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Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0

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

Deadline for manuscript submissions: closed (20 December 2024) | Viewed by 14744

Special Issue Editors

Dr. Menotti Ruvo

E-Mail Website
Guest Editor
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Napoli, Italy
Interests: monoclonal antibodies; antibody functional fragments; antibody drug conjugates
Special Issues, Collections and Topics in MDPI journals
Dr. Annamaria Sandomenico

E-Mail Website
Guest Editor
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Napoli, Italy
Interests: proteins; protein expression; molecular biology; cell culture
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Monoclonal antibodies (mAbs) are amongst the most specialized molecules deputed to the recognition and capture of specific analytes. Hundreds of thousands of mAbs targeting with ever-increasing affinities and specificities with a vast number of different antigens have been generated and are available for the most diverse purposes. Many of them have been validated as irreplaceable agents for diagnosis and therapy or unique reagents for research. Others are being developed using the plethora of emerging technologies that provide new molecular tools based on antibodies and new antibody formats. This journal issue will try to gather the perspective views and the scientific contributions from several groups specialized in this field, specifically focusing on the generation of new monoclonal antibodies or surrogates, like Fabs, Fab2, ScFv, and nanobodies, which may have an impact as novel therapeutic or diagnostic assets in several diseases.

Dr. Menotti Ruvo
Dr. Annamaria Sandomenico
Guest Editors

Manuscript Submission Information

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Keywords

  • Mabs
  • Fabs
  • ScFv
  • nanobodies
  • biomarker detection
  • bispecific antibodies
  • analyte detection
  • sandwich assays

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Related Special Issues

Published Papers (6 papers)

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Research

13 pages, 1817 KiB  
Article
Tumoricidal Activity and Side Effects of Radiolabeled Anti-NCAM [131I]-Iodine-ERIC1 in Neuroblastoma-Bearing Mice
by Thomas Fischer, Felix Dietlein, Detlev Bongartz, Martin Klehr, Beate Zimmermanns, Matthias Schmidt, Angela Mohr, Fabian Mohr, Ferdinand Sudbrock, Philipp Krapf, Alexander Drzezga, Markus Dietlein and Klaus Schomäcker
Int. J. Mol. Sci. 2024, 25(19), 10737; https://doi.org/10.3390/ijms251910737 - 5 Oct 2024
Cited by 1 | Viewed by 1214
Abstract
Preliminary studies on a radioactive antibody against the neural cell adhesion molecule (NCAM) demonstrated a significant accumulation of [131I]I-ERIC1 in neuroblastoma tumor cells in mice. This study aims to validate the therapeutic efficacy and potential adverse effects of these radioactive immunoconjugates [...] Read more.
Preliminary studies on a radioactive antibody against the neural cell adhesion molecule (NCAM) demonstrated a significant accumulation of [131I]I-ERIC1 in neuroblastoma tumor cells in mice. This study aims to validate the therapeutic efficacy and potential adverse effects of these radioactive immunoconjugates (RICs) in neuroblastoma-bearing mice. To determine the highest tolerated dose, healthy SCID mice received 1 to 22 MBq of [131I]I-ERIC1, with the survival time measured. Tumor response was evaluated by administering 0.8 to 22 MBq of [131I]I-ERIC1 to neuroblastoma-bearing mice and assessing tumor size and systemic toxicity through body weight, blood counts, and survival. It was observed that doses up to approximately 3 MBq per animal (150 MBq/kg) were well tolerated, whereas higher doses resulted in systemic toxicity and death. The neuroblastomas exhibited a dose-dependent response, with optimal therapeutic efficacy achieved at 1.8–2.5 MBq per animal (90–125 MBq/kg), significantly extending survival by a factor of five. The antibody ERIC1 is a promising vehicle for the transport of beta emitters into NCAM-positive tumor tissue. An optimal dosage of the [131I]I-ERIC1 antibody can be established with a balance of tumor-static effects and adverse effects, resulting in a marked extension of survival time. Full article
(This article belongs to the Special Issue Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0)
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15 pages, 1494 KiB  
Article
Localization and Tumor Growth Inhibition of I-131-Labeled Monoclonal Antibody ERIC1 in a Subcutaneous Xenograft Model of Small Cell Lung Cancer in SCID Mice
by Thomas Fischer, Christopher Dietrich, Felix Dietlein, Sergio Muñoz Vázquez, Beate Zimmermanns, Philipp Krapf, Ferdinand Sudbrock, Alexander Drzezga, Markus Dietlein and Klaus Schomäcker
Int. J. Mol. Sci. 2024, 25(19), 10638; https://doi.org/10.3390/ijms251910638 - 2 Oct 2024
Viewed by 1150
Abstract
This study evaluates the efficacy of [131I]I-ERIC1 in targeting and inhibiting the growth of SCLC tumors in mice, focusing on tumor accumulation and regression and potential side effects. NCAM-positive NCI-H69 SCLC cells were implanted in CB 17 SCID mice, and [ [...] Read more.
This study evaluates the efficacy of [131I]I-ERIC1 in targeting and inhibiting the growth of SCLC tumors in mice, focusing on tumor accumulation and regression and potential side effects. NCAM-positive NCI-H69 SCLC cells were implanted in CB 17 SCID mice, and [131I]I-ERIC1 biokinetics were measured in organs and tissues at four post-injection time points (24, 72, 96, and 120 h). The experimental series compared tumor growth, survival, and changes in blood counts among three treatment groups (1, 2, or 3 MBq) and a control group, with treatments initiated either two or five days post implantation. [131I]I-ERIC1 was synthesized with >95% radiochemical purity and a specific activity of 15 TBq/mmol. Tumor activity peaked at 31.5 ± 6.6% ID/g after four days, demonstrating significant antitumor efficacy, which resulted in sustained remission and extended survival. Hematological toxicity was observed, with the optimal dose identified as 2 MBq per animal administered two days post implantation. [131I]I-ERIC1 shows promise as a theranostic agent for personalized cancer treatment by effectively targeting SCLC tumors with manageable side effects. However, further studies are required to optimize dosing strategies and minimize toxicity. Full article
(This article belongs to the Special Issue Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0)
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19 pages, 3607 KiB  
Article
Phage Display Revealed the Complex Structure of the Epitope of the Monoclonal Antibody 10H10
by Daniil V. Shanshin, Sophia S. Borisevich, Olga N. Shaprova, Valentina S. Nesmeyanova, Alexander A. Bondar, Yuri B. Porozov, Edward M. Khamitov, Evgeniia A. Kolosova, Arseniya A. Shelemba, Nikita D. Ushkalenko, Elena V. Protopopova, Artemiy A. Sergeev, Valery B. Loktev and Dmitriy N. Shcherbakov
Int. J. Mol. Sci. 2024, 25(19), 10311; https://doi.org/10.3390/ijms251910311 - 25 Sep 2024
Viewed by 1407
Abstract
The annual number of reported human cases of flavivirus infections continues to increase. Measures taken by local healthcare systems and international organizations are not fully successful. In this regard, new approaches to treatment and prevention of flavivirus infections are relevant. One promising approach [...] Read more.
The annual number of reported human cases of flavivirus infections continues to increase. Measures taken by local healthcare systems and international organizations are not fully successful. In this regard, new approaches to treatment and prevention of flavivirus infections are relevant. One promising approach is to use monoclonal antibody preparations. The mouse mAb 10H10 is capable of interacting with viruses belonging to the genus Orthoflavivirus which are pathogenic to humans. ELISA and molecular modeling data can indicate that mAb 10H10 recognizes the fusion loop region of E protein. The KD of interaction between the mAb 10H10 and recombinant analogs of the E protein of the tick-borne encephalitis (TBEV), Zika (ZIKV) and dengue (DENV) viruses range from 1.5 to 4 nM. The aim of this study was to map the epitope of this antibody using phage display technology. After three rounds of biopanning, 60 individual phage clones were chosen. The amino acid sequences of the selected peptides were conveniently divided into five groups. Based on the selected peptides, bacteriophages were obtained carrying peptides on the surfaces of the pIII and pVIII proteins, which were tested for binding to the antibody in ELISA. Thus, the epitope of the mAb 10H10 is the highly conserved region 98-DRGWGNXXGLFGK-110 of the flavivirus E protein. The structures of the complexes of the identified peptides with the antibody paratope are proposed using the molecular docking and dynamics methods. Full article
(This article belongs to the Special Issue Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0)
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16 pages, 3841 KiB  
Article
A Dual Strategy—In Vitro and In Silico—To Evaluate Human Antitetanus mAbs Addressing Their Potential Protective Action on TeNT Endocytosis in Primary Rat Neuronal Cells
by Cauã Pacheco Lima, Gabriela Massaro Barreiros, Adriele Silva Alves Oliveira, Marcelo Medina de Souza, Tania Maria Manieri and Ana Maria Moro
Int. J. Mol. Sci. 2024, 25(11), 5788; https://doi.org/10.3390/ijms25115788 - 26 May 2024
Viewed by 1312
Abstract
Tetanus disease, caused by C. tetani, starts with wounds or mucous layer contact. Prevented by vaccination, the lack of booster shots throughout life requires prophylactic treatment in case of accidents. The incidence of tetanus is high in underdeveloped countries, requiring the administration [...] Read more.
Tetanus disease, caused by C. tetani, starts with wounds or mucous layer contact. Prevented by vaccination, the lack of booster shots throughout life requires prophylactic treatment in case of accidents. The incidence of tetanus is high in underdeveloped countries, requiring the administration of antitetanus antibodies, usually derived from immunized horses or humans. Heterologous sera represent risks such as serum sickness. Human sera can carry unknown viruses. In the search for human monoclonal antibodies (mAbs) against TeNT (Tetanus Neurotoxin), we previously identified a panel of mAbs derived from B-cell sorting, selecting two nonrelated ones that binded to the C-terminal domain of TeNT (HCR/T), inhibiting its interaction with the cellular receptor ganglioside GT1b. Here, we present the results of cellular assays and molecular docking tools. TeNT internalization in neurons is prevented by more than 50% in neonatal rat spinal cord cells, determined by quantitative analysis of immunofluorescence punctate staining of Alexa Fluor 647 conjugated to TeNT. We also confirmed the mediator role of the Synaptic Vesicle Glycoprotein II (SV2) in TeNT endocytosis. The molecular docking assays to predict potential TeNT epitopes showed the binding of both antibodies to the HCR/T domain. A higher incidence was found between N1153 and W1297 when evaluating candidate residues for conformational epitope. Full article
(This article belongs to the Special Issue Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0)
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14 pages, 1948 KiB  
Communication
Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer
by Emma Franco-Mateos, Virginia Souza-Egipsy, Laura García-Estévez, José Pérez-García, María Gion, Laia Garrigós, Patricia Cortez, Cristina Saavedra, Patricia Gómez, Carolina Ortiz, Víctor L. Cruz, Javier Ramos, Javier Cortés and Juan F. Vega
Int. J. Mol. Sci. 2024, 25(7), 3940; https://doi.org/10.3390/ijms25073940 - 1 Apr 2024
Viewed by 1727
Abstract
The binding activity of various trastuzumab biosimilars versus the branded trastuzumab towards the glycosylated extracellular domain of the human epidermal growth factor receptor 2 (HER2) target in the presence of pertuzumab was investigated. We employed size exclusion chromatography with tetra-detection methodology to simultaneously [...] Read more.
The binding activity of various trastuzumab biosimilars versus the branded trastuzumab towards the glycosylated extracellular domain of the human epidermal growth factor receptor 2 (HER2) target in the presence of pertuzumab was investigated. We employed size exclusion chromatography with tetra-detection methodology to simultaneously determine absolute molecular weight, concentration, molecular size, and intrinsic viscosity. All trastuzumab molecules in solution exhibit analogous behavior in their binary action towards HER2 regardless of the order of addition of trastuzumab/pertuzumab. This analogous behavior of all trastuzumab molecules, including biosimilars, highlights the robustness and consistency of their binding activity towards HER2. Furthermore, the addition of HER2 to a mixture of trastuzumab and pertuzumab leads to increased formation of high-order HER2 complexes, up to concentrations of one order of magnitude higher than in the case of sequential addition. The observed increase suggests a potential synergistic effect between these antibodies, which could enhance their therapeutic efficacy in HER2-positive cancers. These findings underscore the importance of understanding the complex interplay between therapeutic antibodies and their target antigens, providing valuable insights for the development of more effective treatment strategies. Full article
(This article belongs to the Special Issue Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0)
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Graphical abstract

22 pages, 3486 KiB  
Article
Evaluation of Phage Display Biopanning Strategies for the Selection of Anti-Cell Surface Receptor Antibodies
by Nadya Panagides, Lucia F. Zacchi, Mitchell J. De Souza, Rodrigo A. V. Morales, Alexander Karnowski, Mark T. Liddament, Catherine M. Owczarek, Stephen M. Mahler, Con Panousis, Martina L. Jones and Christian Fercher
Int. J. Mol. Sci. 2022, 23(15), 8470; https://doi.org/10.3390/ijms23158470 - 30 Jul 2022
Cited by 13 | Viewed by 6662
Abstract
Monoclonal antibodies (mAbs) are one of the most successful and versatile protein-based pharmaceutical products used to treat multiple pathological conditions. The remarkable specificity of mAbs and their affinity for biological targets has led to the implementation of mAbs in the therapeutic regime of [...] Read more.
Monoclonal antibodies (mAbs) are one of the most successful and versatile protein-based pharmaceutical products used to treat multiple pathological conditions. The remarkable specificity of mAbs and their affinity for biological targets has led to the implementation of mAbs in the therapeutic regime of oncogenic, chronic inflammatory, cardiovascular, and infectious diseases. Thus, the discovery of novel mAbs with defined functional activities is of crucial importance to expand our ability to address current and future clinical challenges. In vitro, antigen-driven affinity selection employing phage display biopanning is a commonly used technique to isolate mAbs. The success of biopanning is dependent on the quality and the presentation format of the antigen, which is critical when isolating mAbs against membrane protein targets. Here, we provide a comprehensive investigation of two established panning strategies, surface-tethering of a recombinant extracellular domain and cell-based biopanning, to examine the impact of antigen presentation on selection outcomes with regards to the isolation of positive mAbs with functional potential against a proof-of-concept type I cell surface receptor. Based on the higher sequence diversity of the resulting antibody repertoire, presentation of a type I membrane protein in soluble form was more advantageous over presentation in cell-based format. Our results will contribute to inform and guide future antibody discovery campaigns against cell surface proteins. Full article
(This article belongs to the Special Issue Monoclonal Antibodies and Their Functional Fragments in Research, Diagnosis and Therapy 3.0)
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