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Bioengineering
Special Issues
Development of Therapeutic Antibodies and Their Antigens for Treatment of...
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Development of Therapeutic Antibodies and Their Antigens for Treatment of Disease

A special issue of Bioengineering (ISSN 2306-5354). This special issue belongs to the section "Biochemical Engineering".

Deadline for manuscript submissions: closed (15 July 2023) | Viewed by 6010

Special Issue Editors

Dr. Jung-Hyun Na

E-Mail Website
Guest Editor
Department of Pharmaceutical Engineering, Sangji University, Wonju 26339, Korea
Interests: Protein engineering; Protein Structure; Antibody discovery; Single domain antibody; Therapeutic antigen; Intrinsically disordered protein; Membrane protein
Dr. Tae Hyun Kang

E-Mail Website
Guest Editor
Department of Biopharmaceutical Chemistry, Kookmin University, 77 Jeongneung-ro, Seongbuk-gu, Seoul 02707, Korea
Interests: antibody engineering; therapeutic antibodies

Special Issue Information

Dear Colleagues,

Therapeutic antibodies have become the prevailing class of novel therapeutic drug candidates in recent years, due to their high specificity and fewer adverse effects. As a result, new antibody drugs have been developed to treat various human diseases, including cancers, infectious diseases, and autoimmune diseases, which has led to unprecedented growth in the pharmaceutical market.

This Special Issue covers the development of antibody drugs (or candidates), the latest advances in the discovery, engineering, validation, and manufacturing of therapeutic antibodies, and novel antibody-based therapeutic platforms, including bispecific-antibodies, single-domain antibodies, and antibody–drug conjugates. This Special Issue invites both original research and reviews.

Dr. Jung-Hyun Na
Dr. Tae Hyun Kang
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. Bioengineering 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 2700 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

  • antibody
  • biopharmaceuticals
  • biologics
  • therapeutic biological product
  • antibody discovery
  • antibody engineering
  • antibody validation
  • antibody manufacturing
  • bispecific antibody
  • single-domain antibody
  • antibody–drug conjugate
  • therapeutic drug target

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Published Papers (2 papers)

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Research

11 pages, 11786 KiB  
Article
Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm of Escherichia coli
by Woo Sung Kim, Ji Hyun Kim, Jisun Lee, Su Yeon Ka, Hee Do Chae, Inji Jung, Sang Taek Jung and Jung-Hyun Na
Bioengineering 2022, 9(11), 670; https://doi.org/10.3390/bioengineering9110670 - 10 Nov 2022
Cited by 4 | Viewed by 2551
Abstract
A new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant known as Omicron has caused a rapid increase in recent global patients with coronavirus infectious disease 2019 (COVID-19). To overcome the COVID-19 Omicron variant, production of a recombinant spike receptor binding domain (RBD) [...] Read more.
A new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant known as Omicron has caused a rapid increase in recent global patients with coronavirus infectious disease 2019 (COVID-19). To overcome the COVID-19 Omicron variant, production of a recombinant spike receptor binding domain (RBD) is vital for developing a subunit vaccine or a neutralizing antibody. Although bacterial expression has many advantages in the production of recombinant proteins, the spike RBD expressed in a bacterial system experiences a folding problem related to disulfide bond formation. In this study, the soluble Omicron RBD was obtained by a disulfide isomerase-assisted periplasmic expression system in Escherichia coli. The Omicron RBD purified from E. coli was very well recognized by anti-SARS-CoV-2 antibodies, sotrovimab (S309), and CR3022, which were previously reported to bind to various SARS-CoV-2 variants. In addition, the kinetic parameters of the purified Omicron RBD upon binding to the human angiotensin-converting enzyme 2 (ACE2) were similar to those of the Omicron RBD produced in the mammalian expression system. These results suggest that an E. coli expression system would be suitable to produce functional and correctly folded spike RBDs of the next emerging SARS-CoV-2 variants quickly and inexpensively. Full article
(This article belongs to the Special Issue Development of Therapeutic Antibodies and Their Antigens for Treatment of Disease)
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19 pages, 2477 KiB  
Article
A Multi-Specific DARPin Potently Neutralizes Shiga Toxin 2 via Simultaneous Modulation of Both Toxin Subunits
by Yu Zeng, Mengqiu Jiang, Sally Robinson, Zeyu Peng, Vikas Chonira, Rudo Simeon, Saul Tzipori, Junjie Zhang and Zhilei Chen
Bioengineering 2022, 9(10), 511; https://doi.org/10.3390/bioengineering9100511 - 27 Sep 2022
Cited by 2 | Viewed by 2856
Abstract
Shiga toxin-producing E. coli (STEC) is a common cause of bloody diarrhea. The pathology of STEC infection derives from two exotoxins—Shiga toxin 1 (Stx1) and Shiga toxin 2 (Stx2)—that are secreted by STEC in the gut, from where they are systemically absorbed, causing [...] Read more.
Shiga toxin-producing E. coli (STEC) is a common cause of bloody diarrhea. The pathology of STEC infection derives from two exotoxins—Shiga toxin 1 (Stx1) and Shiga toxin 2 (Stx2)—that are secreted by STEC in the gut, from where they are systemically absorbed, causing severe kidney damage leading to hemolytic uremic syndrome (HUS). Currently, there is no effective treatment for HUS, and only supportive care is recommended. We report the engineering of a panel of designed ankyrin repeat proteins (DARPin) with potent neutralization activity against Stx2a, the major subtype associated with HUS. The best dimeric DARPin, SD5, created via a combination of directed evolution and rational design, neutralizes Stx2a with a half maximal effective concentration (EC50) of 0.61 nM in vitro. The two monomeric DARPin constituents of SD5 exhibit complementary functions—SHT targets the enzymatic A subunit of Stx2a and inhibits the toxin’s catalytic activity, while DARPin #3 binds the B subunit, based on the cryo-EM study, and induces a novel conformational change in the B subunit that distorts its five-fold symmetry and presumably interferes with toxin attachment to target cells. SD5 was fused to an albumin-binding DARPin, and the resulting trimeric DARPin DA1-SD5 efficiently protects mice in a toxin challenge model, pointing to a high potential of this DARPin as a therapeutic for STEC infection. Finally, the unprecedented toxin conformational change induced by DARPin #3 represents a novel mode of action for neutralizing Stx2 toxicity and reveals new targets for future drug development. Full article
(This article belongs to the Special Issue Development of Therapeutic Antibodies and Their Antigens for Treatment of Disease)
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