Search Results - "рекомбинантный штамм"

1

Academic Journal

Heterologous expression of diadenylate cyclase in the form of inclusion bodies with enzymatic activity ; Гетерологичная экспрессия диаденилатциклазы в виде телец включения, обладающих ферментативной активностью

Authors: M. A. Vinter, I. S. Kazlouski, A. I. Zinchenko, М. А. Винтер, И. С. Казловский, А. И. Зинченко

Source: Doklady of the National Academy of Sciences of Belarus; Том 66, № 5 (2022); 509-516 ; Доклады Национальной академии наук Беларуси; Том 66, № 5 (2022); 509-516 ; 2524-2431 ; 1561-8323 ; 10.29235/1561-8323-2022-66-5

Subject Terms: цикло-ди-АМФ, genetic engineering, recombinant strain, Bacillus thuringiensis, heterologous gene expression, inclusion bodies, diadenylate cyclase, cyclo-di-AMP, генная инженерия, рекомбинантный штамм, гетерологичная экспрессия гена, тельца включения, диаденилатциклаза

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Relation: https://doklady.belnauka.by/jour/article/view/1090/1093; A decade of research on the second messenger c-di-AMP / W. Yin [et al.] // FEMS Microbiol. Rev. – 2020. – Vol. 44, N 6. – P. 701–724. https://doi.org/10.1093/femsre/fuaa019; Intranasal delivery of influenza rNP adjuvanted with c-di-AMP induces strong humoral and cellular immune responses and provides protection against virus challenge / M. V. Sanchez [et al.] // PLoS ONE. – 2014. – Vol. 9, N 8. – Art. e104824. https://doi.org/10.1371/journal.pone.0104824; Cyclic di-adenosine monophosphate: a promising adjuvant candidate for the development of neonatal vaccines / D. Lirussi [et al.] // Pharmaceutics. – 2021. – Vol. 13, N 2. – Art. 188. https://doi.org/10.3390/ pharmaceutics13020188; Yan, H. The Promise and challenges of cyclic dinucleotides as molecular adjuvants for vaccine development / H. Yan, W. Chen // Vaccines. – 2021. – Vol. 9, N 8. – Art. 917. https://doi.org/10.3390/vaccines9080917; Chemical synthesis, purification, and characterization of 3′-5′-linked canonical cyclic dinucleotides (CDNs) / C. Wang [et al.] // Meth. Enzymol. – 2019. – Vol. 625. – P. 41−59. https://doi.org/10.1016/bs.mie.2019.04.022; Villaverde, A. Protein aggregation in recombinant bacteria: Biological role of inclusion bodies / A. Villaverde, M. M. Carrio // Biotechnol. Lett. – 2003. – Vol. 25, N 17. – P. 1385–1395. https://doi.org/10.1023/a:1025024104862; Schramm, F. D. Protein aggregation in bacteria / F. D. Schramm, K. Schroeder, K. Jonas // FEMS Microbiol. Rev. – 2020. – Vol. 44, N 1. – P. 54–72. https://doi.org/10.1093/femsre/fuz026; Enzymatic synthesis of 2′-ara and 2′-deoxy analogues of c-di-GMP / A. S. Shchokolova [et al.] // Nucleos. Nucleot. Nucl. Acids. – 2015. – Vol. 34, N 6. – P. 416–423. https://doi.org/10.1080/15257770.2015.1006775; Thermostable adenosine 5′-monophosphate phosphorylase from Thermococcus kodakarensis forms catalytically active inclusion bodies / S. Kamel [et al.] // Sci. Rep. – 2021. – Vol. 11, N 1. – Art. 16880. https://doi.org/10.1038/s41598- 021-96073-5; Re-engineered BCG overexpressing cyclic di-AMP augments trained immunity and exhibits improved efficacy against bladder cancer / A. K. Singh [et al.] // Nat. Commun. – 2022. – Vol. 13, N 1. – Art. 878. https://doi.org/10.1038/s41467- 022-28509-z; Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth / F. M. Mehne [et al.] // J. Biol. Chem. – 2013. – Vol. 288, N 3. – P. 2004–2017. https://doi.org/10.1074/jbc. m112.395491; Создание рекомбинантного штамма Escherichia coli – продуцента диаденилатциклазы и ее использование для синтеза цикло-ди-АМФ / И. С. Казловский [и др.] // Вес. Нац. акад. навук Беларусi. Сер. бiял. навук. – 2015. – № 4. – С. 51–55.; Green, M. R. Molecular cloning. A laboratory manual. 4th ed. / M. R. Green, J. Sambrook. – New York, 2012. – 630 p.; Quan, J. Circular polymerase extension cloning of complex gene libraries and pathways / J. Quan, J. Tian // PLoS ONE. – 2009. – Vol. 4, N 7. – Art. e6441. https://doi.org/10.1371/journal.pone.0006441; Challenges associated with the formation of recombinant protein inclusion bodies in Escherichia coli and strategies to address them for industrial applications / A. Bhatwa [et al.] // Front. Bioeng. Biotechnol. – 2021. – Vol. 9. – Art. 630551. https:// doi.org/10.3389/fbioe.2021.630551; https://doklady.belnauka.by/jour/article/view/1090

Availability: https://doklady.belnauka.by/jour/article/view/1090
https://doi.org/10.29235/1561-8323-2022-66-5-509-516

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2

Academic Journal

Construction of the recombinant Escherichia coli strain producing a homologous thermolabile toxin subunit ; Создание рекомбинантного штамма Escherichia coli, продуцирующего субъединицу гомологичного термолабильного токсина

Authors: I. S. Kazlouski, A. I. Zinchenko, A. V. Solovyeva, O. N. Novikova, Yu. V. Lomako, И. С. Казловский, А. И. Зинченко, А. В. Соловьева, О. Н. Новикова, Ю. В. Ломако

Source: Doklady of the National Academy of Sciences of Belarus; Том 65, № 2 (2021); 185-190 ; Доклады Национальной академии наук Беларуси; Том 65, № 2 (2021); 185-190 ; 2524-2431 ; 1561-8323 ; 10.29235/1561-8323-2021-65-2

Subject Terms: рекомбинантный штамм, thermolabile toxin, colibacteriosis, genetic engineering, recombinant strain, термолабильный токсин, колибактериоз, генная инженерия

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Relation: https://doklady.belnauka.by/jour/article/view/961/958; Characterization of heat-labile toxin-subunit B from Escherichia coli by liquid chromatography-electrospray ionization-mass spectrometry and matrix-assisted laser desorption/ionization time-of-ﬂight mass spectrometry / I. Sospedra [et al.] // Food Chem. Toxicol. – 2012. – Vol. 50, N 11. – P. 3886–3891. https://doi.org/10.1016/j.fct.2012.08.014; Review of newly identiﬁed functions associated with the heat-labile toxin of enterotoxigenic Escherichia coli / Q. Duan [et al.] // Front. Cell. Infect. Microbiol. – 2019. – Vol. 9. – Art. 292. https://doi.org/10.3389/fcimb.2019.00292; Expression of Escherichia coli heat-labile enterotoxin B subunit in Centella (Centella Asiatica (L.) Urban) via biolistic transformation / N. H. Loc [et al.] // Curr. Pharm. Biotechnol. – 2020. – Vol. 21, N 10. – P. 973–979. https://doi.org/10.2174/138 9201021666200226094150; Hur, J. Ontology-based literature mining of E. coli vaccine-associated gene interaction networks / J. Hur, A. Ozgur, Y. He // J. Biomed. Semantics. – 2017. – Vol. 8, N 1. – Art. 12. https://doi.org/10.1186/s13326-017-0122-4; Th1-biased immunoadjuvant effect of the recombinant B subunit of an Escherichia coli heat-labile enterotoxin on an inactivated porcine reproductive and respiratory syndrome virus antigen via intranasal immunization in mice / F. Su [et al.] // J. Vet. Med. Sci. – 2019. – Vol. 81, N 10. – P. 1475–1484. https://doi.org/10.1292/jvms.19-0057; Hur, J. A 2018 workshop: vaccine and drug ontology studies (VDOS 2018) / J. Hur, C. Tao, y. He // BMC Bioinformatics. – 2019. – Vol. 20, N 21. – Art. 705. https://doi.org/10.1186/s12859-019-3191-9; Quan, J. Circular polymerase extension cloning of complex gene libraries and pathways / J. Quan, J. Tian // PLoS ONE. – 2009. – Vol. 4, N 7. – Art. e6441. https://doi.org/10.1371/journal.pone.0006441; Immunization with recombinant fusion of LTB and linear epitope (40–62) of epsilon toxin elicits protective immune response against the epsilon toxin of Clostridium perfringens type D / H. Kaushik [et al.] // AMB Expr. – 2019. – Vol. 9, N 1. – P. 105–116. https://doi.org/10.1186/s13568-019-0824-3; Secretory Expression and Puriﬁcation of Recombinant Escherichia coli Heat-Labile Enterotoxin B Subunit and its Applications on Intranasal Vaccination of Hantavirus / S. Cao [et al.] // Mol. Biotechnol. – 2009. – Vol. 41, N 2. – P. 91–98. https://doi.org/10.1007/s12033-008-9101-4; Effcient extracellular production of recombinant Escherichia coli heat-labile enterotoxin B subunit by using the expression/secretion system of Bacillus brevis and its mucosal immunoadjuvanticity / S. Kozuka [et al.] // Vaccine. – 2000. – Vol. 18, N 17. – P. 1730–1737. https://doi.org/10.1016/s0264-410x(99)00547-2; https://doklady.belnauka.by/jour/article/view/961