ScFv Improvement Approaches

Bemani, Peyman; Mohammadi, Mozafar; Hakakian, Ali

doi:10.2174/0929866525666171129225436

Cited by 11 publications

(7 citation statements)

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“…Moreover, scFvs do not mediate deleterious inflammatory responses such as meningoencephalitis, cerebral microhemorrhages, or even death, due to the lack of the inflammatory Fc domain of mAbs. The above advantages of scFvs are favorable for their clinical application [ 61 , 62 , 63 ].…”

Section: Structure−toxicity Relationships Of Aβ42 Aggregates Revealed...mentioning

confidence: 99%

Conformational Essentials Responsible for Neurotoxicity of Aβ42 Aggregates Revealed by Antibodies against Oligomeric Aβ42

Song

Zhang²,

Zhang³

2022

Molecules

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Soluble aggregation of amyloid β-peptide 1-42 (Aβ42) and deposition of Aβ42 aggregates are the initial pathological hallmarks of Alzheimer’s disease (AD). The bipolar nature of Aβ42 molecule results in its ability to assemble into distinct oligomers and higher aggregates, which may drive some of the phenotypic heterogeneity observed in AD. Agents targeting Aβ42 or its aggregates, such as anti-Aβ42 antibodies, can inhibit the aggregation of Aβ42 and toxicity of Aβ42 aggregates to neural cells to a certain extent. However, the epitope specificity of an antibody affects its binding affinity for different Aβ42 species. Different antibodies target different sites on Aβ42 and thus elicit different neuroprotective or cytoprotective effects. In the present review, we summarize significant information reflected by anti-Aβ42 antibodies in different immunotherapies and propose an overview of the structure (conformation)−toxicity relationship of Aβ42 aggregates. This review aimed to provide a reference for the directional design of antibodies against the most pathogenic conformation of Aβ42 aggregates.

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Section: Structure−toxicity Relationships Of Aβ42 Aggregates Revealed...mentioning

confidence: 99%

Conformational Essentials Responsible for Neurotoxicity of Aβ42 Aggregates Revealed by Antibodies against Oligomeric Aβ42

Song

Zhang²,

Zhang³

2022

Molecules

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“…The scFv have a small molecular weight, strong penetration, and high affinity. They have been widely used in tumor therapy, infectious disease prevention and treatment, food safety residue detection, and other fields [ 43 ].…”

Section: Preparation Of Novel Genetically Engineered Antibodies Fomentioning

confidence: 99%

Advances in Antibody Preparation Techniques for Immunoassays of Total Aflatoxin in Food

et al. 2020

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Aflatoxin (AF) contamination is a major concern in the food and feed industry because of its prevalence and toxicity. Improved aflatoxin detection methods are still needed. Immunoassays are an important method for total aflatoxin (TAF) analysis in food due to its technical advantages such as high specificity, sensitivity, and simplicity, but require high-quality antibodies. Here, we first review the three ways to prepare high-quality antibodies for TAF immunoassay, second, compare the advantages and disadvantages of antigen synthesis methods for B-group and G-group aflatoxins, and third, describe the status of novel genetic engineering antibodies. This review can provide new methods and ideas for the development of TAF immunoassays.

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“…IgY-scFv (around 30 kDa) is only one-six the size of full-length IgY (180 kDa; Figure 1) but retains intact antigen-binding capacity. ScFv, including IgY-scFv, has the advantages of easy penetration into the target tissue, low side effects, high specificity, and high purity; therefore, it has a great biomedical potential of being widely used in clinic [3,8]. Particularly, avian IgY-scFv can fuse to alkaline phosphatase for the detection of aspergillus pathogens [9] and fuse to NanoLuc luciferase for the detection of ferritin [10].…”

Section: Introductionmentioning

confidence: 99%

Chimerism of avian IgY‐scFv and truncated IgG‐Fc: A novel strategy in cross‐species antibody generation and enhancement

Ge,

Dias,

Zhang

2024

Immunology

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Chicken single‐chain fragment variable (IgY‐scFv) is a functional fragment and an emerging development in genetically engineered antibodies with a wide range of biomedical applications. However, scFvs have considerably shorter serum half‐life due to the absence of antibody Fc region compared with the full‐length antibody, and usually requires continuous intravenous administration for efficacy. A promising approach to overcome this limitation is to fuse scFv with immunoglobulin G (IgG) Fc region, for better recognition and mediation by the neonatal Fc receptor (FcRn) in the host. In this study, engineered mammalian ΔFc domains (CH2, CH3, and intact Fc region) were fused with anti‐canine parvovirus‐like particles avian IgY‐scFv to produce chimeric antibodies and expressed in the HEK293 cell expression system. The obtained scFv‐CH2, scFv‐CH3, and scFv‐Fc can bind with antigen specifically and dose‐dependently. Surface plasmon resonance investigation confirmed that scFv‐CH2, scFv‐CH3, and scFv‐Fc had different degrees of binding to FcRn, with scFv‐Fc showing the highest affinity. scFv‐Fc had a significantly longer half‐life in mice compared with the unfused scFv. The identified ΔFcs are promising for the development of engineered Fc‐based therapeutic antibodies and proteins with longer half‐lives. The avian IgY‐scFv‐mammalian IgG Fc region opens up new avenues for antibody engineering, and it is a novel strategy to enhance the rapid development and screening of functional antibodies in veterinary and human medicine.

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ScFv Improvement Approaches

Cited by 11 publications

References 0 publications

Conformational Essentials Responsible for Neurotoxicity of Aβ42 Aggregates Revealed by Antibodies against Oligomeric Aβ42

Conformational Essentials Responsible for Neurotoxicity of Aβ42 Aggregates Revealed by Antibodies against Oligomeric Aβ42

Advances in Antibody Preparation Techniques for Immunoassays of Total Aflatoxin in Food

Chimerism of avian IgY‐scFv and truncated IgG‐Fc: A novel strategy in cross‐species antibody generation and enhancement

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