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Review
. 2020 Jan 1;10(2):938-955.
doi: 10.7150/thno.37443. eCollection 2020.

Monoclonal antibody-based molecular imaging strategies and theranostic opportunities

Affiliations
Review

Monoclonal antibody-based molecular imaging strategies and theranostic opportunities

Niels Dammes et al. Theranostics. .

Abstract

Molecular imaging modalities hold great potential as less invasive techniques for diagnosis and management of various diseases. Molecular imaging combines imaging agents with targeting moieties to specifically image diseased sites in the body. Monoclonal antibodies (mAbs) have become increasingly popular as novel therapeutics against a variety of diseases due to their specificity, affinity and serum stability. Because of the same properties, mAbs are also exploited in molecular imaging to target imaging agents such as radionuclides to the cell of interest in vivo. Many studies investigated the use of mAb-targeted imaging for a variety of purposes, for instance to monitor disease progression and to predict response to a specific therapeutic agent. Herein, we highlighted the application of mAb-targeted imaging in three different types of pathologies: autoimmune diseases, oncology and cardiovascular diseases. We also described the potential of molecular imaging strategies in theranostics and precision medicine. Due to the nearly infinite repertoire of mAbs, molecular imaging can change the future of modern medicine by revolutionizing diagnostics and response prediction in practically any disease.

Keywords: autoimmune diseases; molecular imaging; monoclonal antibodies; oncology and cardiovascular diseases..

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Conflict of interest statement

Competing Interests: The authors have declared that no competing interest exists.

Figures

Figure 1
Figure 1
Antibody engineering enabled the production of a wide variety of IgG derivatives. F(ab')2, Fab and Fab' products are produced by enzymatic digestion of an IgG molecule while the other derivatives are generated using genetic engineering of IgGs. Nanobodies are specifically engineered from a camelid antibody variant that contains only heavy chains. Figure modified from .
Figure 2
Figure 2
Imaging data of 64Cu-labeled anti-α4β7 integrin (DATK32) and anti-β7 integrin (FIB504.64), the latter with either Fab or F(ab')2 antibody fragments. Coronal images are shown in the upper panel and transaxial images in the lower panel. The FIB504.64 clearly shows a better, more specific uptake than the DATK32 antibody. The presence of colitis is evident in the images when compared to healthy control mice, indicating the specificity. This figure is reprinted with permission from Inflammatory Bowel Diseases (Dearling et al., 2016) .
Figure 3
Figure 3
Bio-distribution of 111In-R1507 (against IGF-1R) in three different mouse models of bone sarcoma. A are mice with IGF-1R positive tumors that did respond to anti-IGF-1R therapy. B are mice with IGF-1R positive tumors that did respond only modestly to anti-IGF-1R therapy. C shows the three different models side-by-side (all imaged at day 3). OS-33 is IGF-1R negative, EW-8 is IGF-1R positive but does not respond to anti-IGF-1R therapy and OS-1 is IGF-1R positive and shows a response to anti-IGF-1R therapy. The mouse in the right panel has two tumors, OS-1 (indicated with the white arrow) and OS-33 (indicated with the red arrow). As can be derived from the figure, only OS-1, a IGF-1R positive tumor that responds to the treatment shows significant uptake of 111In-R1507. This adapted figure is reprinted with permission from Clinical Cancer Research (Fleuren et al., 2011) .

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