Nikolaeva, Elena
Sukovatiy, Aleksey
Shishatskaya, Ekaterina] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
[Volova, Tatiana
Vinogradova, Olga
Shishatskaya, Ekaterina] Siberian Fed Univ, Krasnoyarsk, Russia
[Chistyakov, Anton] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T...; Kiselev, E...; Vinogradova, O...; Nikolaeva, E...; Chistyakov, A...; Sukovatiy, A...; Shishatskaya, E...; Project "Biotechnologies of novel biomaterials: Innovative Biopolymers and Biomedicine Devices" [11.G34.31.0013]

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Model of the active site of firefly luciferase [Text] / T. P. Sandalova, N. N. Ugarova // Biochem.-Moscow. - 1999. - Vol. 64, Is. 8. - P. 962-967. - Cited References: 20 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
ESCHERICHIA-COLI
   SEQUENCE
   CLONING
   ENZYME
   CDNA
   SUPERFAMILY
Кл.слова (ненормированные):
bioluminescence -- firefly luciferase -- ATP -- luciferin -- spatial structure -- active site -- enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Karolinska Inst, S-17177 Stockholm, Sweden
Moscow MV Lomonosov State Univ, Sch Chem, Moscow 119899, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sandalova, T.P.; Ugarova, N.N.

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Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay [Text] / L. A. Frank, A. I. Petunin, E. S. Vysotski // Russ. J. Bioorg. Chem. - 2004. - Vol. 30, Is. 4. - P. 327-331, DOI 10.1023/B:RUBI.0000037257.80835.7a. - Cited References: 16 . - ISSN 1068-1620

РУБ Biochemistry & Molecular Biology + Chemistry, Organic
Рубрики:
ESCHERICHIA-COLI
   PURIFICATION
   AEQUORIN
   PROTEIN
   CDNA
Кл.слова (ненормированные):
bioluminescent immunoassay -- obelin -- thyroid stimulating hormone
Аннотация: An efficient procedure for obelin conjugation with immunoglobulins was developed. The possibility was shown of using the resulting conjugates instead of a radioisotope label for the immunoassay of thyroid stimulating hormone in sera; the conjugates provide a sensitivity of 0.01 muIU/ml. The results of bioluminescent immunoassay (sera of 34 patients) satisfactorily correlate with the results of radioisotope assay (R 0.99).

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
DIAS Ltd, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Petunin, A.I.; Vysotski, E.S.

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Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class [Text] / S. . Bauer [et al.] // J. Mol. Biol. - 2004. - Vol. 339, Is. 4. - P. 967-979, DOI 10.1016/j.jmb.2004.04.034. - Cited References: 66 . - ISSN 0022-2836

РУБ Biochemistry & Molecular Biology
Рубрики:
GTP CYCLOHYDROLASE-I
   GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE
   6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE
   ESCHERICHIA-COLI
   DIHYDRONEOPTERIN ALDOLASE
   FOLIC-ACID
   ENZYMATIC SYNTHESIS
   DIHYDROPTEROATE SYNTHASE
   REACTION-MECHANISM
   3-DIMENSIONAL STRUCTURE
Кл.слова (ненормированные):
tetrahydrofolate biosynthesis -- aldolase classes -- retroaldol reaction -- purin binding -- Schiff base
Аннотация: Dihydroneopterin aldolase (DHNA) catalyses a retroaldol reaction yielding 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin, tetrahydrofolate. The enzyme is a potential target for antimicrobial and anti-parasite chemotherapy. A gene specifying a dihydroneopterin aldolase from Arabidopsis thaliana was expressed in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity and crystallised using polyethylenglycol as the precipitating agent. The crystal structure was solved by X-ray diffraction analysis at 2.2 Angstrom resolution. The enzyme forms a D-4-symmetric homo-octamer. Each polypeptide chain is folded into a single domain comprising an antiparallel four-stranded beta-sheet and two long alpha-helices. Four monomers are arranged in a tetrameric ring, and two of these rings form a hollow cylinder. Well defined purine derivatives are found at all eight topologically equivalent active sites. The subunit fold of the enzyme is related to substructures of dihydroneopterin triphosphate epimerase, GTP cyclohydrolase I, and pyruvoyltetrahydropterin synthase, which are all involved in the biosynthesis of pteridine type cofactors, and to urate oxidase, although some members of that superfamily have no detectable sequence similarity Due to structural and mechanistical differences of DHNA in comparison with class I and class II aldolases, a new aldolase class is proposed. (C) 2004 Elsevier Ltd. All rights reserved.

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Держатели документа:
Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
Tech Univ Munich, Lehrstuhl Organ Chem & Biochem, D-85747 Garching, Germany
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bauer, S...; Schott, A.K.; Illarionova, V...; Bacher, A...; Huber, R...; Fischer, M...

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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786 [Text] / T. G. Volova [et al.] // Appl. Biochem. Microbiol. - 2004. - Vol. 40, Is. 2. - P. 170-177, DOI 10.1023/B:ABIM.0000018921.04863.d5. - Cited References: 27 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
POLY-BETA-HYDROXYBUTYRATE
   ORGANISM ALCALIGENES-EUTROPHUS
   ESCHERICHIA-COLI
   PHB
   POLY(3-HYDROXYBUTYRATE)
   BIOSYNTHESIS
   CLONING
   GENES
   CHAIN
   H16
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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10.

The smallest natural high-active luciferase: Cloning and characterization of novel 16.5-kDa luciferase from copepod Metridia longa [Text] / S. V. Markova [et al.] // Biochem. Biophys. Res. Commun. - 2015. - Vol. 457, Is. 1. - P77-82, DOI 10.1016/j.bbrc.2014.12.082. - Cited References:20. - The cloning of cDNA encoding MLuc7 luciferase of M. longa was supported by Bayer AG (Germany); all other studies - by the grant 14-14-01119 of the Russian Science Foundation. We declare that authors have no conflict of interest. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
   SECRETED LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Mammalian -- expression -- Real-time imaging
Аннотация: Coelenterazine-dependent copepod luciferases containing natural signal peptide for secretion are a very convenient analytical tool as they enable monitoring of intracellular events with high sensitivity, without destroying cells or tissues. This property is well suited for application in biomedical research and development of cell-based assays for high throughput screening. We report the cloning of cDNA gene encoding a novel secreted non-allelic 16.5-kDa isoform (MLuc7) of Metridia longa luciferase, which, in fact, is the smallest natural luciferase of known for today. Despite the small size, isoform contains 10 conservative Cys residues suggesting the presence of up to 5 S-S bonds. This hampers the efficient production of functionally active recombinant luciferase in bacterial expression systems. With the use of the baculovirus expression system, we produced substantial amounts of the proper folded MLuc7 luciferase with a yield of similar to 3 mg/L of a high purity protein. We demonstrate that MLuc7 produced in insect cells is highly active and extremely thermostable, and is well suited as a secreted reporter when expressed in mammalian cells ensuring higher sensitivity of detection as compared to another Metridia luciferase isoform (MLuc164) which is widely employed in real-time imaging. (C) 2014 Elsevier Inc. All rights reserved.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.
ИБФ СО РАН

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Burakova, Ludmila P.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Science Foundation [14-14-01119]

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11.

The disulfide-rich Metridia luciferase refolded from E. coli inclusion bodies reveals the properties of a native folded enzyme produced in insect cells / S. V. Markova [et al.] // J. Photochem. Photobiol. B-Biol. - 2017. - Vol. 175. - P51-57, DOI 10.1016/j.jphotobiol.2017.08.024. - Cited References:30. - These studies were funded by RFBR and the Government of Krasnoyarsk Territory according to the research project No. 16-44-242099 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 0356-2016-0712). . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GAUSSIA-PRINCEPS LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
   PROTEIN
Кл.слова (ненормированные):
Copepod luciferase -- Disulfide bonds -- Cysteine-rich protein -- Oxidative -- refolding
Аннотация: The bioluminescence of a marine copepod Metridia Tonga is determined by a small secreted coelenterazine-dependent luciferase that uses coelenterazine as a substrate of enzymatic reaction to generate light (lambda(max) = 480 nm). To date, four different isoforms of the luciferase differing in size, sequences, and properties have been cloned by functional screening. All of them contain ten conserved Cys residues that suggests up to five S-S intramolecular bonds per luciferase molecule. Whereas the use of copepod luciferases as bioluminescent reporters in biomedical research in vivo is growing from year to year, their application for in vitro assays is still limited by the difficulty in obtaining significant amounts of luciferase. The most cost-effective host for producing recombinant proteins is Escherichia coli. However, prokaryotic and eukaryotic cells maintain the reductive environment in cytoplasm that hinders the disulfide bond formation and consequently the proper folding of luciferase. Here we report the expression of the MLuc7 isoform of M. longa luciferase in E. colt cells and the efficient procedure for refolding from inclusion bodies yielding a high-active monomeric protein. Furthermore, in a set of identical experiments we demonstrate that bioluminescent and structural features of MLuc7 produced in bacterial cells are identical to those of MLuc7 isoform produced from culture medium of insect cells. Although the yield of high-purity protein is only 6 mg/L, the application of E. coil cells to produce the luciferase is simpler and more cost-effective than the use of insect cells. We expect that the suggested technology of Metridia luciferase production allows obtaining of sufficient amounts of protein both for the development of novel in vitro analytical assays with the use of MLuc7 as a label and for structural studies.

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Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Fed Res Ctr, Photobiol Lab,Inst Biophys SB, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Gorbunova, Darya A.; Vysotski, Eugene S.; RFBR; Government of Krasnoyarsk Territory [16-44-242099]; Russian Academy of Sciences [0356-2016-0712]

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12.

Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria / A. A. Deeva [et al.] // Proteins. - 2019. - Vol. 87, Is. 9. - P723-729, DOI 10.1002/prot.25696. - Cited References:39. - The Russian Foundation for Basic Research and Krasnoyarsk Region Science and Technology Support Fund, Grant/Award Number: 18-44-243009; Ministry of Education and Science of the Russian Federation, Grant/Award Numbers: 0356-2019-0019, 6.7734.2017 . - ISSN 0887-3585. - ISSN 1097-0134

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ESCHERICHIA-COLI
FLAVIN OXIDOREDUCTASE
CRYSTAL-STRUCTURE
Кл.слова (ненормированные):
bacterial bioluminescence -- Fre -- functional divergence -- gene duplication -- LuxG -- NAD(P)H -- flavin-oxidoreductase
Аннотация: In luminous bacteria NAD(P)H:flavin-oxidoreductases LuxG and Fre, there are homologous enzymes that could provide a luciferase with reduced flavin. Although Fre functions as a housekeeping enzyme, LuxG appears to be a source of reduced flavin for bioluminescence as it is transcribed together with luciferase. This study is aimed at providing the basic conception of Fre and LuxG evolution and revealing the peculiarities of the active site structure resulted from a functional variation within the oxidoreductase family. A phylogenetic analysis has demonstrated that Fre and LuxG oxidoreductases have evolved separately after the gene duplication event, and consequently, they have acquired changes in the conservation of functionally related sites. Namely, different evolutionary rates have been observed at the site responsible for specificity to flavin substrate (Arg 46). Also, Tyr 72 forming a part of a mobile loop involved in FAD binding has been found to be conserved among Fre in contrast to LuxG oxidoreductases. The conservation of different amino acid types in NAD(P)H binding site has been defined for Fre (arginine) and LuxG (proline) oxidoreductases.

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Держатели документа:
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Svobodny Prosp 79, Krasnoyarsk 660041, Russia.
RAS, Inst Cell Biophys, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia.
State Inst Informat Technol & Telecommun SIIT & T, Dept Appl Res Informatizat, Moscow, Russia.
RAS, Fed Res Ctr, Krasnoyarsk Sci Ctr SB, Lab Photobiol,Inst Biophys SB, Krasnoyarsk, Russia.

Доп.точки доступа:
Deeva, Anna A.; Zykova, Evgenia A.; Nemtseva, Elena V.; Kratasyuk, Valentina A.; Nemtseva, Elena; Russian Foundation for Basic Research [18-44-243009]; Ministry of Education and Science of the Russian Federation [0356-2019-0019, 6.7734.2017]; Krasnoyarsk Region Science and Technology [18-44-243009]

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13.

Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system / D. Chang, Y. K. Liu, Y. Y. Chen [et al.] // BMC Vet. Res. - 2020. - Vol. 16, Is. 1. - Ст. 202, DOI 10.1186/s12917-020-02422-3. - Cited References:30. - This work was financially supported by the National Natural Science Foundation of China (No. 31870917), The program for Innovative Research Team of Science and Technology in University of Henan Province (No. 20IRTSTHN024) and Key Scientific Research Projects of Colleges and Universities in Henan Province of China (No. 18B230008). The funding bodies played no role in the design of the study, the collection, analysis, and interpretation of data and in writing the manuscript. . - ISSN 1746-6148

РУБ Veterinary Sciences
Рубрики:
VIRUS-LIKE PARTICLES
   ESCHERICHIA-COLI
   GENETIC-ANALYSIS
   CPV-VP2
Кл.слова (ненормированные):
Canine parvovirus -- VP2 protein -- Baculovirus expression system
Аннотация: Background Canine parvovirus (CPV) is now recognized as a serious threat to the dog breeding industry worldwide. Currently used CPV vaccines all have their specific drawbacks, prompting a search for alternative safe and effective vaccination strategies such as subunit vaccine. VP2 protein is the major antigen targeted for developing CPV subunit vaccine, however, its production in baculovirus expression system remains challenging due to the insufficient yield. Therefore, our study aims to increase the VP2 protein production by using an improved baculovirus expression system and to evaluate the immunogenicity of the purified VP2 protein in mice. Results The results showed that high-level expression of the full length VP2 protein was achieved using our modified baculovirus expression system. The recombinant virus carrying two copies of VP2 gene showed the highest expression level, with a productivity of 186 mg/L, which is about 1.4-1.6 fold that of the recombinant viruses carrying only one copy. The purified protein reacted with Mouse anti-His tag monoclonal antibody and Rabbit anti-VP2 polyclonal antibody. BALB/c mice were intramuscularly immunized with purified VP2 protein twice at 2 week intervals. After vaccination, VP2 protein could induce the mice produce high level of hemagglutination inhibition antibodies. Conclusions Full length CPV VP2 protein was expressed at high level and purified efficiently. Moreover, it stimulated mice to produce high level of antibodies with hemmaglutination inhibition properties. The VP2 protein expressed in this study could be used as a putative economic and efficient subunit vaccine against CPV infection.

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Держатели документа:
Nanyang Normal Univ, Sch Agr Engn, Henan Provincal Engn & Technol Ctr Hlth Prod Live, Nanyang 473061, Peoples R China.
Nanyang Normal Univ, Sch Agr Engn, Key Lab Ecol Secur, Nanyang 473061, Peoples R China.
Nanyang Normal Univ, Sch Agr Engn, Collaborat Innovat Ctr Water Secur Water Source R, Nanyang 473061, Peoples R China.
Russian Acad Sci, Fed Res Ctr, Krasnoyarsk Sci Ctr, Inst Biophys,Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Chang, Dao; Liu, Yangkun; Chen, Yangyang; Hu, Xiaomin; Burov, Andrey; Puzyr, Alexey; Bondar, Vladimir; Yao, Lunguang; National Natural Science Foundation of ChinaNational Natural Science Foundation of China [31870917]; program for Innovative Research Team of Science and Technology in University of Henan Province [20IRTSTHN024]; Key Scientific Research Projects of Colleges and Universities in Henan Province of China [18B230008]

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