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Journal articles on the topic 'Recombinant protein'

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Published: 4 June 2021
Last updated: 10 March 2023

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1

Astuti, R. W., N. Wijayanti, and A. Haryanto. "Expression of Recombinant Fusion Protein from Local Isolate of Newcastle Disease Virus and Antibody Response to Recombinant Fusion Protein in Broiler Chickens Post-Vaccination." Journal of the Indonesian Tropical Animal Agriculture 45, no. 2 (May 15, 2020): 78–90. http://dx.doi.org/10.14710/jitaa.45.2.78-90.

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This research aimed to express and purify the recombinant Fusion (F) protein of Newcastle Disease Virus (NDV) from a local isolate in Galur, Kulon Progo, Indonesia (0663/04/2013) from recombinant vector plasmid pBT7-N-His F, and to study the antibody response in the broiler sera which were injected with pure recombinant F protein compared with treated broilers that were vaccinated with commercial inactive NDV vaccines and control broilers without vaccination. The results showed that the recombinant F protein of NDV was successfully expressed, purified and visualized by SDS-PAGE with Coomassie Brilliant Blue staining and Westernblotting methods as a specific recombinant F protein with a molecular weight of 28 kDa. The pure recombinant F protein then was injected into broilers to determine the antibody response in broiler serum. Indirect ELISA showed that the production of antibodies was high in F protein vaccinated groups in comparison with other treated and control groups. The recombinant F protein has potential to be developed as a recombinant vaccine candidate after truncating the 6x His-tag part to obtain higher antibody respond if compared with antibody production in broiler serum post vaccinated with some commercially available broiler vaccines.
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Kim, Yoo-Gon, Woo-Jong Lee, Chan-Hee Won, Yong-Hee Kim, Ji-Sun Yun, Min-Seon Hong, and Chul-Soo Shin. "A study on short-term stability of recombinant protein A." Analytical Science and Technology 24, no. 3 (June 25, 2011): 193–99. http://dx.doi.org/10.5806/ast.2011.24.3.193.

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3

Lewis, Peter. "Recombinant protein drugs." British Journal of Clinical Pharmacology 53, no. 4 (April 2002): 411. http://dx.doi.org/10.1046/j.1365-2125.2002.01571.x.

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4

Ferrari, Luca, and Stefan G. D. Rüdiger. "Recombinant production and purification of the human protein Tau." Protein Engineering, Design and Selection 31, no. 12 (December 1, 2018): 447–55. http://dx.doi.org/10.1093/protein/gzz010.

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Abstract Tau protein is a microtubule-stabilising protein whose aggregation is linked to Alzheimer’s Disease and other forms of dementia. Tau biology is at the heart of cytoskeletal dynamics and neurodegenerative mechanisms, making it a crucial protein to study. Tau purification, however, is challenging as Tau is disordered, which makes it difficult to produce in recombinant system and is degradation-prone. It is thus challenging to obtain pure and stable preparations of Tau. Here, we present a fast and robust protocol to purify Tau recombinantly in Escherichia coli. Our protocol allows purifying Tau either tag-less or FLAG-tagged at its N-terminus, and Tau fragments of interest. By exploiting a cleavable affinity tag and two anion exchange columns, we obtained Tau preparations of high purity, stable and suitable for in vitro studies, including aggregation experiments that resemble neurodegenerative processes.
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Rodrigues, M., S. Li, K. Murata, D. Rodriguez, J. R. Rodriguez, I. Bacik, J. R. Bennink, J. W. Yewdell, A. Garcia-Sastre, and R. S. Nussenzweig. "Influenza and vaccinia viruses expressing malaria CD8+ T and B cell epitopes. Comparison of their immunogenicity and capacity to induce protective immunity." Journal of Immunology 153, no. 10 (November 15, 1994): 4636–48. http://dx.doi.org/10.4049/jimmunol.153.10.4636.

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Abstract We compared the effectiveness of several recombinant influenza and vaccinia viruses to induce a malaria-specific immune response. The CD8+ T cell epitope of the circumsporozoite (CS) protein of Plasmodium yoelii, a rodent malaria parasite, was expressed in two distinct influenza virus proteins, the hemagglutinin and the neuraminidase. These recombinant viruses were found to be equally efficient at inducing CS-specific CD8+ T cells in mice. A third recombinant virus, which expresses a B cell epitope of the CS protein, induced neutralizing anti-sporozoite Abs. Expression in the same recombinant virus of the CD8+ T cell epitope and of the B cell epitope did not impair the capacity of this recombinant virus to induce malaria-specific CD8+ T cells and neutralizing Abs. The immunogenicity of a vaccinia virus, expressing the entire CS protein, was compared with that of a highly attenuated vaccinia strain expressing the same protein and with that of another vaccinia virus expressing only the CD8+ T cell epitope. All three vaccinia virus recombinants elicited CS-specific CD8+ cells and a potent inhibitory response against pre-erythrocytic stages of malaria parasites. Optimal levels of anti-sporozoite Abs, inhibition of liver stage development, and protection against malaria infection resulted from repeatedly immunizing the animals with recombinant influenza viruses followed by boosters with a recombinant vaccinia virus. These findings support the concept that live viral vectors expressing the appropriate proteins and/or epitopes can be used as promising vaccine candidates.
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Llompart, Blanca, Immaculada Llop-Tous, Pablo Marzabal, Margarita Torrent, Roser Pallissé, Miriam Bastida, M. Dolors Ludevid, and Fabien Walas. "Protein production from recombinant protein bodies." Process Biochemistry 45, no. 11 (November 2010): 1816–20. http://dx.doi.org/10.1016/j.procbio.2010.01.016.

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7

Lobb, Leslie, Boguslaw Stec, Evan K. Kantrowitz, Akihito Yamano, Vivian Stojanoff, Ofer Markman, and Martha M. Teeter. "Expression, purification and characterization of recombinant crambin." "Protein Engineering, Design and Selection" 9, no. 12 (1996): 1233–39. http://dx.doi.org/10.1093/protein/9.12.1233.

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8

Ohtake, Satoshi, and Tsutomu Arakawa. "Recombinant Therapeutic Protein Vaccines." Protein & Peptide Letters 20, no. 12 (November 2013): 1324–44. http://dx.doi.org/10.2174/092986652012131112122245.

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9

Fuerst, Walter. "Recombinant Activated Protein C." Critical Care Medicine 32, no. 1 (January 2004): 311–12. http://dx.doi.org/10.1097/01.ccm.0000104932.57061.ad.

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10

Stein, M.D.,, Richard A. "Recombinant Protein Expression Advances." Genetic Engineering & Biotechnology News 31, no. 16 (September 15, 2011): 34–36. http://dx.doi.org/10.1089/gen.31.16.14.

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11

Bill, Roslyn M., Alan D. Goddard, and Alice J. Rothnie. "Recombinant Membrane Protein Methods." Methods 147 (September 2018): 1–2. http://dx.doi.org/10.1016/j.ymeth.2018.08.007.

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12

Tuan, Rocky S. "RECOMBINANT GENE EXPRESSION PROTOCOLS AND RECOMBINANT PROTEIN PROTOCOLS." Shock 8, no. 4 (October 1997): 311. http://dx.doi.org/10.1097/00024382-199710000-00013.

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13

Oulton, Tate, Joshua Obiero, Isabel Rodriguez, Isaac Ssewanyana, Rebecca A. Dabbs, Christine M. Bachman, Bryan Greenhouse, et al. "Plasmodium falciparum serology: A comparison of two protein production methods for analysis of antibody responses by protein microarray." PLOS ONE 17, no. 8 (August 29, 2022): e0273106. http://dx.doi.org/10.1371/journal.pone.0273106.

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The evaluation of protein antigens as putative serologic biomarkers of infection has increasingly shifted to high-throughput, multiplex approaches such as the protein microarray. In vitro transcription/translation (IVTT) systems–a similarly high-throughput protein expression method–are already widely utilised in the production of protein microarrays, though purified recombinant proteins derived from more traditional whole cell based expression systems also play an important role in biomarker characterisation. Here we have performed a side-by-side comparison of antigen-matched protein targets from an IVTT and purified recombinant system, on the same protein microarray. The magnitude and range of antibody responses to purified recombinants was found to be greater than that of IVTT proteins, and responses between targets from different expression systems did not clearly correlate. However, responses between amino acid sequence-matched targets from each expression system were more closely correlated. Despite the lack of a clear correlation between antigen-matched targets produced in each expression system, our data indicate that protein microarrays produced using either method can be used confidently, in a context dependent manner, though care should be taken when comparing data derived from contrasting approaches.
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14

Schönherr, Robert, Janine Mia Rudolph, and Lars Redecke. "Protein crystallization in living cells." Biological Chemistry 399, no. 7 (June 27, 2018): 751–72. http://dx.doi.org/10.1515/hsz-2018-0158.

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AbstractProtein crystallization in living cells has been observed surprisingly often as a native assembly process during the past decades, and emerging evidence indicates that this phenomenon is also accessible for recombinant proteins. But only recently the advent of high-brilliance synchrotron sources, X-ray free-electron lasers, and improved serial data collection strategies has allowed the use of these micrometer-sized crystals for structural biology. Thus,in cellulocrystallization could offer exciting new possibilities for proteins that do not crystallize applying conventional approaches. In this review, we comprehensively summarize the current knowledge of intracellular protein crystallization. This includes an overview of the cellular functions, the physical properties, and, if known, the mode of regulation of nativein cellulocrystal formation, complemented with a discussion of the reported crystallization events of recombinant proteins and the current method developments to successfully collect X-ray diffraction data fromin cellulocrystals. Although the intracellular protein self-assembly mechanisms are still poorly understood, regulatory differences between nativein cellulocrystallization linked to a specific function and accidently crystallizing proteins, either disease associated or recombinantly introduced, become evident. These insights are important to systematically exploit living cells as protein crystallization chambers in the future.
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15

Goo, Tae Won, Eun Young Yun, Sung Wan Kim, Kwang Ho Choi, Seok Woo Kang, Kisang Kwon, Joung-Soon Choi, and O.-Yu Kwon. "Secretion of the Antibacterial Recombinant Protein Enbocin." Zeitschrift für Naturforschung C 63, no. 3-4 (April 1, 2008): 284–88. http://dx.doi.org/10.1515/znc-2008-3-420.

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The insect baculovirus expression vector system (BEVS) is useful for the production of biologically active recombinant proteins. However, the overexpression of foreign proteins in this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we have developed a versatile baculovirus expression and secretion system using the Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion improved the secretion and antibacterial activity of recombinant enbocin proteins. Thus, bPDI gene fusion is a useful addition to the BEVS for the large-scale production of bioactive recombinant proteins
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16

Yu, Xue-Jie, Patricia A. Crocquet-Valdes, Louis C. Cullman, Vsevolod L. Popov, and David H. Walker. "Comparison of Ehrlichia chaffeensisRecombinant Proteins for Serologic Diagnosis of Human Monocytotropic Ehrlichiosis." Journal of Clinical Microbiology 37, no. 8 (1999): 2568–75. http://dx.doi.org/10.1128/jcm.37.8.2568-2575.1999.

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Diagnosis of human monocytotropic ehrlichiosis (HME) generally depends on serology that detects the antibody response to immunodominant proteins of Ehrlichia chaffeensis. Protein immunoblotting was used to evaluate the reaction of the antibodies in patients’ sera with the recombinant E. chaffeensis 120- and 28-kDa proteins as well as the 106- and the 37-kDa proteins. The cloning of the genes encoding the latter two proteins is described in this report. Immunoelectron microscopy demonstrated that the 106-kDa protein is located at the surfaces of ehrlichiae and on the intramorular fibrillar structures associated with E. chaffeensis. The 37-kDa protein is homologous to the iron-binding protein of gram-negative bacteria. Forty-two serum samples from patients who were suspected to have HME were tested by immunofluorescence (IFA) using E. chaffeensis antigen and by protein immunoblotting using recombinant E. chaffeensisproteins expressed in Escherichia coli. Thirty-two serum samples contained IFA antibodies at a titer of 1:64 or greater. The correlation of IFA and recombinant protein immunoblotting was 100% for the 120-kDa protein, 41% for the 28-kDa protein, 9.4% for the 106-kDa protein, and 0% for the 37-kDa protein. None of the recombinant antigens yielded false-positive results. All the sera reactive with the recombinant 28- or the 106-kDa proteins also reacted with the recombinant 120-kDa protein.
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Koval, Olga, Galina Kochneva, Anastasiya Tkachenko, Olga Troitskaya, Galina Sivolobova, Antonina Grazhdantseva, Anna Nushtaeva, Elena Kuligina, and Vladimir Richter. "Recombinant Vaccinia Viruses Coding Transgenes of Apoptosis-Inducing Proteins Enhance Apoptosis But Not Immunogenicity of Infected Tumor Cells." BioMed Research International 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/3620510.

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Genetic modifications of the oncolytic vaccinia virus (VV) improve selective tumor cell infection and death, as well as activation of antitumor immunity. We have engineered a double recombinant VV, coding human GM-CSF, and apoptosis-inducing protein apoptin (VV-GMCSF-Apo) for comparing with the earlier constructed double recombinant VV-GMCSF-Lact, coding another apoptosis-inducing protein, lactaptin, which activated different cell death pathways than apoptin. We showed that both these recombinant VVs more considerably activated a set of critical apoptosis markers in infected cells than the recombinant VV coding GM-CSF alone (VV-GMCSF-dGF): these were phosphatidylserine externalization, caspase-3 and caspase-7 activation, DNA fragmentation, and upregulation of proapoptotic protein BAX. However, only VV-GMCSF-Lact efficiently decreased the mitochondrial membrane potential of infected cancer cells. Investigating immunogenic cell death markers in cancer cells infected with recombinant VVs, we demonstrated that all tested recombinant VVs were efficient in calreticulin and HSP70 externalization, decrease of cellular HMGB1, and ATP secretion. The comparison of antitumor activity against advanced MDA-MB-231 tumor revealed that both recombinants VV-GMCSF-Lact and VV-GMCSF-Apo efficiently delay tumor growth. Our results demonstrate that the composition of GM-CSF and apoptosis-inducing proteins in the VV genome is very efficient tool for specific killing of cancer cells and for activation of antitumor immunity.
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18

Wingfield, Paul T., Robert J. Mattaliano, H. Robson MacDonald, Stewart Craig, G. Marius Clore, Angela M. Gronenborn, and Ursula Schmeissner. "Recombinant-derived interleukin-1α stabilized against specific deamidation." "Protein Engineering, Design and Selection" 1, no. 5 (1987): 413–17. http://dx.doi.org/10.1093/protein/1.5.413.

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19

Geng, Xindu, and Lili Wang. "Liquid chromatography of recombinant proteins and protein drugs." Journal of Chromatography B 866, no. 1-2 (April 2008): 133–53. http://dx.doi.org/10.1016/j.jchromb.2008.01.041.

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20

Volkova, N. V., A. V. Ivanova, A. A. Isaeva, O. A. Polezhaeva, A. V. Zaykovskaya, D. N. Shcherbakov, and E. I. Kazachinskaya. "Obtaining Recombinant Antigens for the Development of Serological Diagnosis of Marburg Fever." Problems of Particularly Dangerous Infections, no. 4 (February 7, 2021): 47–52. http://dx.doi.org/10.21055/0370-1069-2020-4-47-52.

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Aim. Production of recombinant viral antigens of the main immunodominant proteins: glycoprotein (GPΔMLD), nucleoprotein (NP) and matrix protein (VP40) of the Marburg virus, as well as the study of their antigenic and immunogenic properties.Materials and methods. To create recombinant proteins GPΔMLD, NP and VP40 of the Marburg virus, synthesized nucleotide sequences encoding these proteins cloned into the pET21a expression vector were used. The immunogenic and antigenic properties of the obtained recombinant proteins were tested using a number of biomodels (mice, chickens, and guinea pigs).Results and discussion. Recombinant plasmids containing genes encoding proteins GPΔMLD, NP, VP40 of the Marburg virus, as well as Escherichia coli producing strains, with the yield of purified preparations of recombinant proteins GPΔMLD, NP, VP40 from one liter of culture fluid – 5, 10, and 10 μg were obtained, respectively. When mice are immunized, recombinant proteins GP, NP, and VP40 MARV induce the synthesis of high titer antibodies (recombinant proteins NP and VP40 – more than 409600, and recombinant protein GPΔMLD – 12800). Mouse antibodies specific to recombinant proteins interact in an enzyme-linked immunosorbent assay (ELISA) with the antigen of inactivated MARV. Antibodies of chickens immunized with virus-like particles containing the surface glycoprotein of the Marburg virus and antibodies of guinea pigs immunized with an experimental DNA vaccine containing the GPΔMLD MARV gene recognize the recombinant GPΔMLD protein and the viral protein in the inactivated MARV. The resulting recombinant proteins are immunogenic/antigenic and can be used for the development of enzymelinked immunosorbent assay systems.
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Mihailova, N. A., E. M. Zimina, A. V. Soldatenkova, and A. A. Kaloshin. "DEVELOPMENT OF THE VACCINE BASED ON THE RECOMBINANT ANTIGENS OF PSEUDOMONAS AERUGINOSA." Journal of microbiology epidemiology immunobiology 1, no. 1 (August 23, 2019): 74–80. http://dx.doi.org/10.36233/0372-9311-2019-1-74-80.

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Aim. The aim is obtaining, investigation and selection of recombinant antigens for inclusion theirs into the against Pseudomonas vaccine. Materials and methods. The genes encoding of the outer membrane proteins F, L and I and Exotoxin A were synthesized by PCR with the genomic DNA of Pseudomonas aeruginosa. The amplified sequences were cloned into plasmid vectors for expression in cells of Escherichia coli. As the result of expression were the synthesized recombinant proteins that were purified in columns with a nickel-activated sorbent. The authenticity of the recombinant antigens was assessed by electrophoresis and immunoblotting. For assessing the immunogenicity of the recombinant proteins,they were sorbed on aluminum hydroxide and used for intraperitoneal immunization of mice. After a course of immunization, mice were injected intraperitoneally with a live virulent culture or еxotoxin A. Results. The obtained recombinant outer membrane proteins OprF, OprL and OprI, as well as the deletion variant of еxotoxin A (toxoid) stimulated immune reactions and protected the experimental animals from the virulent culture of P. aeruginosa. Using of the complexes of the recombinant proteins, as well as immunization with the fusion proteins consisting from sequences of two or three recombinant antigens, produced an additive increase in protective effects. The combination of the recombinant OprF protein and the recombinant toxoid (efficiency index of protective properties (EI 3.0) and two recombinant fusion proteins (EI 3.5) were the most effective. The first recombinant fusion protein (OprF-aTox-OprI) consisted from fused polypeptide sequences of OprF, toxoid and OprI. The second recombinant fusion protein (OprF-OprI) consisted from fused polypeptide sequences of OprF and OprI. Conclusion. The data obtained showed the fundamental possibility of using recombinant fusion proteins OprF-aTox-OprI and OprF-OprI as well as the complex of the recombinant OprF protein and the recombinant toxoid as the candidated vaccines against Pseudomonas aeruginosa.
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Huang, Li-Fen, Desyanti Saulina Sinaga, Chia-Chun Tan, Shu-Ju Micky Hsieh, and Chi-Hung Huang. "Expression of Recombinant Human Octamer-Binding Transcription Factor 4 in Rice Suspension Cells." International Journal of Molecular Sciences 22, no. 3 (January 30, 2021): 1409. http://dx.doi.org/10.3390/ijms22031409.

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The rice cell suspension culture system is a good way to produce recombinant human proteins, owing to its high biosafety and low production cost. Human Octamer-binding Transcription Factor 4 (Oct4) is a fundamental transcription factor responsible for maintaining human pluripotent embryonic stem cells. Recombinant Oct4 protein has been used to induce pluripotent stem cells. In this study, recombinant Oct4 proteins are produced via a sugar starvation-inducible αAmy3/RAmy3D promoter–signal peptide-based rice recombinant protein expression system. Oct4 mRNAs accumulate in the transgenic rice suspension cells under sugar starvation. The Oct4 recombinant protein is detected in the transgenic rice suspension cells, and its highest yield is approximately 0.41% of total cellular soluble proteins after one day of sugar starvation. The rice cell-synthesized recombinant human Oct4 protein show DNA-binding activity in vitro, which implies that the protein structure is correct for enabling specific binding to the target DNA motif.
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23

UHLÉN, MATHIAS, TOMAS MOKS, and LARS ABRAHMSÉN. "Protein engineering to optimize recombinant protein purification." Biochemical Society Transactions 16, no. 2 (April 1, 1988): 111–12. http://dx.doi.org/10.1042/bst0160111.

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24

Kühn, S., C. Skerka, and P. F. Zipfel. "Mapping of the complement regulatory domains in the human factor H-like protein 1 and in factor H1." Journal of Immunology 155, no. 12 (December 15, 1995): 5663–70. http://dx.doi.org/10.4049/jimmunol.155.12.5663.

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Abstract The human factor H-like protein 1 (FHL-1) is composed of seven repetitive domains (short consensus repeats; SCRs) that are identical in sequence to the seven NH2-terminal SCRs of the complement regulatory protein factor H. We have identified the native FHL-1 protein as a 42-kDa human plasma protein by immunoblotting and by comparing the mobility to that of a recombinant FHL-1 protein. Here, we demonstrate the existence of two distinct co-migrating human plasma proteins that represent the 42-kDa FHL-1 protein and the previously identified 43-kDa factor H-related 1 beta protein. Similar to factor H, the recombinant FHL-1 protein displays cofactor activity in factor I-mediated cleavage of C3b. To identify relevant SCRs of factor H and FHL-1, we recombinantly expressed the domains shared between the two proteins in the baculovirus expression system. Recombinant FHL-1 and all truncated forms that include SCRs 1 to 4 displayed cofactor activity. All four NH2-terminal SCRs are essential, as deletion mutants composed of SCR 1 and 4 only; of SCRs 1, 2, and 4 only, or of SCRs 1, 3, and 4 only were functionally inactive. Similarly, the distance between these individually folding domains is critical for function, as a recombinant protein that had two and four amino acids inserted between SCRs 1 and 2 or between SCRs 3 and 4, respectively, had no activity. These results demonstrate that all four NH2-terminal SCRs of FHL-1 (and of factor H) are required for cofactor activity in factor I-mediated cleavage of C3b, and that the distance between these SCRs is essential.
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Thier, Marc, Bernhard Münst, Stephanie Mielke, and Frank Edenhofer. "Cellular Reprogramming Employing Recombinant Sox2 Protein." Stem Cells International 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/549846.

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Induced pluripotent stem (iPS) cells represent an attractive option for the derivation of patient-specific pluripotent cells for cell replacement therapies as well as disease modeling. To become clinically meaningful, safe iPS cells need to be generated exhibiting no permanent genetic modifications that are caused by viral integrations of the reprogramming transgenes. Recently, various experimental strategies have been applied to accomplish transgene-free derivation of iPS cells, including the use of nonintegrating viruses, episomal expression, or excision of transgenes after reprogramming by site-specific recombinases or transposases. A straightforward approach to induce reprogramming factors is the direct delivery of either synthetic mRNA or biologically active proteins. We previously reported the generation of cell-permeant versions of Oct4 (Oct4-TAT) and Sox2 (Sox2-TAT) proteins and showed that Oct4-TAT is reprogramming-competent, that is, it can substitute for Oct4-encoding virus. Here, we explore conditions for enhanced Sox2-TAT protein stabilization and functional delivery into somatic cells. We show that cell-permeant Sox2 protein can be stabilized by lipid-rich albumin supplements in serum replacement or low-serum-supplemented media. Employing optimized conditions for protein delivery, we demonstrate that Sox2-TAT protein is able to substitute for viral Sox2. Sox2-piPS cells express pluripotency-associated markers and differentiate into all three germ layers.
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Grage, Katrin, Verena Peters, and Bernd H. A. Rehm. "Recombinant Protein Production byIn VivoPolymer Inclusion Display." Applied and Environmental Microbiology 77, no. 18 (July 29, 2011): 6706–9. http://dx.doi.org/10.1128/aem.05953-11.

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ABSTRACTA novel approach to produce purified recombinant proteins was established. The target protein is produced as polyhydroxyalkanoate (PHA) synthase fusion protein, which mediates intracellular formation of PHA inclusions displaying the target protein. After isolation of the PHA inclusions, the pure target protein was released by simple enterokinase digestion.
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Mei, Liu, Lu Lin-Jing, Huang Jun-Yan, Zhang Shu-Huan, Bi Ding-Ren, and Sun Ming. "Display of H5N1Avian influenza virushaemagglutinin HA1 onBacillus thuringiensiscell surface and its immunogenicity for mice." Chinese Journal of Agricultural Biotechnology 4, no. 3 (December 2007): 221–28. http://dx.doi.org/10.1017/s1479236207001702.

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AbstractThe S-layer protein CTC surface display system ofBacillus thuringiensiswas used to test the possibility of displaying H5N1Avian influenza virus(AIV) haemagglutinin HA1 on the cell surface ofB. thuringiensis. Two recombinant plasmids, pCTC-HA1P and pCSHA1P, were constructed by replacing the central part below the surface anchor sequenceslhof S-layer protein genectcwith partha1gene(ha1p). pCTC-HA1P harboured the fusion genectc-ha1pand pCSHA1P the fusion genecsa-ctc-ha1p,csarepresenting thecsaABoperon (very important in anchoring S-layer protein on the bacterial cell surface). Two recombinantB. thuringiensisstrains were constructed by electrotransferring recombinant plasmids toB. thuringiensisplasmid-free derivative strain BMB171. Strains obtained were CH (bearing pCSHA1P) and BCCH (bearing pCTC-HA1P as well as thecsaABoperon-carrying plasmid pMIL-CSA). The vegetative cells of CH and BCCH were used as antigens in haemagglutination (HA) and haemagglutination inhibition (HI) assays. HA assay showed recombinant HA1 proteins successfully displayed on the cell surface of CH and BCCH. HI assay showed that these recombinant HA1 proteins were specific to standard positive HI (haemagglutination inhibition test) serum of subtype H5 AIV. After immunization of mice with vegetative cells, both CH and BCCH elicited a humoral response to HA1 and exhibited immunogenicity as indicated by enzyme-linked immunosorbent assay (ELISA). ELISA also showed that CH exhibited a higher immunogenicity than BCCH. The strategy developed in this study suggests the possibility of generating a heat-stable and oral veterinary vaccine against AIV with theB. thuringiensisS-layer protein CTC surface display system.
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Zagursky, Robert J., Peggy Ooi, Kevin F. Jones, Michael J. Fiske, Robert P. Smith, and Bruce A. Green. "Identification of a Haemophilus influenzae5′-Nucleotidase Protein: Cloning of the nucA Gene and Immunogenicity and Characterization of the NucA Protein." Infection and Immunity 68, no. 5 (May 1, 2000): 2525–34. http://dx.doi.org/10.1128/iai.68.5.2525-2534.2000.

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ABSTRACT We report on the identification of a surface-exposed, highly conserved, immunogenic nontypeable Haemophilus influenzae(NTHi) protein, which elicits cross-reactive bactericidal antibodies against NTHi. The protein was extracted from NTHi strain P860295 with KSCN and purified; it migrated as a single band on a sodium dodecyl sulfate-polyacrylamide gel with an apparent molecular mass of 63 kDa. Mouse antiserum generated against the purified protein was reactive on whole-cell enzyme-linked immunosorbent assay (ELISA) with seven NTHi strains and type b Eagan and Whittier strains and exhibited bactericidal activity to homologous and heterologous NTHi strains. However, the protein is made in small amounts in NTHi as corroborated by immunoelectron microscopy. To further study this protein, we cloned, sequenced, and expressed it recombinantly in Escherichia coli. The recombinant protein is localized in the periplasm ofE. coli and has been purified to homogeneity. Both the recombinant and native proteins possess 5′-nucleotidase activity; hence, the protein has been called NucA. Mouse antiserum directed against the recombinant NucA protein was reactive on Western immunoblots and whole-cell ELISA with all H. influenzaestrains tested including Eagan and was bactericidal for two heterologous strains tested. The antiserum also resulted in a log reduction in bacteremia, in an infant-rat protection study withH. influenzae type b as the challenge strain. These features suggest that NucA is a potential subunit vaccine candidate against NTHi disease.
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Glass, Pamela J., Laura J. White, Judith M. Ball, Isabelle Leparc-Goffart, Michele E. Hardy, and Mary K. Estes. "Norwalk Virus Open Reading Frame 3 Encodes a Minor Structural Protein." Journal of Virology 74, no. 14 (July 15, 2000): 6581–91. http://dx.doi.org/10.1128/jvi.74.14.6581-6591.2000.

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ABSTRACT Norwalk virus (NV) is a causative agent of acute epidemic nonbacterial gastroenteritis in humans. The inability to cultivate NV has required the use of molecular techniques to examine the genome organization and functions of the viral proteins. The function of the NV protein encoded by open reading frame 3 (ORF 3) has been unknown. In this paper, we report the characterization of the NV ORF 3 protein expressed in a cell-free translation system and in insect cells and show its association with recombinant virus-like particles (VLPs) and NV virions. Expression of the ORF 3 coding region in rabbit reticulocyte lysates resulted in the production of a single protein with an apparent molecular weight of 23,000 (23K protein), which is not modified by N-linked glycosylation. The ORF 3 protein was expressed in insect cells by using two different baculovirus recombinants; one recombinant contained the entire 3′ end of the genome beginning with the ORF 2 coding sequences (ORFs 2+3), and the second recombinant contained ORF 3 alone. Expression from the construct containing both ORF 2 and ORF 3 resulted in the expression of a single protein (23K protein) detected by Western blot analysis with ORF 3-specific peptide antisera. However, expression from a construct containing only the ORF 3 coding sequences resulted in the production of multiple forms of the ORF 3 protein ranging in size from 23,000 to 35,000. Indirect-immunofluorescence studies using an ORF 3 peptide antiserum showed that the ORF 3 protein is localized to the cytoplasm of infected insect cells. The 23K ORF 3 protein was consistently associated with recombinant VLPs purified from the media of insect cells infected with a baculovirus recombinant containing the entire 3′ end of the NV genome. Western blot analysis of NV purified from the stools of NV-infected volunteers revealed the presence of a 35K protein as well as multiple higher-molecular-weight bands specifically recognized by an ORF 3 peptide antiserum. These results indicate that the ORF 3 protein is a minor structural protein of the virion.
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Hsu, Eric, Timothy Osslund, Rebecca Nybo, Bao-Lu Chen, William C. Kenney, C. Fred Morris, Tsutomu Arakawa, and Linda O. Narhi. "Enhanced stability of recombinant keratinocyte growth factor by mutagenesis." Protein Engineering, Design and Selection 19, no. 4 (February 14, 2006): 147–53. http://dx.doi.org/10.1093/protein/gzj013.

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Feng, Ziru, Xifeng Li, Baofang Fan, Cheng Zhu, and Zhixiang Chen. "Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability." International Journal of Molecular Sciences 23, no. 21 (November 4, 2022): 13516. http://dx.doi.org/10.3390/ijms232113516.

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The production of therapeutic and industrial recombinant proteins in plants has advantages over established bacterial and mammalian systems in terms of cost, scalability, growth conditions, and product safety. In order to compete with these conventional expression systems, however, plant expression platforms must have additional economic advantages by demonstrating a high protein production yield with consistent quality. Over the past decades, important progress has been made in developing strategies to increase the yield of recombinant proteins in plants by enhancing their expression and reducing their degradation. Unlike bacterial and animal systems, plant expression systems can utilize not only cell cultures but also whole plants for the production of recombinant proteins. The development of viral vectors and chloroplast transformation has opened new strategies to drastically increase the yield of recombinant proteins from plants. The identification of promoters for strong, constitutive, and inducible promoters or the tissue-specific expression of transgenes allows for the production of recombinant proteins at high levels and for special purposes. Advances in the understanding of RNAi have led to effective strategies for reducing gene silencing and increasing recombinant protein production. An increased understanding of protein translation, quality control, trafficking, and degradation has also helped with the development of approaches to enhance the synthesis and stability of recombinant proteins in plants. In this review, we discuss the progress in understanding the processes that control the synthesis and degradation of gene transcripts and proteins, which underlie a variety of developed strategies aimed at maximizing recombinant protein production in plants.
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Sims, Andrew H., Manda E. Gent, Karin Lanthaler, Nigel S. Dunn-Coleman, Stephen G. Oliver, and Geoffrey D. Robson. "Transcriptome Analysis of Recombinant Protein Secretion by Aspergillus nidulans and the Unfolded-Protein Response In Vivo." Applied and Environmental Microbiology 71, no. 5 (May 2005): 2737–47. http://dx.doi.org/10.1128/aem.71.5.2737-2747.2005.

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ABSTRACT Filamentous fungi have a high capacity for producing large amounts of secreted proteins, a property that has been exploited for commercial production of recombinant proteins. However, the secretory pathway, which is key to the production of extracellular proteins, is rather poorly characterized in filamentous fungi compared to yeast. We report the effects of recombinant protein secretion on gene expression levels in Aspergillus nidulans by directly comparing a bovine chymosin-producing strain with its parental wild-type strain in continuous culture by using expressed sequence tag microarrays. This approach demonstrated more subtle and specific changes in gene expression than those observed when mimicking the effects of protein overproduction by using a secretion blocker. The impact of overexpressing a secreted recombinant protein more closely resembles the unfolded-protein response in vivo.
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Duffy, Michael F., Kevin G. Whithear, Amir H. Noormohammadi, Philip F. Markham, Michael Catton, Jennie Leydon, and Glenn F. Browning. "Indirect Enzyme-Linked Immunosorbent Assay for Detection of Immunoglobulin G Reactive with a Recombinant Protein Expressed from the Gene Encoding the 116-Kilodalton Protein ofMycoplasma pneumoniae." Journal of Clinical Microbiology 37, no. 4 (1999): 1024–29. http://dx.doi.org/10.1128/jcm.37.4.1024-1029.1999.

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Serology remains the method of choice for laboratory diagnosis ofMycoplasma pneumoniae infection. Currently available serological tests employ complex cellular fractions of M. pneumoniae as antigen. To improve the specificity of M. pneumoniae diagnosis, a recombinant protein was assessed as a serodiagnostic reagent. A panel of recombinant proteins were expressed from a cloned M. pneumoniae gene that encodes a 116-kDa surface protein antigen. The recombinant proteins were assessed for reactivity with patient sera and the most antigenic was further assessed for its serodiagnostic potential by indirect enzyme-linked immunosorbent assay (ELISA). The ELISA based on the recombinant protein was equivalent in sensitivity to the commercial test (Serodia Myco II; Fujirebio Inc.) to which it was compared. Southern and Western blotting data suggested that the recombinant protein derived from the 116-kDa protein of M. pneumoniae could provide a species-specific diagnostic tool, although further assessment is required.
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Alatortseva, G. I., A. V. Sidorov, L. N. Nesterenko, L. N. Luhverchik, V. V. Dotsenko, I. I. Amiantova, V. Yu Kabargina, et al. "DESIGN OF HEPATITIS E VIRUS GENOTYPE 1 RECOMBINANT CAPSID PROTEIN: CLONING, EXPRESSION, PURIFICATION, EVALUATION OF THE ANTIGENIC PROPERTIES." Journal of microbiology epidemiology immunobiology, no. 6 (December 28, 2017): 72–80. http://dx.doi.org/10.36233/0372-9311-2017-6-72-80.

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Aim. The development of the hepatitis E virus (HEV) genotype 1 recombinant capsid protein. Materials and methods. Escherichia coli strains, plasmid vectors, serological and clinical samples, ELISA reagent kits, molecular biological, bioinformatic, biotechnological, biochemical and serological methods. Results. Using HEV genotype 1 DNA copy of subgenomic virus RNA we made E.coli strains producing recombinabt capsid protein, containing C-terminal fragment of ORF2 protein fused to E.coli beta-galactosidase. Recombinant protein ORF2 had been isolated from the inclusion bodies of the E.coli biomass and purified by size exclusion chromatography. By Western blotting it had been shown specific interaction of the recombinant polypeptide with anti-HEV IgG from pool of positive sera. Antigenic specificity of the recombinant polypeptide had been confirmed by enzyme-linked immunosorbent assay with sera of hepatitis E patients and reference groups: healthy donors, patients with hepatitis А, В, C, infectious mononucleosis and cytomegalovirus infection, HIV-infected patients. Conclusion. HEV genotype 1 ORF2 recombinant antigen had been developed, and its possible use in diagnostic tests had been experimentally shown.
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Fisher, Adam C., Charles H. Haitjema, Cassandra Guarino, Eda Çelik, Christine E. Endicott, Craig A. Reading, Judith H. Merritt, A. Celeste Ptak, Sheng Zhang, and Matthew P. DeLisa. "Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli." Applied and Environmental Microbiology 77, no. 3 (December 3, 2010): 871–81. http://dx.doi.org/10.1128/aem.01901-10.

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ABSTRACTTheCampylobacter jejuni pglgene cluster encodes a complete N-linked protein glycosylation pathway that can be functionally transferred intoEscherichia coli. In this system, we analyzed the interplay between N-linked glycosylation, membrane translocation and folding of acceptor proteins in bacteria. We developed a recombinant N-glycan acceptor peptide tag that permits N-linked glycosylation of diverse recombinant proteins expressed in the periplasm of glycosylation-competentE. colicells. With this “glycosylation tag,” a clear difference was observed in the glycosylation patterns found on periplasmic proteins depending on their mode of inner membrane translocation (i.e., Sec, signal recognition particle [SRP], or twin-arginine translocation [Tat] export), indicating that the mode of protein export can influence N-glycosylation efficiency. We also established that engineered substrate proteins targeted to environments beyond the periplasm, such as the outer membrane, the membrane vesicles, and the extracellular medium, could serve as substrates for N-linked glycosylation. Taken together, our results demonstrate that theC. jejuniN-glycosylation machinery is compatible with distinct secretory mechanisms inE. coli, effectively expanding the N-linked glycome of recombinantE. coli. Moreover, this simple glycosylation tag strategy expands the glycoengineering toolbox and opens the door to bacterial synthesis of a wide array of recombinant glycoprotein conjugates.
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Abed, Y., G. St-Laurent, H. Zhang, R. M. Jacobs, and D. Archambault. "Development of a Western Blot Assay for Detection of Bovine Immunodeficiency-Like Virus Using Capsid and Transmembrane Envelope Proteins Expressed from Recombinant Baculovirus." Clinical Diagnostic Laboratory Immunology 6, no. 2 (March 1, 1999): 168–72. http://dx.doi.org/10.1128/cdli.6.2.168-172.1999.

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ABSTRACT A 120-amino-acid polypeptide selected from the transmembrane protein region (tTM) and the major capsid protein p26 of bovine immunodeficiency-like virus (BIV) were expressed as fusion proteins from recombinant baculoviruses. The antigenic reactivity of both recombinant fusion proteins was confirmed by Western blot with bovine and rabbit antisera to BIV. BIV-negative bovine sera and animal sera positive for bovine syncytial virus and bovine leukemia virus failed to recognize the recombinant fusion proteins, thereby showing the specificity of the BIV Western blot. One hundred and five bovine serum samples were tested for the presence of anti-BIV antibodies by the recombinant protein-based Western blot and a reference Western blot assay using cell culture-derived virions as test antigens. There was a 100% concordance when the p26 fusion protein was used in the Western blot. However, the Western blot using the tTM fusion protein as its test antigen identified four BIV-positive bovine sera which had tested negative in both the p26 recombinant-protein-based and the reference Western blot assays. This resulted in the lower concordance of 96.2% between the tTM-protein-based and reference Western blot assays. The results of this study showed that the recombinant p26 and tTM proteins can be used as test antigens for the serodetection of BIV-infection in animals.
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Salánki, Katalin, Ákos Gellért, Emese Huppert, Gábor Náray-Szabó, and Ervin Balázs. "Compatibility of the movement protein and the coat protein of cucumoviruses is required for cell-to-cell movement." Journal of General Virology 85, no. 4 (April 1, 2004): 1039–48. http://dx.doi.org/10.1099/vir.0.19687-0.

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For the cell-to-cell movement of cucumoviruses both the movement protein (MP) and the coat protein (CP) are required. These are not reversibly exchangeable between Cucumber mosaic virus (CMV) and Tomato aspermy virus (TAV). The MP of CMV is able to function with the TAV CP (chimera RT), but TAV MP is unable to promote the cell-to-cell movement in the presence of CMV CP (chimera TR). To gain further insight into the non-infectious nature of the TR recombinant, RNA 3 chimeras were constructed with recombinant MPs and CPs. The chimeric MP and one of the CP recombinants were infectious. The other recombinant CP enabled virus movement only after the introduction of two point mutations (Glu→Lys and Lys→Arg at aa 62 and 65, respectively). The mutations served to correct the CP surface electrostatic potential that was altered by the recombination. The infectivity of the TR virus on different test plants was restored by replacing the sequence encoding the C-terminal 29 aa of the MP with the corresponding sequence of the CMV MP gene or by exchanging the sequence encoding the C-terminal 15 aa of the CP with the same region of TAV. The analysis of the recombinant clones suggests a requirement for compatibility between the C-terminal 29 aa of the MP and the C-terminal two-thirds of the CP for cell-to-cell movement of cucumoviruses.
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38

Sankar, S. Gowri, K. J. Dhanajeyan, R. Paramasivan, V. Thenmozhi, B. K. Tyagi, and S. John Vennison. "High-Level Expression of Functionally Active Dengue-2 Non-Structural Antigen 1 Production inEscherichia coli." BioMed Research International 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/343195.

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Detection of nonstructural protein (NS1) is an important diagnostic marker during acute phase of dengue infection. Not only for diagnostic purpose, the protein had important role in vaccine design as well, as a candidate for studying virus assembly and maturation. Various researchers employed different expression systems and strategies for recombinant NS1 protein production. Attempts to express NS1 protein in prokaryotic and yeast expression system result in formation of insoluble protein which needs to undergo refolding to attain native structural and functional forms. Here, we report the production of soluble NS1 protein inE. coliby using appropriate vector and employing suitable culture conditions to maximize protein production. Proteins were purified using metal affinity chromatography. SDS-PAGE and western blot analysis reveal the native structure of NS1 protein. Solid phase ELISA using the recombinantly expressed antigen with positive and negative dengue samples showed that the expressed protein retains its antigenic and immunological properties. To our knowledge, this is the first report on the successful production of functionally active recombinant dengue-2 NS1 protein production without undergoing anyin vitroposttranslational modification process.
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Heidary, Somayyeh, Amir Yaghoubi Nezhad, and Atefeh Mehrabi Far. "Colonization and Investigation of Vibrio Cholera Recombination Protein in E-Coli." International Journal of Engineering & Technology 7, no. 4.7 (September 27, 2018): 32. http://dx.doi.org/10.14419/ijet.v7i4.7.20375.

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Background and aim: Vibrio cholerae is a gram-negative bacterial pathogen that causes diarrheal disease. One of the most pathogenic factors of V. cholerae is toxin-coregulated pili. This pilus is required as the first factor in the colonization and bacterial persistence in the small intestine. Materials and Methods: In this study, V. cholerae toxin-coregulated pili A (TCPA) gene was amplified using PCR method. The above genes were purified and then expressed by being cloned into the pGEX4T-1 plasmid. Then the recombinant plasmid structure was introduced into the E. coli bacterium. Protein production was carried out by IPTG induction and optimization of culture conditions. The recombinant proteins were purified using Glutathione S-Transferase (GST) Assay Kit and western blot test was then carried out for confirmation of recombinant protein. Protein levels were measured using Bradford protein assay. Results: The results of the present study proved the successful expression of recombinant proteins in E. coli cells. The recombinant protein was purified by affinity chromatography. The reaction pattern between these proteins and their anti-antibodies showed that these proteins have antigenic properties. Conclusion: Since it was proved that these proteins have antigenic properties in this study, they may be used as an appropriate antigen for vaccination of V. cholera.
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Dale, J. B., E. Y. Chiang, and J. W. Lederer. "Recombinant tetravalent group A streptococcal M protein vaccine." Journal of Immunology 151, no. 4 (August 15, 1993): 2188–94. http://dx.doi.org/10.4049/jimmunol.151.4.2188.

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Abstract Previous studies have shown that the amino-terminal regions of group A streptococcal M proteins contain primarily protective (opsonic) epitopes and not tissue-cross-reactive epitopes. Limited primary structures from multiple serotypes of M protein containing only protective epitopes could potentially be linked together to form a broadly protective vaccine. The present studies were undertaken to determine the protective immunogenicity of a recombinant, multivalent hybrid molecule containing amino-terminal subunits of types 24, 5, 6, and 19 M proteins. Polymerase chain reaction primers were designed to amplify emm gene fragments ranging from 35 to 113 codons. The PCR products were ligated in tandem and inserted into pKK223-3. The tetravalent M protein that was purified from extracts of Escherichia coli migrated as a single band on SDS-PAGE with an apparent m.w. of 31 kDa. In immunoblot analyses, the hybrid protein reacted with serotype-specific antisera indicating that it contained all four M protein subunits. Rabbits immunized with the purified tetravalent M protein developed significant antibody levels against all four serotypes of native M proteins represented in the hybrid protein. None of the antisera cross-reacted with human tissues. The immune sera also opsonized all four serotypes of group A streptococci. Our data show that a hybrid protein containing subunits from multiple M proteins can evoke broadly protective immune responses without tissue-cross-reactive antibodies.
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Hayat, Seyed Mohammad Gheibi, Najmeh Farahani, Behrouz Golichenari, and Amirhossein Sahebkar. "Recombinant Protein Expression in Escherichia coli (E.coli): What We Need to Know." Current Pharmaceutical Design 24, no. 6 (May 10, 2018): 718–25. http://dx.doi.org/10.2174/1381612824666180131121940.

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Background: Host, vector, and culture conditions (including cultivation media) are considered among the three main elements contributing to a successful production of recombinant proteins. Accordingly, one of the most common hosts to produce recombinant therapeutic proteins is Escherichia coli. Methodology: A comprehensive literature review was performed to identify important factors affecting production of recombinant proteins in Escherichia coli. Results: Escherichia coli is taken into account as the easiest, quickest, and cheapest host with a fully known genome. Thus, numerous modifications have been carried out on Escherichia coli to optimize it as a good candidate for protein expression and; as a result, several engineered strains of Escherichia coli have been designed. In general; host strain, vector, and cultivation parameters are recognized as crucial ones determining success of recombinant protein expression in Escherichia coli. In this review, the role of host, vector, and culture conditions along with current pros and cons of different types of these factors leading to success of recombinant protein expression in Escherichia coli were discussed. Conclusion: Successful protein expression in Escherichia coli necessitates a broad knowledge about physicochemical properties of recombinant proteins, selection among common strains of Escherichia coli and vectors, as well as factors related to media including time, temperature, and inducer.
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Jamrichová, Daniela, Lenka Tišáková, Veronika Jarábková, and Andrej Godány. "How to approach heterogeneous protein expression for biotechnological use: An overview." Nova Biotechnologica et Chimica 16, no. 1 (June 27, 2017): 1–11. http://dx.doi.org/10.1515/nbec-2017-0001.

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AbstractProduction of recombinant proteins in Escherichia coli expression systems has shown many advantages, as well as disadvantages, especially for biotechnological and other down-stream applications. The choice of an appropriate vector depends on the gene, to be cloned for purification procedures and other analyses. Selection of a suitable production strain plays an important role in the preparation of recombinant proteins. The main criteria for the selection of the host organism are the properties of the recombinant produced protein, its subsequent use and the total amount desired. The most common problems in eukaryotic gene expression and recombinant proteins purification are, for instance, post-translational modifications, formation of disulphide bonds, or inclusion bodies. Obtaining a purified protein is a key step enabling further characterization of its role in the biological system. Moreover, methods of protein purification have been developed in parallel with the discovery of proteins and the need for their studies and applications. After protein purification, and also between the individual purification steps, it is necessary to test protein stability under different conditions over time. Shortly, all the essential points have been briefly discussed, which could be encountered during production and purification of a recombinant protein of interest, especially from eukaryotic source and expressed heterogeneously in prokaryotic production system.
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Kaloshin, A. A., A. V. Soldatenkova, E. M. Zimina, and N. A. Mikhailova. "OBTAINING FUSED RECOMBINANT PROTEINS OprF-ΔOprI, ΔOprF-ΔOprI AND OprF-aTox-ΔOprl OF PSEUDOMONAS AERUGINOSA." Journal of microbiology epidemiology immunobiology, no. 5 (October 28, 2017): 32–38. http://dx.doi.org/10.36233/0372-9311-2017-5-32-38.

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Aim. Obtaining fused recombinant proteins of Pseudomonas aeruginosa that have protective properties against experimental pseudomonas infection. Materials and methods. Fused sequences of P. aeruginosa genes oprF, oprl and deleted form of toxA were cloned in plasmids for the expression in Escherichia coli. The synthesized recombinant proteins were purified in Ni-sepharose columns. Recombinant proteins were administered to mice intraperitonealiy twice with a 2 week interval to evaluate protective properties. Virulent culture of P. aeruginosa strain PA103 was injected into the animals intraperitonealiy 2 weeks after the immunization course as experimental challenge. Results. 3 fused recombinant proteins were produced: 1. OprF-ΔOprl included full sequence of OprF protein and deletion variant of OprI (lacking first 20 amino acids); 2. AOprF-AOprl consisted of C-terminal region (192 - 342 amino acids) OprF and deletion variant of Oprl protein; 3. OprF-aTox-ΔOprI included full sequence of OprF protein, sequence of nontoxic variant of exotoxin A (without 106 C-terminal amino acids) and deletion variant of Oprl protein. Fused recombinant proteins OprF-AOprl and OprF-aTox-ΔOprI at immunization doses of 25 and 50 pg for the first and second protein, respectively, were shown to have the best protective properties. Conclusion. The results obtained open perspectives for further studies to create specific immune biological preparations based on fused recombinant proteins of P. aeruginosa.
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Zhang, Xianan, Nico Betterle, Diego Hidalgo Martinez, and Anastasios Melis. "Recombinant Protein Stability in Cyanobacteria." ACS Synthetic Biology 10, no. 4 (March 8, 2021): 810–25. http://dx.doi.org/10.1021/acssynbio.0c00610.

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Soares, Alexandra, Ana Azevedo, Luciana C. Gomes, and Filipe J. Mergulhão. "Recombinant protein expression in biofilms." AIMS Microbiology 5, no. 3 (2019): 232–50. http://dx.doi.org/10.3934/microbiol.2019.3.232.

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46

Hawkins, Bryan J. "Recombinant Bone Morphogenetic Protein-2." Techniques in Foot & Ankle Surgery 6, no. 2 (June 2007): 80–88. http://dx.doi.org/10.1097/btf.0b013e33180620fc2.

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47

Porro, Danilo, Michael Sauer, Paola Branduardi, and Diethard Mattanovich. "Recombinant Protein Production in Yeasts." Molecular Biotechnology 31, no. 3 (2005): 245–60. http://dx.doi.org/10.1385/mb:31:3:245.

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48

Porte,, Mathieu. "TGE for Recombinant Protein Production." Genetic Engineering & Biotechnology News 32, no. 5 (March 2012): 46–47. http://dx.doi.org/10.1089/gen.32.5.19.

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STINSON, STEPHEN. "Recombinant clotting protein passes trials." Chemical & Engineering News 69, no. 1 (January 7, 1991): 8. http://dx.doi.org/10.1021/cen-v069n001.p008.

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Anné, Jozef, Bárbara Maldonado, Jan Van Impe, Lieve Van Mellaert, and Kristel Bernaerts. "Recombinant protein production and streptomycetes." Journal of Biotechnology 158, no. 4 (April 2012): 159–67. http://dx.doi.org/10.1016/j.jbiotec.2011.06.028.

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