Partial Characterization of the Human Serum Transferrin Epitope Reactive with the Monoclonal Antibody TRC-2

Öztürk, Savaş; Çirakoğlu, Beyazıt; Bermek, Engin

doi:10.1089/153685903322286584

Cited by 3 publications

(1 citation statement)

References 29 publications

(32 reference statements)

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“…Since this cycle is vital for the cell, TFR is used as a proliferation marker for the cells where highly proliferating cells express more TFR, and serves as a target for therapy. Blocking of TFR with monoclonal antibodies poses a cytotoxic effect, and this is proposed as a mechanism to inhibit cell growth [ 17 , 18 ]. Another strategy utilizing the TFR is using it for the targeted delivery of drugs in malignancies, since highly-proliferating cells express more TFR than their healthy counterparts [ 19 , 20 ].…”

Section: Introductionmentioning

confidence: 99%

Biological Activity of the Carrier as a Factor in Immunogen Design for Haptens

et al. 2018

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Immunoanalytical methods are frequently employed in the detection of hazardous small molecular weight compounds. However, antibody development for these molecules is a challenge, because they are haptens and cannot induce a humoral immune response in experimental animals. Immunogenic forms of haptens are usually prepared by conjugating them to a protein carrier which serves as an immune stimulator. However, the carrier is usually considered merely as a bulk mass, and its biological activity is ignored. Here, we induced an endocytic receptor, transferrin receptor, by selecting its ligand as a carrier protein to enhance antibody production. We conjugated aflatoxin, a potent carcinogenic food contaminant, to transferrin and evaluated its potential to stimulate antibody production with respect to ovalbumin conjugates. Transferrin conjugates induced aflatoxin-specific immune responses in the second immunization, while ovalbumin conjugates reached similar antibody titers after 5 injections. Monoclonal antibodies were successfully developed with mice immunized with either of the conjugates.

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Section: Introductionmentioning

confidence: 99%

Biological Activity of the Carrier as a Factor in Immunogen Design for Haptens

et al. 2018

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Epitope mapping of anti‐human transferrin monoclonal antibodies: potential uses for transferrin–transferrin receptor interaction studies

Perera

García

Guirola

et al. 2008

J of Molecular Recognition

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Human transferrin (hTf) is an 80 kDa glycoprotein involved in iron transport from the absorption sites to the sites of storage and utilization. Additionally, transferrin also plays a relevant role as a bacteriostatic agent preventing uncontrolled bacterial growth in the host. In this work we describe a well-characterized Mabs panel in terms of precise epitope localization and estimate affinity for the two major hTf isoforms. We found at least four antigenic regions in the hTf molecule, narrowed down the interacting antigen residues within three of such regions, and located them on a molecular model of hTf. Two of the antigenic regions partially overlap with previously described transferrin-binding sites for both human receptor (antigenic region I: containing amino acid residues from Asp-69 to Asn-76 at the N-lobe) and bacterial receptors from two pathogenic species (antigenic region III: amino acid residues from Leu-665 to Ser-672 at the C-lobe). Hence, such monoclonal antibodies (Mabs) could be used as an additional tool for conformational studies and/or the characterization of the interaction between hTf and both types of receptor molecules.

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