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  • Title: Optimization of anti-tumor necrosis factor-alpha single chain Fv displayed on phages for creation of functional antibodies.
    Author: Mukai Y, Okamoto T, Kawamura M, Shibata H, Sugita T, Imai S, Abe Y, Nagano K, Nomura T, Kamada H, Tsutsumi Y, Mayumi T, Nakagawa S, Tsunoda S.
    Journal: Pharmazie; 2006 Oct; 61(10):889-90. PubMed ID: 17069432.
    Abstract:
    In this study, we converted the immunoglobulin-type anti-human tumor necrosis factor-alpha (TNF-alpha) monoclonal antibody (Mab) to a scFv-type antibody in order to assess its basic properties. The immunoglobulin VH and VL genes were isolated from the hybridoma that produced an anti-TNF-alpha neutralizing Mab, and they were then linked together to create scFvs of the VL-VH or VH-VL-form. The binding affinity to TNF-a was retained in both scFvs. Interestingly, the VL-VH-type scFv effectively inhibited the TNF-alpha-mediated cytotoxicity, while this neutralization activity was dramatically decreased in the VH-VL-type scFv. These results suggest that the VL-VH-type scFv is a suitable template to create improved versions of the anti-TNF-alpha antibody using a phage display system, and they also show that the structural format must be taken into account in manufacturing scFvs.
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