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Advances in Therapeutic Antibody Engineering

A Special Issue of International Journal of Molecular Sciences (ISSN 1422-0067) belonging to the section "Molecular Immunology".

Deadline for manuscript submissions: 30 April 2027 | Viewed by 625

Editor


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Guest Editor
1. Center of Biomolecular Therapy and Diagnostic, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
2. Division of Clinical Immunology, Department of Medical Technology, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
Interests: immunology; protein engineering; gene therapy

Special Issue Information

Dear Colleagues,

The landscape of therapeutic antibodies is undergoing a profound transformation. Evolving beyond traditional monospecific formats, the current wave of innovation is driven by complex, multifunctional molecules designed to unlock novel mechanisms of action and overcome clinical resistance.

This Special Issue focuses on the rapid ascent of next-generation antibody therapeutics. We highlight breakthroughs in bispecific and multispecific antibodies, the resurgence of antibody-drug conjugates (ADCs) featuring novel payloads and smarter linkers, and the unique advantages of nanobodies for challenging targets. Furthermore, we emphasize the transformative impact of artificial intelligence (AI) and machine learning in accelerating de novo antibody design and predictive developability.

We invite researchers to submit original articles and reviews covering antibody design, optimization, and clinical applications. Join us in showcasing the cutting-edge engineering strategies that are redefining precision medicine across oncology, autoimmune disorders, and beyond.

Prof. Dr. Chatchai Tayapiwatana
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 250 words) can be sent to the Editorial Office for assessment.

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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 antibodies
  • bispecific antibodies
  • antibody-drug conjugates (ADCs)
  • nanobodies
  • AI-driven drug design
  • Fc engineering
  • immunotherapy

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Published Papers (1 paper)

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Research

13 pages, 985 KB  
Article
Generation and Characterization of the Human Anti-HTNV Antibody KJJ4
by Ziyan Chen, Yanbo Wang, Yongli Hou, Liang Fang, Linfeng Cheng, Yusi Zhang, Chunmei Zhang, Yun Zhang, Ying Ma, Kang Tang and Lihua Chen
Int. J. Mol. Sci. 2026, 27(18), 7994; https://doi.org/10.3390/ijms27187994 - 8 Sep 2026
Viewed by 161
Abstract
Hantaan virus (HTNV) is the predominant causative agent of hemorrhagic fever with renal syndrome (HFRS) in China, yet no specific antiviral therapy is currently available. Neutralizing antibodies (NAbs) represent a promising strategy, but most existing anti-HTNV NAbs are heterologous and carry immunogenicity risks. [...] Read more.
Hantaan virus (HTNV) is the predominant causative agent of hemorrhagic fever with renal syndrome (HFRS) in China, yet no specific antiviral therapy is currently available. Neutralizing antibodies (NAbs) represent a promising strategy, but most existing anti-HTNV NAbs are heterologous and carry immunogenicity risks. Here, two fully human antibodies from a previously established human anti-HTNV phage display library were generated and characterized. KJJ3, a VL-VL tandem antibody derived from clone 3–12, showed weak binding to inactivated HTNV and minimal neutralizing activity (IC50 = 27.12 μg/mL). However, KJJ4, an engineered IgG4 antibody derived from clone 4–19 and carrying the S108P hinge mutation to prevent Fab-arm exchange, bound inactivated HTNV antigen and recombinant glycoprotein Gn (residues 19–371) in a dose-dependent manner, with only weak binding to Gc. Surface plasmon resonance yielded an association rate constant of 4.70 × 103 M−1s−1, a dissociation rate constant of 3.06 × 10−3 s−1, and an equilibrium dissociation constant of 650 nM for monomeric Gn19–371. In a Vero E6 focus-reduction microneutralization assay, KJJ4 neutralized HTNV in vitro with an IC50 of 2.879 μg/mL. These data establish KJJ4 as a fully human anti-HTNV antibody with experimentally defined in vitro binding and neutralizing activity, warranting further evaluation in animal models of HTNV infection. Full article
(This article belongs to the Special Issue Advances in Therapeutic Antibody Engineering)
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