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Recent Advances in Antibody Therapeutics 2.0
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Recent Advances in Antibody Therapeutics 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pharmacology".

Deadline for manuscript submissions: closed (31 May 2023) | Viewed by 11707

Special Issue Editor

Prof. Dr. Yong-Seok Heo

E-Mail Website
Guest Editor
Department of Chemistry, Konkuk University, Seoul 05029, Republic of Korea
Interests: therapeutic antibody; cancer immunotherapy; antibody engineering; structure and mechanism of antibody drugs; protein structure
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue follows the publication of the first edition on “Recent Advances in Antibody Therapeutics”, which presented 10 more high-quality papers.

Antibody-based therapeutics have achieved unprecedented success for the treatment of various diseases, including cancer, immune disorders, and infectious diseases. The recent success in immune checkpoint inhibitors and chimeric antigen receptor T cells (CAR-T) has provided a major breakthrough in cancer immunotherapy. Therapeutic antibodies are also expected to play a role in the prevention and treatment of the coronavirus pandemic (COVID-19).

These achievements in the field of antibody therapeutics are related to major advances in antibody engineering for the generation of safe, specific, high-affinity, and non-immunogenic antibodies during the last few decades. In addition, currently, a major area of antibody research and development includes the discovery of novel targets and novel antibodies, gradual improvements in the characteristics of the existing antibodies, combining antibodies such as bispecific antibodies, antibody–drug conjugates (ADC), CAR-T cells, bispecific T-cell engagers (BiTE), and developing novel antibody-based scaffolds with superior properties to those already in use.

This Special Issue will cover all aspects of the role and mechanism of antibody-based therapeutics in disease treatment, recent advances in antibody engineering, and noteworthy antibody-based products under investigation for treating various diseases. Original papers and review articles are welcomed.

Prof. Dr. Yong-Seok Heo
Guest Editor

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • therapeutic antibody
  • antibody–drug conjugate (ADC)
  • chimeric antigen receptor T cell (CAR-T)
  • bispecific antibody
  • bispecific T-cell engager (BiTE)
  • nanobody
  • immunotherapy
  • cancer
  • autoimmune disease
  • infectious disease
  • COVID-19
  • biosimilar
  • antibody engineering
  • structure and mechanism of antibody drugs

Published Papers (3 papers)

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Research

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15 pages, 3036 KiB  
Article
A Novel Antibody-Drug Conjugate Targeting Nectin-2 Suppresses Ovarian Cancer Progression in Mouse Xenograft Models
by Yun Hee Sim, Yun Jung Um, Jeong-Yang Park, Min-Duk Seo and Sang Gyu Park
Int. J. Mol. Sci. 2022, 23(20), 12358; https://doi.org/10.3390/ijms232012358 - 15 Oct 2022
Cited by 5 | Viewed by 2557
Abstract
Ovarian cancer is the fifth leading cause of cancer, followed by front line is mostly platinum agents and PARP inhibitors, and very limited option in later lines. Therefore, there is a need for alternative therapeutic options. Nectin-2, which is overexpressed in ovarian cancer, [...] Read more.
Ovarian cancer is the fifth leading cause of cancer, followed by front line is mostly platinum agents and PARP inhibitors, and very limited option in later lines. Therefore, there is a need for alternative therapeutic options. Nectin-2, which is overexpressed in ovarian cancer, is a known immune checkpoint that deregulates immune cell function. In this study, we generated a novel anti-nectin-2 antibody (chimeric 12G1, c12G1), and further characterized it using epitope mapping, enzyme-linked immunosorbent assay, surface plasmon resonance, fluorescence-activated cell sorting, and internalization assays. The c12G1 antibody specifically bound to the C2 domain of human nectin-2 with high affinity (KD = 2.90 × 10−10 M), but not to mouse nectin-2. We then generated an antibody-drug conjugate comprising the c12G1 antibody conjugated to DM1 and investigated its cytotoxic effects against cancer cells in vitro and in vivo. c12G1-DM1 induced cell cycle arrest at the mitotic phase in nectin-2-positive ovarian cancer cells, but not in nectin-2-negative cancer cells. c12G1-DM1 induced ~100-fold cytotoxicity in ovarian cancer cells, with an IC50 in the range of 0.1 nM~7.4 nM, compared to normal IgG-DM1. In addition, c12G1-DM1 showed ~91% tumor growth inhibition in mouse xenograft models transplanted with OV-90 cells. These results suggest that c12G1-DM1 could be used as a potential therapeutic agent against nectin-2-positive ovarian cancers. Full article
(This article belongs to the Special Issue Recent Advances in Antibody Therapeutics 2.0)
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15 pages, 2162 KiB  
Article
Isolated Variable Domains of an Antibody Can Assemble on Blood Coagulation Factor VIII into a Functional Fv-like Complex
by Svetlana A. Shestopal, Leonid A. Parunov, Philip Olivares, Haarin Chun, Mikhail V. Ovanesov, John R. Pettersson and Andrey G. Sarafanov
Int. J. Mol. Sci. 2022, 23(15), 8134; https://doi.org/10.3390/ijms23158134 - 23 Jul 2022
Cited by 2 | Viewed by 1973
Abstract
Single-chain variable fragments (scFv) are antigen-recognizing variable fragments of antibodies (FV) where both subunits (VL and VH) are connected via an artificial linker. One particular scFv, iKM33, directed against blood coagulation factor VIII (FVIII) was shown to inhibit major FVIII [...] Read more.
Single-chain variable fragments (scFv) are antigen-recognizing variable fragments of antibodies (FV) where both subunits (VL and VH) are connected via an artificial linker. One particular scFv, iKM33, directed against blood coagulation factor VIII (FVIII) was shown to inhibit major FVIII functions and is useful in FVIII research. We aimed to investigate the properties of iKM33 enabled with protease-dependent disintegration. Three variants of iKM33 bearing thrombin cleavage sites within the linker were expressed using a baculovirus system and purified by two-step chromatography. All proteins retained strong binding to FVIII by surface plasmon resonance, and upon thrombin cleavage, dissociated into VL and VH as shown by size-exclusion chromatography. However, in FVIII activity and low-density lipoprotein receptor-related protein 1 binding assays, the thrombin-cleaved iKM33 variants were still inhibitory. In a pull-down assay using an FVIII-affinity sorbent, the isolated VH, a mixture of VL and VH, and intact iKM33 were carried over via FVIII analyzed by electrophoresis. We concluded that the isolated VL and VH assembled into scFv-like heterodimer on FVIII, and the isolated VH alone also bound FVIII. We discuss the potential use of both protease-cleavable scFvs and isolated Fv subunits retaining high affinity to the antigens in various practical applications such as therapeutics, diagnostics, and research. Full article
(This article belongs to the Special Issue Recent Advances in Antibody Therapeutics 2.0)
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Review

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21 pages, 1084 KiB  
Review
Camelid Single-Domain Antibodies: Promises and Challenges as Lifesaving Treatments
by Mehdi Arbabi-Ghahroudi
Int. J. Mol. Sci. 2022, 23(9), 5009; https://doi.org/10.3390/ijms23095009 - 30 Apr 2022
Cited by 40 | Viewed by 6475
Abstract
Since the discovery of camelid heavy-chain antibodies in 1993, there has been tremendous excitement for these antibody domains (VHHs/sdAbs/nanobodies) as research tools, diagnostics, and therapeutics. Commercially, several patents were granted to pioneering research groups in Belgium and the Netherlands between 1996–2001. Ablynx was [...] Read more.
Since the discovery of camelid heavy-chain antibodies in 1993, there has been tremendous excitement for these antibody domains (VHHs/sdAbs/nanobodies) as research tools, diagnostics, and therapeutics. Commercially, several patents were granted to pioneering research groups in Belgium and the Netherlands between 1996–2001. Ablynx was established in 2001 with the aim of exploring the therapeutic applications and development of nanobody drugs. Extensive efforts over two decades at Ablynx led to the first approved nanobody drug, caplacizumab (Cablivi) by the EMA and FDA (2018–2019) for the treatment of rare blood clotting disorders in adults with acquired thrombotic thrombocytopenic purpura (TPP). The relatively long development time between camelid sdAb discovery and their entry into the market reflects the novelty of the approach, together with intellectual property restrictions and freedom-to-operate issues. The approval of the first sdAb drug, together with the expiration of key patents, may open a new horizon for the emergence of camelid sdAbs as mainstream biotherapeutics in the years to come. It remains to be seen if nanobody-based drugs will be cheaper than traditional antibodies. In this review, I provide critical perspectives on camelid sdAbs and present the promises and challenges to their widespread adoption as diagnostic and therapeutic agents. Full article
(This article belongs to the Special Issue Recent Advances in Antibody Therapeutics 2.0)
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