Abstract
The analysis of secreted antibody from large and diverse populations of B cells in parallel at the clonal level can reveal desirable antibodies for diagnostic or therapeutic applications. By immobilizing B cells in microdroplets with particulate reporters, decoding and isolating them in a microscopy environment, we have recovered panels of antibodies with rare attributes to therapeutically relevant targets. The ability to screen up to 100 million cells in a single experiment can be fully leveraged by accessing primary B-cell populations from evolutionarily divergent species such as chickens.
Highlights
The ‘age of monoclonal antibodies’ was ushered in with the advent of hybridoma technology in the 1970s
Antibody is secreted from the B cell and diffuses locally within the gel encapsulated microenvironment (GEM) where it binds to its target displayed on the reporter
GEMs are made in batches accommodating as few as several thousand or as many as 100 million total cells, but experiments are generally performed with 10–50 million cells when using splenocytes
Summary
The ‘age of monoclonal antibodies’ was ushered in with the advent of hybridoma technology in the 1970s. The compounded annual growth rate of the mAb market is 8% [1] Throughout this period of rapid growth, antibody discovery has relied heavily on classical hybridoma technology in spite of three significant limitations. Targets that are highly conserved between mammals are often poorly immunogenic in rodents It is generally difficult using hybridoma technology to raise antibodies that are rodent cross-reactive, a necessary property for testing in many animal models of disease. Binding of the ligand TRAIL can induce apoptosis in a variety of cell types and agonistic antibodies to these receptors are pro-apoptotic [43,44,45]. A highly specific and antagonistic P2X3 mAb has potential therapeutic value
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