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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

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Published Papers (2 papers)

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Research

14 pages, 1948 KiB

Open AccessCommunication

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://0-doi-org.brum.beds.ac.uk/10.3390/ijms25073940 - 01 Apr 2024

Viewed by 578

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 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

Open AccessArticle

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://0-doi-org.brum.beds.ac.uk/10.3390/ijms23158470 - 30 Jul 2022

Cited by 6 | Viewed by 4104

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 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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