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September 1, 2020Russian Journal of Bioorganic Chemistry

Humanized antibody hB16 possesses the same properties as murine mAb B16 in binding and neutralizing human interferon-beta.

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Why the study?

Humanization of antibodies to develop novel therapeutic agents with low immunogenicity remains an important scientific challenge.

Population

Transient CHO cells expressing humanized hB16 and chimeric chB16 antibodies

Comparison

Humanized antibody hB16 vs murine mAb B16 and chimeric antibody chB16

Design

Preclinical laboratory study

Key result

Humanized antibody hB16 possesses the same properties as murine mAb B16 in binding and neutralizing human interferon-beta.

Authors

ВРВ. С. РыбченкоАПА. А. ПанинаVNValery Novoseletsky

Discussion

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Overview

Offers candidate for IFN-beta/ErbB2 immune complex; leaves open clinical translation pending human trials.

Structured PICO

P
Population
Transient CHO cells expressing humanized antibody hB16 and chimeric antibody chB16
I
Intervention
Humanization of murine antibody B16 using CDR-grafting method
C
Comparator
Murine mAb B16 and chimeric antibody chB16
O
Outcome
Antibody properties (binding and neutralizing human interferon-beta)surrogate

The successful humanization of murine antibody B16 provides a potential component for a therapeutic immune complex targeting interferon-beta and the ErbB2 receptor.

Cite This Study

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.

synapsesocial.com/papers/6a7dcbf8d0946debe9150422https://doi.org/10.1134/s1068162020050209
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