Abstract
Bispecific antibodies with binding specificities for two different antigens have prompted a lot of interest into their development and application. Currently, more than ten bispecific antibodies have been clinically validated for the treatment of various diseases, including cancers and inflammatory diseases. Intensive studies in antibody engineering drive the generation of different bispecific antibody formats that differ in size and shape. However, the most prominent formats, such as IgG-single-chain (sc) Fv or dual-variable domain (DVD) IgG, deviating from the natural IgG structure, may lead to manufacturing difficulties or increase the potential risk of immunogenicity. Thus, the recent efforts focus on the development of bispecific antibodies by Fc heterodimerization that maintain the native structure of the antibody IgG molecule. This review summarizes the various techniques and methods to generate bispecific antibody molecules with Fc heterodimerization, and discusses perspectives of their application.
Keywords: Bispecific antibody, Fc heterodimerization, quadroma, Knobs-into-holes, strand-exchange engineered domain.
Current Pharmaceutical Biotechnology
Title:Generation of Bispecific Antibodies by Fc Heterodimerization and their Application
Volume: 17 Issue: 15
Author(s): Zhizhen Chen, Liping Wang, Tianshu Xu, Qifei Wang, Lishan Kang and Qi Zhao
Affiliation:
Keywords: Bispecific antibody, Fc heterodimerization, quadroma, Knobs-into-holes, strand-exchange engineered domain.
Abstract: Bispecific antibodies with binding specificities for two different antigens have prompted a lot of interest into their development and application. Currently, more than ten bispecific antibodies have been clinically validated for the treatment of various diseases, including cancers and inflammatory diseases. Intensive studies in antibody engineering drive the generation of different bispecific antibody formats that differ in size and shape. However, the most prominent formats, such as IgG-single-chain (sc) Fv or dual-variable domain (DVD) IgG, deviating from the natural IgG structure, may lead to manufacturing difficulties or increase the potential risk of immunogenicity. Thus, the recent efforts focus on the development of bispecific antibodies by Fc heterodimerization that maintain the native structure of the antibody IgG molecule. This review summarizes the various techniques and methods to generate bispecific antibody molecules with Fc heterodimerization, and discusses perspectives of their application.
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Cite this article as:
Chen Zhizhen, Wang Liping, Xu Tianshu, Wang Qifei, Kang Lishan and Zhao Qi, Generation of Bispecific Antibodies by Fc Heterodimerization and their Application, Current Pharmaceutical Biotechnology 2016; 17 (15) . https://dx.doi.org/10.2174/1389201017666161018150553
DOI https://dx.doi.org/10.2174/1389201017666161018150553 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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