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Journal articles on the topic 'High-yield protein expression'

Author: Grafiati

Published: 5 June 2025

Last updated: 1 August 2025

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1

Vasseur-Godbillon, Corinne, Djemel Hamdane, Michael C. Marden та Véronique Baudin-Creuza. "High-yield expression in Escherichia coli of soluble human α-hemoglobin complexed with its molecular chaperone". Protein Engineering, Design and Selection 19, № 3 (2006): 91–97. http://dx.doi.org/10.1093/protein/gzj006.

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2

Lin, Bo, Hailing Meng, Hui Bing, Dongting Zhangsun, and Sulan Luo. "Efficient Expression of Acetylcholine-Binding Protein fromAplysia californicain Bac-to-Bac System." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/691480.

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The Bac-to-Bac baculovirus expression system can efficiently produce recombinant proteins, but the system may have to be optimized to achieve high-level expression for different candidate proteins. We reported here the efficient expression of acetylcholine-binding proteins from sea haresAplysia californica(Ac-AChBP) and a convenient method to monitor protein expression level in this expression system. Three key factors affecting expression of Ac-AChBP were optimized for maximizing the yield, which included the cell density, volume of the infecting baculovirus inoculums, and the culturing time

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3

Sandee, Duanpen, and Walter L. Miller. "High-Yield Expression of a Catalytically Active Membrane-Bound Protein: Human P450 Oxidoreductase." Endocrinology 152, no. 7 (2011): 2904–8. http://dx.doi.org/10.1210/en.2011-0230.

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P450 oxidoreductase (POR) is a two-flavin protein that reduces microsomal P450 enzymes and some other proteins. Preparation of active bacterially expressed human POR for biochemical studies has been difficult because membrane-bound proteins tend to interact with column matrices. To reduce column-protein interactions and permit more vigorous washing, human POR lacking 27 N-terminal residues (N-27 POR) was modified to carry a C-terminal Gly3His6-tag (N-27 POR-G3H6). When expressed in Escherichia coli, N-27 POR-G3H6 could be purified to apparent homogeneity by a modified, single-step nickel-nitri

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4

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 (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 redu

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Qiao, Zilin, Yuejiao Liao, Mengyuan Pei, et al. "RSAD2 Is an Effective Target for High-Yield Vaccine Production in MDCK Cells." Viruses 14, no. 11 (2022): 2587. http://dx.doi.org/10.3390/v14112587.

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Increasingly, attention has focused on improving vaccine production in cells using gene editing technology to specifically modify key virus regulation-related genes to promote virus replication. In this study, we used DIA proteomics analysis technology to compare protein expression differences between two groups of MDCK cells: uninfected and influenza A virus (IAV) H1N1-infected cells 16 h post infection (MOI = 0.01). Initially, 266 differentially expressed proteins were detected after infection, 157 of which were upregulated and 109 were downregulated. We screened these proteins to 23 genes r

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Kaipa, Jagan Mohan, Ganna Krasnoselska, Raymond J. Owens, and Joop van den Heuvel. "Screening of Membrane Protein Production by Comparison of Transient Expression in Insect and Mammalian Cells." Biomolecules 13, no. 5 (2023): 817. http://dx.doi.org/10.3390/biom13050817.

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Membrane proteins are difficult biomolecules to express and purify. In this paper, we compare the small-scale production of six selected eukaryotic integral membrane proteins in insect and mammalian cell expression systems using different techniques for gene delivery. The target proteins were C terminally fused to the green fluorescent marker protein GFP to enable sensitive monitoring. We show that the choice of expression systems makes a considerable difference to the yield and quality of the six selected membrane proteins. Virus-free transient gene expression (TGE) in insect High Five cells

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Aslam, Muhammad Shahbaz, Iram Gull, Malik Siddique Mahmood та ін. "High yield expression, characterization, and biological activity of IFNα2-Tα1 fusion protein". Preparative Biochemistry & Biotechnology 50, № 3 (2019): 281–91. http://dx.doi.org/10.1080/10826068.2019.1689509.

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8

Wang, Leyu, Meta Foster, Yan Zhang, et al. "High yield expression of non-phosphorylated protein tyrosine kinases in insect cells." Protein Expression and Purification 61, no. 2 (2008): 204–11. http://dx.doi.org/10.1016/j.pep.2008.05.017.

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9

Sun, Jiakang, June A. Mayor, Rusudan Kotaria, and Ronald S. Kaplan. "High-Yield Expression and Purification of a Plasma Membrane Citrate Transport Protein." Biophysical Journal 96, no. 3 (2009): 686a. http://dx.doi.org/10.1016/j.bpj.2008.12.3624.

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10

Chen, Xiaojing, Karyn L. Wilde, Hui Wang, et al. "High yield expression and efficient purification of deuterated human protein galectin-2." Food and Bioproducts Processing 90, no. 3 (2012): 563–72. http://dx.doi.org/10.1016/j.fbp.2011.12.004.

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11

Ta, Duy Tien, Erik Steen Redeker, Brecht Billen, et al. "An efficient protocol towards site-specifically clickable nanobodies in high yield: cytoplasmic expression inEscherichia colicombined with intein-mediated protein ligation." Protein Engineering Design and Selection 28, no. 10 (2015): 351–63. http://dx.doi.org/10.1093/protein/gzv032.

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12

Chytła, Agnieszka, Weronika Gajdzik-Nowak, Agnieszka Biernatowska, Aleksander F. Sikorski, and Aleksander Czogalla. "High-Level Expression of Palmitoylated MPP1 Recombinant Protein in Mammalian Cells." Membranes 11, no. 9 (2021): 715. http://dx.doi.org/10.3390/membranes11090715.

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Our recent studies have pointed to an important role of the MAGUK family member, MPP1, as a crucial molecule interacting with flotillins and involved in the lateral organization of the erythroid plasma membrane. The palmitoylation of MPP1 seems to be an important element in this process; however, studies on the direct effect of palmitoylation on protein–protein or protein–membrane interactions in vitro are still challenging due to the difficulties in obtaining functional post-translationally modified recombinant proteins and the lack of comprehensive protocols for the purification of palmitoyl

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Takahashi, Maria Beatriz, Aline Florencio Teixeira, and Ana Lucia Tabet Oller Nascimento. "Overcoming problems to produce the recombinant protein LipL21 of Leptospira interrogans." BioTechniques 74, no. 3 (2023): 137–42. http://dx.doi.org/10.2144/btn-2022-0076.

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The production of leptospiral recombinant proteins in the soluble form and in high yield from Escherichia coli is still a challenge. This work presents the cloning, expression and purification of the outer membrane protein of Leptospira interrogans, LipL21, which is considered an interesting target for vaccine and diagnostics development. The expression profile and yield of LipL21 was compared after cloning in the vectors pAE, pET28a and pET-SUMO, and it was observed that LipL21 was expressed in a low amount with pAE vector. By using the pET-28a vector, protein expression was increased, but th

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Sun, Hong, Songyu Wang, Mei Lu, Christine E. Tinberg, and Benjamin M. Alba. "Protein production from HEK293 cell line-derived stable pools with high protein quality and quantity to support discovery research." PLOS ONE 18, no. 6 (2023): e0285971. http://dx.doi.org/10.1371/journal.pone.0285971.

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Antibody-based therapeutics and recombinant protein reagents are often produced in mammalian expression systems, which provide human-like post-translational modifications. Among the available mammalian cell lines used for recombinant protein expression, Chinese hamster ovary (CHO)-derived suspension cells are generally utilized because they are easy to culture and tend to produce proteins in high yield. However, some proteins purified from CHO cell overexpression suffer from clipping and display undesired non-human post translational modifications (PTMs). In addition, CHO cell lines are often

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15

Fan, Youpeng, Junhong Wei, Wei Wang, et al. "Utilization of Recombinant Baculovirus Expression System to Produce the RBD Domain of SARS-CoV-2 Spike Protein." Pathogens 11, no. 6 (2022): 672. http://dx.doi.org/10.3390/pathogens11060672.

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Continuous outbreaks of viral diseases in humans facilitates a need for the rapid development of viral test kits and vaccines. These require expression systems to produce a pure and high yield of target viral proteins. We utilized a baculovirus–silkworm expression system to produce the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. First, we had to develop a strategy for constructing a recombinant baculovirus for RBD expression. For this, the coding region of the Bombyx mori cypovirus (BmCPV) polyhedron was assembled with the Bombyx mori nuclear polyhedrosis virus (BmNPV) promo

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16

Barth, S., M. Huhn, B. Matthey, A. Klimka, E. A. Galinski, and A. Engert. "Compatible-Solute-Supported Periplasmic Expression of Functional Recombinant Proteins under Stress Conditions." Applied and Environmental Microbiology 66, no. 4 (2000): 1572–79. http://dx.doi.org/10.1128/aem.66.4.1572-1579.2000.

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ABSTRACT The standard method of producing recombinant proteins such as immunotoxins (rITs) in large quantities is to transform gram-negative bacteria and subsequently recover the desired protein from inclusion bodies by intensive de- and renaturing procedures. The major disadvantage of this technique is the low yield of active protein. Here we report the development of a novel strategy for the expression of functional rIT directed to the periplasmic space of Escherichia coli. rITs were recovered by freeze-thawing of pellets from shaking cultures of bacteria grown under osmotic stress (4% NaCl

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17

Su, Pin-Chuan, William Si, Deidre L. Baker, and Bryan W. Berger. "High-yield membrane protein expression from E. coli using an engineered outer membrane protein F fusion." Protein Science 22, no. 4 (2013): 434–43. http://dx.doi.org/10.1002/pro.2224.

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18

Liu, Ru-Shi. "High-yield expression of recombinant SARS coronavirus nucleocapsid protein in methylotrophic yeastPichia pastoris." World Journal of Gastroenterology 10, no. 24 (2004): 3602. http://dx.doi.org/10.3748/wjg.v10.i24.3602.

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19

Malash, Mohamed N., Nahla A. Hussein, Shaden Muawia, Mahmoud I. Nasr, and Rania Siam. "An optimized protocol for high yield expression and purification of an extremophilic protein." Protein Expression and Purification 169 (May 2020): 105585. http://dx.doi.org/10.1016/j.pep.2020.105585.

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20

Wang, Hong, Sidra Charagh, Nannan Dong, et al. "Genome-Wide Analysis of Heat Shock Protein Family and Identification of Their Functions in Rice Quality and Yield." International Journal of Molecular Sciences 25, no. 22 (2024): 11931. http://dx.doi.org/10.3390/ijms252211931.

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Heat shock proteins (Hsps), acting as molecular chaperones, play a pivotal role in plant responses to environmental stress. In this study, we found a total of 192 genes encoding Hsps, which are distributed across all 12 chromosomes, with higher concentrations on chromosomes 1, 2, 3, and 5. These Hsps can be divided into six subfamilies (sHsp, Hsp40, Hsp60, Hsp70, Hsp90, and Hsp100) based on molecular weight and homology. Expression pattern data indicated that these Hsp genes can be categorized into three groups: generally high expression in almost all tissues, high tissue-specific expression,

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21

Choi, Hye-Ji, Dae-Eun Cheong, Su-Kyoung Yoo, Jaehong Park, Dong-Hyun Lee, and Geun-Joong Kim. "Soluble Expression of hFGF19 without Fusion Protein through Synonymous Codon Substitutions and DsbC Co-Expression in E. coli." Microorganisms 8, no. 12 (2020): 1942. http://dx.doi.org/10.3390/microorganisms8121942.

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Human fibroblast growth factor 19 (hFGF19) is a difficult-to-express protein that is frequently fused with another protein for soluble expression. However, residual amino acids after cleavage with protease represent one of the major problems in therapeutic protein development. Here, we introduced synonymous codon substitutions in the N-terminal region encoding sequence of hFGF19 and co-expressed disulfide bond isomerase (ΔssDsbC) to functionally express hFGF19 without any fusion protein. Synonymous codon substitution significantly increased hFGF19 expression. Subsequent co-expression of ΔssDsb

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22

Stammen, Simon, Britta Katrin Müller, Claudia Korneli, et al. "High-Yield Intra- and Extracellular Protein Production Using Bacillus megaterium." Applied and Environmental Microbiology 76, no. 12 (2010): 4037–46. http://dx.doi.org/10.1128/aem.00431-10.

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ABSTRACT The Bacillus megaterium protein production system based on the inducible promoter of the xyl operon (P xylA ) was systematically optimized. Multiple changes in basic promoter elements, such as the −10 and −35 region and the ribosome-binding site, resulted in an 18-fold increase of protein production compared to the production of the previously established system. The production in shaking-flask culture of green fluorescent protein (Gfp) as a model product led to 82.5 mg per g cell dry weight (gCDW) or 124 mg liter−1. In fed-batch cultivation, the volumetric protein yield was increased

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23

Ma, Yi, Liu Cui, Meng Wang, Qiuli Sun, Kaisheng Liu, and Jufang Wang. "A Novel and Efficient High-Yield Method for Preparing Bacterial Ghosts." Toxins 13, no. 6 (2021): 420. http://dx.doi.org/10.3390/toxins13060420.

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Bacterial ghosts (BGs) are empty cell envelopes possessing native extracellular structures without a cytoplasm and genetic materials. BGs are proposed to have significant prospects in biomedical research as vaccines or delivery carriers. The applications of BGs are often limited by inefficient bacterial lysis and a low yield. To solve these problems, we compared the lysis efficiency of the wild-type protein E (EW) from phage ΦX174 and the screened mutant protein E (EM) in the Escherichia coli BL21(DE3) strain. The results show that the lysis efficiency mediated by protein EM was improved. The

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de Grahl, Imke, Sweta Suman Rout, Jodi Maple-Grødem, and Sigrun Reumann. "Development of a constitutive and an auto-inducible high-yield expression system for recombinant protein production in the microalga Nannochloropsis oceanica." Applied Microbiology and Biotechnology 104, no. 20 (2020): 8747–60. http://dx.doi.org/10.1007/s00253-020-10789-4.

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Abstract Photoautotrophic microalgae offer a great potential as novel hosts for efficient recombinant protein production. Nannochloropsis oceanica produces an extraordinarily high content of polyunsaturated fatty acids, and its robust growth characteristics, published genome sequence and efficient nuclear transformation make N. oceanica a promising candidate for biotechnological applications. To establish a robust and flexible system for recombinant protein production, we cloned six endogenous, potentially constitutive or inducible promoters from N. oceanica strain CCMP1779 and investigated th

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Brumfield, Susan, Deborah Willits, Liang Tang, John E. Johnson, Trevor Douglas, and Mark Young. "Heterologous expression of the modified coat protein of Cowpea chlorotic mottle bromovirus results in the assembly of protein cages with altered architectures and function." Journal of General Virology 85, no. 4 (2004): 1049–53. http://dx.doi.org/10.1099/vir.0.19688-0.

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We have developed methods for producing viral-based protein cages in high yield that are amenable to genetic modification. Expression of the structural protein of Cowpea chlorotic mottle bromovirus (CCMV) using the yeast-based Pichia pastoris heterologous expression system resulted in the assembly of particles that were visibly indistinguishable from virus particles produced in the natural host. We have shown that a collection of non-infectious CCMV coat protein mutants expressed in the P. pastoris system assemble into viral protein cages with altered architectures and function. This provides

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Gomez-Lugo, Jessica J., Nestor G. Casillas-Vega, Alma Gomez-Loredo, Isaias Balderas-Renteria, and Xristo Zarate. "High-Yield Expression and Purification of Scygonadin, an Antimicrobial Peptide, Using the Small Metal-Binding Protein SmbP." Microorganisms 12, no. 2 (2024): 278. http://dx.doi.org/10.3390/microorganisms12020278.

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(1) Background: Producing active antimicrobial peptides with disulfide bonds in bacterial strains is challenging. The cytoplasm of Escherichia coli has a reducing environment, which is not favorable to the formation of disulfide bonds. Additionally, E. coli may express proteins as insoluble aggregates known as inclusion bodies and have proteolytic systems that can degrade recombinant peptides. Using E. coli strains like SHuffle and tagging the peptides with fusion proteins is a common strategy to overcome these difficulties. Still, the larger size of carrier proteins can affect the final yield

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Vold, Victoria Amstrup, Sebastian Glanville, Dan Arne Klaerke, and Per Amstrup Pedersen. "pXOOY: A dual-function vector for expression of membrane proteins in Saccharomyces cerevisiae and Xenopus laevis oocytes." PLOS ONE 18, no. 2 (2023): e0281868. http://dx.doi.org/10.1371/journal.pone.0281868.

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On the quest for solving structures of membrane proteins by X-ray crystallography or cryo-EM, large quantities of ultra-pure protein are a paramount prerequisite. Obtaining enough protein of such high standard is not a trivial task, especially for difficult-to-express membrane proteins. Producing membrane protein for structural studies is often performed in Escherichia coli or Saccharomyces cerevisiae and is frequently complemented with functional studies. Ion channels and electrogenic receptors are traditionally studied in terms of their electrophysiological behavior, which cannot be performe

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Khodak, Yulia Alexandrovna, Alexandra Yurievna Ryazanova, Ivan Ivanovich Vorobiev, Alexander Leonidovich Kovalchuk, Nikolay Nikolaevich Ovechko, and Petr Gennadievich Aparin. "High-Level Production of Soluble Cross-Reacting Material 197 in Escherichia coli Cytoplasm Due to Fine Tuning of the Target Gene’s mRNA Structure." BioTech 12, no. 1 (2023): 9. http://dx.doi.org/10.3390/biotech12010009.

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Cross-reacting material 197 (CRM197) is a non-toxic mutant of the diphtheria toxin and is widely used as a carrier protein in conjugate vaccines. This protein was first obtained from the supernatant of the mutant Corynebacterium diphtheriae strain. This pathogenic bacteria strain is characterized by a slow growth rate and a relatively low target protein yield, resulting in high production costs for CRM197. Many attempts have been made to establish high-yield protocols for the heterologous expression of recombinant CRM197 in different host organisms. In the present work, a novel CRM197-producin

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Uhoraningoga, Albert, Gemma Kinsella, Gary Henehan, and Barry Ryan. "The Goldilocks Approach: A Review of Employing Design of Experiments in Prokaryotic Recombinant Protein Production." Bioengineering 5, no. 4 (2018): 89. http://dx.doi.org/10.3390/bioengineering5040089.

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The production of high yields of soluble recombinant protein is one of the main objectives of protein biotechnology. Several factors, such as expression system, vector, host, media composition and induction conditions can influence recombinant protein yield. Identifying the most important factors for optimum protein expression may involve significant investment of time and considerable cost. To address this problem, statistical models such as Design of Experiments (DoE) have been used to optimise recombinant protein production. This review examines the application of DoE in the production of r

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Billerhart, Magdalena, Monika Hunjadi, Vanessa Hawlin, et al. "Recombinant Human CD19 in CHO-K1 Cells: Glycosylation Patterns as a Quality Attribute of High Yield Processes." International Journal of Molecular Sciences 24, no. 13 (2023): 10891. http://dx.doi.org/10.3390/ijms241310891.

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CD19 is an essential protein in personalized CD19-targeting chimeric antigen receptor (CAR)-T cell-based cancer immunotherapies and CAR-T cell functionality evaluation. However, the recombinant expression of this “difficult to-express” (DTE) protein is challenging, and therefore, commercial access to the protein is limited. We have previously described the successful stable expression of our soluble CD19-AD2 fusion protein of the CD19 extracellular part fused with human serum albumin domain 2 (AD2) in CHO-K1 cells. The function, stability, and secretion rate of DTE proteins can be improved by

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Lim, Chin Giaw, Zachary L. Fowler, Thomas Hueller, Steffen Schaffer, and Mattheos A. G. Koffas. "High-Yield Resveratrol Production in Engineered Escherichia coli." Applied and Environmental Microbiology 77, no. 10 (2011): 3451–60. http://dx.doi.org/10.1128/aem.02186-10.

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ABSTRACTPlant polyphenols have been the subject of several recent scientific investigations since many of the molecules in this class have been found to be highly active in the human body, with a plethora of health-promoting activities against a variety of diseases, including heart disease, diabetes, and cancer, and with even the potential to slow aging. Further development of these potent natural therapeutics hinges on the formation of robust industrial production platforms designed using specifically selected as well as engineered protein sources along with the construction of optimal expres

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Hwang, Dong Soo, Seong Hye Lim, Yoon Jeong Yang, and Hyung Joon Cha. "Mass-Production of Practical Mussel Adhesive Protein in Escherichia Coli." Advanced Materials Research 47-50 (June 2008): 857–60. http://dx.doi.org/10.4028/www.scientific.net/amr.47-50.857.

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Mussel adhesive proteins (MAPs) have received increased attention as potential environmentally friendly adhesives under aqueous conditions and in medicine. However, attempts to produce functional recombinant MAPs (mainly foot protein type 1, fp-1) by several expression systems have failed. Even though we previously reported a functional expression of recombinant foot protein type 5 (fp-5) with significant adhesive ability in Escherichia coli, its practical use was limited by several problems such as low production yield, low purification yield, and high levels of post-purification insolubility

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Martin, G. A., R. Kawaguchi, Y. Lam, A. DeGiovanni, M. Fukushima, and W. Mutter. "High-Yield, In Vitro Protein Expression Using a Continuous-Exchange, Coupled Transcription/Translation System." BioTechniques 31, no. 4 (2001): 948–53. http://dx.doi.org/10.2144/01314pf01.

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Wang, Fei, Jiawen Sun, Wenyan Guo, and Yang Wu. "Application of the Insect Cell-Baculovirus Expression Vector System in Adeno-Associated Viral Production." Applied Sciences 14, no. 23 (2024): 10948. http://dx.doi.org/10.3390/app142310948.

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Insect Cell-Baculovirus Expression Vector System (IC-BEVS) is an efficient protein expression platform, which is famous for its high-level expression of complex protein in insect cells. The system is based on baculoviruses such as Autographa californica multiple nucleopolyhedrovirus (AcMNPV), and the expression efficiency of the target proteins has been significantly improved by optimizing the viral vectors and cell lines. In recent years, IC-BEVS have shown great potential for Adeno-Associated Virus (AAV) production, particularly excelling in AAV structural protein expression and recombinant

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Lodi, Tiziana, Barbara Neglia, and Claudia Donnini. "Secretion of Human Serum Albumin by Kluyveromyces lactis Overexpressing KlPDI1 and KlERO1." Applied and Environmental Microbiology 71, no. 8 (2005): 4359–63. http://dx.doi.org/10.1128/aem.71.8.4359-4363.2005.

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ABSTRACT The control of protein conformation during translocation through the endoplasmic reticulum is often a bottleneck for heterologous protein production. The core pathway of the oxidative folding machinery includes two conserved proteins: Pdi1p and Ero1p. We increased the dosage of the genes encoding these proteins in the yeast Kluyveromyces lactis and evaluated the secretion of heterologous proteins. KlERO1, an orthologue of Saccharomyces cerevisiae ERO1, was cloned by functional complementation of the ts phenotype of an Scero1 mutant. The expression of KlERO1 was induced by treatment of

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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 (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 susp

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Yu, Kang, Congjing Cao, Luwen Huang, and Enxu Wang. "Characterization of Escherichia coli as a Recombinant Protein Expression Host and its Optimization." Academic Journal of Science and Technology 12, no. 2 (2024): 223–25. http://dx.doi.org/10.54097/qsa77p06.

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Engineered Escherichia coli serves as an efficient platform for the production of a diverse array of recombinant proteins, thereby addressing the pharmaceutical industry's demand for high-quality biological agents. Nevertheless, challenges related to protein folding and the complexities involved in product purification must be acknowledged. This review delineates the advantages and disadvantages of utilizing E. coli as an expression host and further investigates various strategies aimed at optimizing and enhancing the E. coli expression system to elevate the yield, purity, and biological activ

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Kim, Mijeong, Hijin Kim, Wondo Lee, Yoonjung Lee, Soon-Wook Kwon, and Joohyun Lee. "Quantitative Shotgun Proteomics Analysis of Rice Anther Proteins after Exposure to High Temperature." International Journal of Genomics 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/238704.

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In rice, the stage of development most sensitive to high temperature stress is flowering, and exposure at this stage can result in spikelet sterility, thereby leading to significant yield losses. In this study, protein expression patterns of rice anthers from Dianxi4, a high temperature tolerant Japonica rice variety, were compared between samples exposed to high temperature and those grown in natural field conditions in Korea. Shotgun proteomics analysis of three replicate control and high-temperature-treated samples identified 3,266 nonredundant rice anther proteins (false discovery rate &lt

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Li, Zhengchun, Zijing Zhou, Qiandong Hou, Luonan Shen, Hong Zhao, and Xiaopeng Wen. "Physiological, Proteomic, and Resin Yield-Related Genes Expression Analysis Provides Insights into the Mechanisms Regulating Resin Yield in Masson Pine." International Journal of Molecular Sciences 24, no. 18 (2023): 13813. http://dx.doi.org/10.3390/ijms241813813.

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Masson pine (Pinus massoniana Lamb.) is an important resin-producing conifer species in China. Resin yield is a highly heritable trait and varies greatly among different genotypes. However, the mechanisms regulating the resin yield of masson pine remain largely unknown. In this study, physiological, proteomic, and gene expression analysis was performed on xylem tissues of masson pine with high and low resin yield. Physiological investigation showed that the activity of terpene synthase, as well as the contents of soluble sugar, jasmonic acid (JA), methyl jasmonate (MeJA), gibberellins (GA1, GA

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Ecker, Jeffrey W., Greg A. Kirchenbaum, Spencer R. Pierce, et al. "High-Yield Expression and Purification of Recombinant Influenza Virus Proteins from Stably-Transfected Mammalian Cell Lines." Vaccines 8, no. 3 (2020): 462. http://dx.doi.org/10.3390/vaccines8030462.

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Influenza viruses infect millions of people each year, resulting in significant morbidity and mortality in the human population. Therefore, generation of a universal influenza virus vaccine is an urgent need and would greatly benefit public health. Recombinant protein technology is an established vaccine platform and has resulted in several commercially available vaccines. Herein, we describe the approach for developing stable transfected human cell lines for the expression of recombinant influenza virus hemagglutinin (HA) and recombinant influenza virus neuraminidase (NA) proteins for the pur

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Wutt, Daqing, Jiong Shen, and Binggen Ru. "Expression and purification of human metallothionein-3 beta domain in e.coli." Protein & Peptide Letters 7, no. 4 (2000): 257–63. http://dx.doi.org/10.2174/092986650704221207123557.

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Abstract: J3-domain of metallothionein-3/growth inhibitory factor(MT-3/GIF) is crucial to the neuronal growth inhibitory activity of MT-3. The MT-3 J3 domain was efficiently expressed as the soluble fusion form with GST protein at a high level which accounted for over 30% total cellular proteins. After the thrombin cleavage and purification, the bioactive recombinant MT-3 J3 domain was recovered with the yield of 6 mg/L of medium.

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Hardy, David, Roslyn M. Bill, Anass Jawhari, and Alice J. Rothnie. "Functional Expression of Multidrug Resistance Protein 4 MRP4/ABCC4." SLAS DISCOVERY: Advancing the Science of Drug Discovery 24, no. 10 (2019): 1000–1008. http://dx.doi.org/10.1177/2472555219867070.

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To study the function and structure of membrane proteins, high quantities of pure and stable protein are needed. One of the first hurdles in accomplishing this is expression of the membrane protein at high levels and in a functional state. Membrane proteins are naturally expressed at low levels, so finding a suitable host for overexpression is imperative. Multidrug resistance protein 4 (MRP4) or ATP-binding cassette subfamily C member 4 (ABCC4) is a multi-transmembrane protein that is able to transport a range of organic anionic compounds (both endogenous and xenobiotic) out of the cell. This

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Cardoso, Vânia, Joana L. A. Brás, Inês F. Costa, et al. "Generation of a Library of Carbohydrate-Active Enzymes for Plant Biomass Deconstruction." International Journal of Molecular Sciences 23, no. 7 (2022): 4024. http://dx.doi.org/10.3390/ijms23074024.

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In nature, the deconstruction of plant carbohydrates is carried out by carbohydrate-active enzymes (CAZymes). A high-throughput (HTP) strategy was used to isolate and clone 1476 genes obtained from a diverse library of recombinant CAZymes covering a variety of sequence-based families, enzyme classes, and source organisms. All genes were successfully isolated by either PCR (61%) or gene synthesis (GS) (39%) and were subsequently cloned into Escherichia coli expression vectors. Most proteins (79%) were obtained at a good yield during recombinant expression. A significantly lower number (p < 0

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Wang, Yi, Xiaolong Yuan, Siguang Li, Wei Chen, and Jiang Li. "Gene cloning and functional characterization of three 1-deoxy-D-xylulose 5-phosphate synthases in Simao pine." BioResources 13, no. 3 (2018): 6370–82. http://dx.doi.org/10.15376/biores.13.3.6370-6382.

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Pine oleoresin is an important industrial resource, used widely in pharmaceuticals, cosmetics, and insecticides. To reveal the function of 1-deoxy-D-xylulose 5-phosphate synthase (DXS) in oleoresin biosynthesis in Simao pine, three complete cDNAs of DXS genes were obtained, of lengths 2223 bp (PkDXS1), 2217 bp (PkDXS2), and 2142 bp (PkDXS3). Phylogenetic analysis showed that PkDXS1 belonged to DXS type 1, and both PkDXS2 and PkDXS3 belonged to DXS type 2. Functional complementation experiments indicated that the three PkDXS genes had DXS protein function. Real-time PCR detection showed that ph

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Snead, Kelly, Vanessa Wall, Hannah Ambrose, Dominic Esposito, and Matthew Drew. "Polycistronic baculovirus expression of SUGT1 enables high-yield production of recombinant leucine-rich repeat proteins and protein complexes." Protein Expression and Purification 193 (May 2022): 106061. http://dx.doi.org/10.1016/j.pep.2022.106061.

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Morão, Luana G., Lívia R. Manzine, Lívia Oliveira D. Clementino, Carsten Wrenger, and Alessandro S. Nascimento. "A scalable screening of E. coli strains for recombinant protein expression." PLOS ONE 17, no. 7 (2022): e0271403. http://dx.doi.org/10.1371/journal.pone.0271403.

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Structural biology projects are highly dependent on the large-scale expression of soluble protein and, for this purpose, heterologous expression using bacteria or yeast as host systems is usually employed. In this scenario, some of the parameters to be optimized include (i) those related to the protein construct, such as the use of a fusion protein, the choice of an N-terminus fusion/tag or a C-terminus fusion/tag; (ii) those related to the expression stage, such as the concentration and selection of inducer agent and temperature expression and (iii) the choice of the host system, which includ

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Alberghina, L., D. Porro, E. Martegani, and BM Ranzi. "Efficient production of recombinant DNA proteins in Saccharomyces cerevisiae by controlled high‐cell‐density fermentation." Biotechnology and Applied Biochemistry 14, no. 1 (1991): 82–92. http://dx.doi.org/10.1111/j.1470-8744.1991.tb00168.x.

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High levels of expression of heterologous proteins (from 5 to 15% of total cell proteins) in the budding yeast Saccharomyces cerevisiae have been obtained previously by the use of the inducible strong hybrid promoter UASGAL/CYC1, in batch as well in continuous cultures. However, in order to maximize the yield of heterologous proteins, a computer controlled fed‐batch fermentation is essential. For this reason we have developed a fed‐batch system based on a semiconductor gas detector that measures ethanol in the outflow gases. The optimal conditions are described for very high production (up to

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Chi, Kaijun, Huilin Xu, Hanjie Li, Ganglong Yang, Xiaoman Zhou, and Xiao-Dong Gao. "Expression of a Siglec-Fc Protein and Its Characterization." Biology 12, no. 4 (2023): 574. http://dx.doi.org/10.3390/biology12040574.

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The emerging importance of the Siglec-sialic acid axis in human disease, especially cancer, has necessitated the identification of ligands for Siglecs. Recombinant Siglec-Fc fusion proteins have been widely used as ligand detectors, and also as sialic acid-targeted antibody-like proteins for cancer treatment. However, the heterogenetic properties of the Siglec-Fc fusion proteins prepared from various expression systems have not been fully elucidated. In this study, we selected HEK293 and CHO cells for producing Siglec9-Fc and further evaluated the properties of the products. The protein yield

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Xia, Wei, Mengkai Hu, Yang Pan, Dan Wu, and Jing Wu. "Improved Production of Streptomyces sp. FA1 Xylanase in a Dual-Plasmid Pichia pastoris System." Current Issues in Molecular Biology 43, no. 3 (2021): 2289–304. http://dx.doi.org/10.3390/cimb43030161.

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Methanol is considered as a potential hazard in the methanol-induced yeast expression of food-related enzymes. To increase the production efficiency of recombinant proteins in Pichia pastoris without methanol induction, a novel dual-plasmid system was constructed, for the first time, by a combining the strategies of genomic integration and episomal expression. To obtain a high copy number of the target gene, the autonomously replicating sequence derived from Kluyveromyces lactis (PARS) was used to construct episomal vectors carrying the constitutive promoters PGAP and PGCW14. In addition, an i

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Chen, Wei, Caiqian Zhang, Yeqing Wu, and Xiuping Su. "Soluble expression and purification of high-bioactivity recombinant human bone morphogenetic protein-2 by codon optimisation in Escherichia coli." Protein Engineering, Design and Selection 32, no. 3 (2019): 153–57. http://dx.doi.org/10.1093/protein/gzz028.

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Abstract We developed a simple method of preparing recombinant human bone morphogenetic protein-2 (rhBMP-2) with high biological activity. This rhBMP-2 was overproduced in Escherichia coli as a fusion protein with thioredoxin 6xHis-tag at its amino terminus. The cDNA fragment of human bone morphogenetic protein-2 (hBMP-2) fused to the secretion signal of alkaline phosphatase (PhoA) was expressed under T7 promoter in E. coli. After DNA sequence confirmation, the recombinant vector pETpho-bmp2 was transformed into E. coli BL21 (DE3). rhBMP-2 was produced by the recombinant strain pETpho-bmp2/BL2

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