Abstract
Phage display technology allows for rapid selection of antibodies from the large repertoire of human antibody fragments displayed on phages. However, antibody fragments should be converted to IgG for biological characterizations and affinity of antibodies obtained from phage display library is frequently not sufficient for efficient use in clinical settings. Here, we describe a new approach that combines phage and mammalian cell display, enabling simultaneous affinity screening of full-length IgG antibodies. Using this strategy, we successfully obtained a novel germline-like anti-TIM-3 monoclonal antibody named m101, which was revealed to be a potent anti-TIM-3 therapeutic monoclonal antibody via in vitro and in vivo experiments, indicating its effectiveness and power. Thus, this platform can help develop new monoclonal antibody therapeutics with high affinity and low immunogenicity.
Highlights
Over the past decades, monoclonal antibodies have become the most important class of therapeutic biologicals on drug market [1, 2]
Antibody affinity plays an important role in biological efficacy [4], and higher antibody affinity typically allows for lower dosage
Measured with a microplate reader (Biotek). To validate this new technology, we set out to generate antibodies with high binding affinity for T-cell immunoglobulin Screening of anti-TIM-3-Fc monoclonal antibodies (mAbs) from phage display library and mucin domain-containing protein 3 (TIM-3), which is a First, we used a large phage display naive human Fab library promising candidate for cancer immunotherapy [25, 26] that was constructed by using mixed PBMC cDNAs from 40 healthy first reported in 2002 [27]
Summary
Monoclonal antibodies (mAbs) have become the most important class of therapeutic biologicals on drug market [1, 2]. A possibility to address one of these issues is to use mammalian cell display, which possesses intrinsic abilities to fold and glycosylate full-length IgG [21] It enables the display of whole IgG and selection of positive clones with high affinity and other specific biological functions by fluorescence-activated cell sorting (FACS) [7, 8, 22,23,24], allowing for highly controlled and real-time selection of IgG. To validate this new technology, we set out to generate antibodies with high binding affinity for T-cell immunoglobulin Screening of anti-TIM-3-Fc mAb from phage display library and mucin domain-containing protein 3 (TIM-3), which is a First, we used a large phage display naive human Fab library promising candidate for cancer immunotherapy [25, 26] that was constructed by using mixed PBMC cDNAs from 40 healthy first reported in 2002 [27].
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