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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryavtsev A. N., Burakova L. P., Barinova K. A., Frank L. A.
Заглавие : A test system for tick-borne encephalitis virus detection based on bioluminescent immunoassay
Место публикации : J. Sib. Fed. Univ. - Biol.: Siberian Federal University, 2020. - Vol. 13, Is. 3. - С. 310-321. - ISSN 19971389 (ISSN), DOI 10.17516/1997-1389-0296
Аннотация: The tick-borne encephalitis virus (TBEV) is the causative agent of one of the most severe human neuroinfections. The infection transmitted by ixodid ticks is spread throughout the forest and forest-steppe zones of the temperate climatic belt of the Eurasian continent, including the Siberian region of the Russian Federation. Despite the availability of commercial analytical systems for the detection of TBEV, the task of developing approaches to a quick and reliable analysis that can be performed routinely, particularly in environmental studies, remains topical. A solid-phase bioluminescent immunoassay for determining the tick-borne encephalitis virus (TBEV) in ticks was developed. The assay is based on the hybrid protein consisting of a modified thermostable version of Renilla muelleri luciferase and a single-chain mini-antibody to protein E. This unique protein had been obtained and investigated by the authors earlier. The current study describes the expression of the hybrid protein in two different strains of recombinant E. coli cells. The optimal conditions for obtaining a highly purified protein were found. The bioluminescent reaction of the luciferase domain was triggered with the help of the stable natural form of the substrate, a Ca-dependent coelenterazine-binding protein, the recombinant variant of which was obtained by the authors. The conditions for production and storage of the immunoassay components (the hybrid protein, the stable form of the luciferase substrate, and activated microplates) were determined. Using the developed test system, more than 900 tick samples were analyzed for TBEV. In terms of sensitivity (89.5%) and specificity (98.9%), the proposed method is not inferior to colorimetric detection and is much simpler and faster than the latter. © Siberian Federal University. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Yu M., Benjamin M. M., Srinivasan S., Morin E. E., Shishatskaya E. I., Schwendeman S. P., Schwendeman A.
Заглавие : Battle of GLP-1 delivery technologies
Место публикации : Adv. Drug Deliv. Rev.: Elsevier B.V., 2018. - ISSN 0169409X (ISSN) , DOI 10.1016/j.addr.2018.07.009
Ключевые слова (''Своб.индексиров.''): albumin fusion--exenatide--fatty acid conjugate--fc fusion--glp-1 receptor agonist--half-life--peptide delivery--pharmacokinetics
Аннотация: Glucagon-like peptide-1 receptor agonists (GLP-1 RAs) belong to an important therapeutic class for treatment of type 2 diabetes. Six GLP-1 RAs, each utilizing a unique drug delivery strategy, are now approved by the Food and Drug Administration (FDA) and additional, novel GLP-1 RAs are still under development, making for a crowded marketplace and fierce competition among the manufacturers of these products. As rapid elimination is a major challenge for clinical application of GLP-1 RAs, various half-life extension strategies have been successfully employed including sequential modification, attachment of fatty-acid to peptide, fusion with human serum albumin, fusion with the fragment crystallizable (Fc) region of a monoclonal antibody, sustained drug delivery systems, and PEGylation. In this review, we discuss the scientific rationale of the various half-life extension strategies used for GLP-1 RA development. By analyzing and comparing different approved GLP-1 RAs and those in development, we focus on assessing how half-life extending strategies impact the pharmacokinetics, pharmacodynamics, safety, patient usability and ultimately, the commercial success of GLP-1 RA products. We also anticipate future GLP-1 RA development trends. Since similar drug delivery strategies are also applied for developing other therapeutic peptides, we expect this case study of GLP-1 RAs will provide generalizable concepts for the rational design of therapeutic peptides products with extended duration of action. © 2018 Elsevier B.V.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova, Ludmila P., Kudryavtsev, Alexander N., Stepanyuk, Galina A., Baykov, Ivan K., Morozova, Vera V., Tikunova, Nina V., Dubova, Maria A., Lyapustin, Victor N., Yakimenko, Valeri V., Frank, Ludmila A.
Заглавие : Bioluminescent detection probe for tick-borne encephalitis virus immunoassay
Колич.характеристики :7 с
Коллективы : Russian Academy of Sciences, Siberian Branch [139], Russian Academy of Sciences [VI 57.1.1]
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2015. - Vol. 407, Is. 18. - С. 5417-5423. - ISSN 1618-2642, DOI 10.1007/s00216-015-8710-6. - ISSN 1618-2650(eISSN)
Примечания : Cited References:19. - The work was supported by the Russian Academy of Sciences, Siberian Branch, within the framework of the Interdisciplinary Integration Project No. 139 and the State budget allocated to the fundamental research at the Russian Academy of Sciences (project No. VI 57.1.1).
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
ENZYME-IMMUNOASSAY
RENILLA-MUELLERI
Ключевые слова (''Своб.индексиров.''): tick-borne encephalitis virus--single-chain antibody--luciferase--immunoassay
Аннотация: To facilitate the detection of the tick-borne encephalitis virus (TBEV), the causative agent of one of the most severe human neuroinfections, we have developed an immunoassay based on bioluminescent hybrid protein 14D5a-Rm7 as a detection probe. The protein containing Renilla luciferase as a reporter and a single-chain variable fragment (scFv) of murine immunoglobulin to TBEV as a recognition element was constructed, produced by bacterial expression, purified, and tested. Both domains were shown to reveal their specific biological properties-affinity to the target antigen and bioluminescent activity. Hybrid protein was applied as a label for solid-phase immunoassay of the antigens, associated with the tick-borne encephalitis virus (native glycoprotein E or extracts of the infected strain of lab ticks). The assay demonstrates high sensitivity (0.056 ng of glycoprotein E; 10(4)-10(5) virus particles or 0.1 pg virions) and simplicity and is competitive with conventional methods for detection of TBEV.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L..., Markova S..., Remmel N..., Vysotski E..., Gitelson I...
Заглавие : Bioluminescent signal system: bioluminescence immunoassay of pathogenic organisms
Колич.характеристики :6 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2007. - Vol. 22, Is. 3. - С. 215-220. - ISSN 1522-7235, DOI 10.1002/bio.952
Примечания : Cited References: 14
Предметные рубрики: AEQUORIN
AGENTS
OBELIN
ASSAYS
LABEL
Ключевые слова (''Своб.индексиров.''): obelin--bioluminescence immunoassay--infective agents
Аннотация: The Ca2+-regulated photoprotein obelin has been examined as a label for bioluminescence immunoassay of infective agents. The hepatitis B virus (HbsAg) and the bacteria Escherichia coli and Shigella sonnei lipopolysaccharide (LPS) were chosen as model antigens. Chemically synthesized obelin-corresponding antibody conjugates were used in a solid-phase microplate immunoassay. The sensitivities achieved by the assay were 0.25 ng/mL for S. sonnei LPS and 0.375 ng/mL for HbsAg. A novel, filter-based immunoassay to determine bacterial admixtures in the environment was proposed. The NanoCeram filters were effectively applied to 'trap' and pre-concentrate pathogens from samples under study for the purposes of further detection and measurement of the absorbed material by bioluminescence immunoassay. Copyright (C) 2007 John Wiley & Sons, Ltd.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Purtov K.V., Petunin A.I., Burov A.E., Puzyr A.P., Bondar V.S.
Заглавие : Nanodiamonds as Carriers for Address Delivery of Biologically Active Substances
Колич.характеристики :6 с
Коллективы :
Место публикации : Nanoscale Res. Lett.: SPRINGER, 2010. - Vol. 5, Is. 3. - С. 631-636. - ISSN 1931-7573, DOI 10.1007/s11671-010-9526-0
Примечания : Cited References: 24. - This work was supported by the Program # 27 for Basic Research of the Presidium of RAS (project 3.6.3).
Предметные рубрики: ANTICANCER DRUGS
NANOPARTICLES
ADSORPTION
PARTICLES
PROTEINS
Ключевые слова (''Своб.индексиров.''): nanodiamonds--ligand--protein immobilization--nanocarrier--targeted delivery
Аннотация: Surface of detonation nanodiamonds was functionalized for the covalent attachment of immunoglobulin, and simultaneously bovine serum albumin and Rabbit Anti-Mouse Antibody. The nanodiamond-IgG(I125) and RAM-nanodiamond-BSA(I125) complexes are stable in blood serum and the immobilized proteins retain their biological activity. It was shown that the RAM-nanodiamond-BSA(I125) complex is able to bind to the target antigen immobilized on the Sepharose 6B matrix through antibody-antigen interaction. The idea can be extended to use nanodiamonds as carriers for delivery of bioactive substances (i.e., drugs) to various targets in vivo.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ovchinnikova T.M., Savchenko A.A., Sukhovol'skii V.G., Khlebopros R.G.
Заглавие : Structural and temporal links between the components of humoral immunity.
Место публикации : Doklady Biochemistry. - 2000. - Vol. 374, Is. 1-6. - С. 186-188. - ISSN 00124958 (ISSN)
Ключевые слова (''Своб.индексиров.''): immunoglobulin a--immunoglobulin d--immunoglobulin g--immunoglobulin m--antibody production--article--biological model--blood--herpes simplex--human--immunology--physiology--regression analysis--antibody formation--herpes simplex--humans--immunoglobulin a--immunoglobulin d--immunoglobulin g--immunoglobulin m--models, immunological--regression analysis
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Chang, Dao, Liu, Yangkun, Chen, Yangyang, Hu, Xiaomin, Burov, Andrey, Puzyr, Alexey, Bondar, Vladimir, Yao, Lunguang
Заглавие : Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system
Колич.характеристики :9 с
Коллективы : 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]
Место публикации : BMC Vet. Res.: BMC, 2020. - Vol. 16, Is. 1. - Ст.202. - ISSN 1746-6148(eISSN), DOI 10.1186/s12917-020-02422-3
Примечания : 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.
Предметные рубрики: VIRUS-LIKE PARTICLES
ESCHERICHIA-COLI
GENETIC-ANALYSIS
CPV-VP2
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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Chang D., Liu Y., Chen Y., Hu X., Burov A., Puzyr A., Bondar V., Yao L.
Заглавие : Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system
Место публикации : BMC Vet. Res.: BioMed Central Ltd., 2020. - Vol. 16, Is. 1. - Ст.202. - ISSN 17466148 (ISSN), DOI 10.1186/s12917-020-02422-3
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. © 2020 The Author(s).
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova M. D., Markova S. V., Tikunova N. V., Vysotski E. S.
Заглавие : The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 14. - Ст.4971. - С. 1-16. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21144971
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepod Metridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N-or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (KD = 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (KD = 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform of M. longa luciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana, V, Tikunova, Nina, V, Vysotski, Eugene S.
Заглавие : The Smallest Isoform ofMetridia longaLuciferase as a Fusion Partner for Hybrid Proteins
Колич.характеристики :16 с
Коллективы : Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; ICBFM SB RAS [AAAA-A17-117020210027-9]; Government of Krasnoyarsk Territory
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 14. - Ст.4971. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21144971
Примечания : Cited References:49. - The reported study was funded by the Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (S.V.M, M.D.L., and E.S.V.) and by the Russian State funded budget project of ICBFM SB RAS No. AAAA-A17-117020210027-9 (N.V.T.).
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
BIOLUMINESCENT REPORTER
GAUSSIA
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepodMetridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N- or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (K-D= 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (K-D= 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform ofM. longaluciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins.
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