Key result
Humanized antibody hB16 possesses the same properties as murine mAb B16 in binding and neutralizing human interferon-beta.
Why the study?
Humanization of antibodies to develop novel therapeutic agents with low immunogenicity remains an important scientific challenge.
The successful humanization of murine antibody B16 provides a potential component for a therapeutic immune complex targeting interferon-beta and the ErbB2 receptor.
Answers are grounded in this paper and cite their sources.
Offers candidate for IFN-beta/ErbB2 immune complex; leaves open clinical translation pending human trials.
Humanization of antibodies for the development of novel therapeutic agents with low immunogenicity remains a topical problem in modern science. In the present work we describe the humanization of murine antibody B16 which binds and neutralizes human interferon-beta using the CDR-grafting method. Based on amino acid sequences of humanized and murine antibodies we constructed models of variable domains, analyzed, and compared them. The genes of humanized antibody hB16 and chimeric antibody chB16 were expressed in transient CHO cells. Antibodies were recovered from conditioned media, purified using affinity chromatography, and their properties were studied by biochemical and immunochemical methods. It was proven that humanized antibody hB16 possesses the same properties as murine mAb B16. This humanized antibody hB16 will be used in further work in order to obtain therapeutic immune complex composed of human interferon-beta and bispecific antibody which binds interferon-beta and the ErbB2 receptor.
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Рыбченко et al. (2020) studied this question. Humanized antibody hB16 vs. Murine mAb B16 was evaluated on Antibody properties (binding and neutralizing human interferon-beta). Humanized antibody hB16 possesses the same properties as murine mAb B16 in binding and neutralizing human interferon-beta.
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