A recombinant scFv antibody against human spleen ferritin was expressed as a barstar-fused protein in Escherichia coli and in Nicotiana tabacum plants and suspension cell cultures. As demonstrated by immunoblotting with antibarstar antibodies, direction of the recombinant protein to the endomembrane system of plant cells ensured its stability and solubility. Production of the recombinant protein did not differ between parental transgenic plants and their first-generation progeny. Fusion with barstar allowed not only immunochemical detection of the recombinant scFv antibody, but also their purification from the plant material by affinity chromatography with barnase-His6 immobilized on a metal-affinity carrier.
Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Non-competitive immunoassay for zearalenone based on phage display developed recombinant antibody and anti-immunocomplex peptide.
Food Chem
January 2025
College of Life Science, Shandong Agricultural University, Tai'an 271018, China. Electronic address:
Zearalenone (ZEN) is a widely distributed mycotoxin with potent estrogenic activity. Detecting ZEN is crucial for assessing its potential health risks. This study developed a highly sensitive non-competitive magnetic phage anti-immunocomplex immunoassay (Nc-MPHAIA) for ZEN detection, utilizing the anti-ZEN single-chain variable fragment (ScFv) and anti-immunocomplex peptide (AIcP), both of which were screened using phage display technology.
View Article and Find Full Text PDFGrB-Fc-KS49, an anti-EMP2 granzyme B fusion protein therapeutic alters immune cell infiltration and suppresses breast cancer growth.
J Immunother Cancer
December 2024
Department of Pathology and Laboratory Medicine, University of California Los Angeles, Los Angeles, California, USA
Background: Granzyme B (GrB) is a key effector molecule, delivered by cytotoxic T lymphocytes and natural killer cells during immune surveillance to induce cell death. Fusion proteins and immunoconjugates represent an innovative therapeutic approach to specifically deliver a deadly payload to target cells. Epithelial membrane protein-2 (EMP2) is highly expressed in invasive breast cancer (BC), including triple-negative BC (TNBC), and represents an attractive therapeutic target.
View Article and Find Full Text PDFDevelopment of a recombinant human IgG1 monoclonal antibody against the TRBV5-1 segment of the T cell receptor for the treatment of mature T cell neoplasms.
Front Immunol
January 2025
Dipartimento di Biomedicina e Prevenzione, Università di Roma Tor Vergata, Rome, Italy.
Background: Mature T-cell neoplasms arise from the neoplastic transformation of a single T lymphocyte, and all cells in a neoplastic clone share the same V segment in the beta chain of the T-cell receptor (TCR). These segments may represent an innovative target for the development of targeted therapies.
Methods: A specific V segment of the TCR beta chain (TRBV5-1) was analyzed using bioinformatic tools, identifying three potential antigenic peptides.
A High-Affinity Monoclonal Antibody Against the Pancreatic Ductal Adenocarcinoma Target, Anterior Gradient-2 (AGR2/PDIA17).
Antibodies (Basel)
December 2024
Department of Pharmacology and Immunology, Medical University of South Carolina, Charleston, SC 29425, USA.
Background/objectives: Anterior Gradient-2 (AGR2/PDIA17) is a member of the protein disulfide isomerase (PDI) family of oxidoreductases. AGR2 is up-regulated in several solid tumors, including pancreatic ductal adenocarcinoma (PDAC). Given the dire need for new therapeutic options for PDAC patients, we investigated the expression and function of AGR2 in PDAC and developed a novel series of affinity-matured AGR2-specific single-chain variable fragments (scFvs) and monoclonal antibodies.
View Article and Find Full Text PDFProduction and functional analysis of a phage displayed scFv recombinant antibody targeting EGFR/HER2 dimerization domain.
Protein Expr Purif
December 2024
Department of Immunology, School of Medicine, Mazandaran University of Medical Sciences, Sari, Iran; Molecular and Cell Biology Research Center (MCBRC), School of Medicine, Mazandaran University of Medical Sciences, Sari, Iran. Electronic address:
Background: Tumor cells exploit epidermal growth factor receptor (EGFR) family to develop resistance against therapeutic antibodies, such as Herceptin. Upon ligand binding, dimerization between EGFR and HER2 is one of the most important causes of treatment failure in breast cancer and other cancers expressing EGFR and HER2. The aim of this study was to develop and evaluate the function of a human recombinant single-chain variable fragment (scFv) antibody against the dimerization domain of EGFR to inhibit its interaction with other members of the epidermal growth factor receptor family, especially HER2.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!