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Recombinant Proteins for Molecular Biology Research: Technologies and Applications

A special issue of Current Issues in Molecular Biology (ISSN 1467-3045). This special issue belongs to the section "Biochemistry, Molecular and Cellular Biology".

Deadline for manuscript submissions: 30 April 2025 | Viewed by 3691

Special Issue Editors

Dr. Tsutomu Arakawa

E-Mail Website
Guest Editor
Alliance Protein Laboratories, 6042 Cornerstone Ct West, Suite A1, San Diego, CA 92121, USA
Interests: modulation of aqueous protein solution by solvents
Special Issues, Collections and Topics in MDPI journals
Dr. Yasunari Matsuzaka

E-Mail Website
Guest Editor
Division of Molecular and Medical Genetics, Center for Gene and Cell Therapy, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108-8639, Japan
Interests: extracellular vesicles; vaccine; cancer; mRNA; microRNAs; immune responses; T cells; dendritic cells; major histocompatibility complex (MHC); deep learning; virus
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The Special Issue “Recombinant Proteins for Molecular Biology Research: Technologies and Applications” welcomes contributions from experts in the following areas of recombinant protein production:

  1. Protein vaccines.

With the recent COVID-19 pandemic, it has become clear how important it is to be able to generate vaccines in a timely fashion, and recombinant protein vaccines are one method of doing so.

  1. Intra-cellular signaling factors.

There are many potential intra-cellular signaling proteins, which play a key role in cell metabolism and diseases. The availability of these proteins helps us to understand their roles in metabolic processes and diseases and also to develop drugs that target these signaling proteins.

  1. Membrane proteins.

Membrane proteins are the most important target of therapeutic drugs. The ability to generate purified and functional membrane proteins helps to develop rational drug designs.

Dr. Tsutomu Arakawa
Dr. Yasunari Matsuzaka
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Current Issues in Molecular Biology is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • recombinant proteins
  • vaccine
  • intra-cellular signaling factors
  • membrane proteins
  • drug targets

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Published Papers (3 papers)

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Research

11 pages, 3387 KiB  
Article
Recombinant C-Terminal Catalytic Domain of Rat L-Gulono Lactone Oxidase Produced in Bacterial Cells Is Enzymatically Active
by Abdul Aziz M. Gad, Anna Gora-Sochacka and Agnieszka Sirko
Curr. Issues Mol. Biol. 2024, 46(8), 8958-8968; https://doi.org/10.3390/cimb46080529 - 16 Aug 2024
Cited by 1 | Viewed by 718
Abstract
The L-gulonolactone oxidase enzyme (GULO) catalyzes the last step of L-ascorbic acid (vitamin C) biosynthesis. This enzymatic activity is lost in primates. The full-length rat GULO has been previously produced in plants and demonstrated to be active. In this study, we compared the [...] Read more.
The L-gulonolactone oxidase enzyme (GULO) catalyzes the last step of L-ascorbic acid (vitamin C) biosynthesis. This enzymatic activity is lost in primates. The full-length rat GULO has been previously produced in plants and demonstrated to be active. In this study, we compared the activity of two variants of GULO produced in Escheriachia coli cells, full-length rat GULO (fGULO) and its C-terminal catalytic domain (cGULO). The expression and purification of the recombinant proteins were optimized, and their biological activity was confirmed by two methods, the GULO activity assay in the protein extracts and the ‘in-gel’ staining for GULO activity. Both variants of recombinant GULO were biologically active in both assays. However, cGULO is more promising than fGULO for ascorbic acid production because it is more efficiently produced by bacteria. Furthermore, the optimal activities of the fGULO and cGULO recombinant proteins were observed at pH 7 and 6.5, and at temperatures of 40 and 30 °C, respectively. Kinetic studies revealed that at low substrate concentrations, Km values for fGULO and cGULO were 53.5 ± 5 and 42 ± 6.3 µM, respectively. Full article
(This article belongs to the Special Issue Recombinant Proteins for Molecular Biology Research: Technologies and Applications)
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15 pages, 721 KiB  
Article
Stable Production of a Tethered Recombinant Eel Luteinizing Hormone Analog with High Potency in CHO DG44 Cells
by Munkhzaya Byambaragchaa, Sei Hyen Park, Sang-Gwon Kim, Min Gyu Shin, Shin-Kwon Kim, Sung-Pyo Hur, Myung-Hum Park, Myung-Hwa Kang and Kwan-Sik Min
Curr. Issues Mol. Biol. 2024, 46(6), 6085-6099; https://doi.org/10.3390/cimb46060363 - 15 Jun 2024
Cited by 1 | Viewed by 1119
Abstract
We produced a recombinant eel luteinizing hormone (rec-eel LH) analog with high potency in Chinese hamster ovary DG44 (CHO DG44) cells. The tethered eel LH mutant (LH-M), which had a linker comprising the equine chorionic gonadotropin (eLH/CG) β-subunit carboxyl-terminal peptide (CTP) region (amino [...] Read more.
We produced a recombinant eel luteinizing hormone (rec-eel LH) analog with high potency in Chinese hamster ovary DG44 (CHO DG44) cells. The tethered eel LH mutant (LH-M), which had a linker comprising the equine chorionic gonadotropin (eLH/CG) β-subunit carboxyl-terminal peptide (CTP) region (amino acids 115 to 149), was inserted between the β-subunit and α-subunit of wild-type tethered eel LH (LH-wt). Monoclonal cells transfected with the tethered eel LH-wt and eel LH-M plasmids were isolated from five to nine clones of CHO DG44 cells, respectively. The secreted quantities abruptly increased on day 3, with peak levels of 5000–7500 ng/mL on day 9. The molecular weight of tethered rec-eel LH-wt was 32–36 kDa, while that of tethered rec-eel LH-M increased to approximately 38–44 kDa, indicating the detection of two bands. Treatment with the peptide N-glycanase F decreased the molecular weight by approximately 8 kDa. The oligosaccharides at the eCG β-subunit O-linked glycosylation sites were appropriately modified post-translation. The EC50 value and maximal responsiveness of eel LH-M increased by approximately 2.90- and 1.29-fold, respectively, indicating that the mutant exhibited more potent biological activity than eel LH-wt. Phosphorylated extracellular regulated kinase (pERK1/2) activation resulted in a sharp peak 5 min after agonist treatment, with a rapid decrease thereafter. These results indicate that the new tethered rec-eel LH analog had more potent activity in cAMP response than the tethered eel LH-wt in vitro. Taken together, this new eel LH analog can be produced in large quantities using a stable CHO DG44 cell system. Full article
(This article belongs to the Special Issue Recombinant Proteins for Molecular Biology Research: Technologies and Applications)
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Graphical abstract

14 pages, 4198 KiB  
Communication
Surface Engineering of Escherichia coli to Display Its Phytase (AppA) and Functional Analysis of Enzyme Activities
by Patricia L. A. Muñoz-Muñoz, Celina Terán-Ramírez, Rosa E. Mares-Alejandre, Ariana B. Márquez-González, Pablo A. Madero-Ayala, Samuel G. Meléndez-López and Marco A. Ramos-Ibarra
Curr. Issues Mol. Biol. 2024, 46(4), 3424-3437; https://doi.org/10.3390/cimb46040215 - 17 Apr 2024
Cited by 1 | Viewed by 1544
Abstract
Escherichia coli phytase (AppA) is widely used as an exogenous enzyme in monogastric animal feed mainly because of its ability to degrade phytic acid or its salt (phytate), a natural source of phosphorus. Currently, successful recombinant production of soluble AppA has been achieved [...] Read more.
Escherichia coli phytase (AppA) is widely used as an exogenous enzyme in monogastric animal feed mainly because of its ability to degrade phytic acid or its salt (phytate), a natural source of phosphorus. Currently, successful recombinant production of soluble AppA has been achieved by gene overexpression using both bacterial and yeast systems. However, some methods for the biomembrane immobilization of phytases (including AppA), such as surface display on yeast cells and bacterial spores, have been investigated to avoid expensive enzyme purification processes. This study explored a homologous protein production approach for displaying AppA on the cell surface of E. coli by engineering its outer membrane (OM) for extracellular expression. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of total bacterial lysates and immunofluorescence microscopy of non-permeabilized cells revealed protein expression, whereas activity assays using whole cells or OM fractions indicated functional enzyme display, as evidenced by consistent hydrolytic rates on typical substrates (i.e., p-nitrophenyl phosphate and phytic acid). Furthermore, the in vitro results obtained using a simple method to simulate the gastrointestinal tract of poultry suggest that the whole-cell biocatalyst has potential as a feed additive. Overall, our findings support the notion that biomembrane-immobilized enzymes are reliable for the hydrolysis of poorly digestible substrates relevant to animal nutrition. Full article
(This article belongs to the Special Issue Recombinant Proteins for Molecular Biology Research: Technologies and Applications)
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