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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: 20 December 2024 | Viewed by 7222

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

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

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

Related Special Issues

Published Papers (3 papers)

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Research

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 592
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 982
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 6 | Viewed by 4703
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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