Publication details

Recombinant antibodies for in vivo applications

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Year of publication 2014
Type Appeared in Conference without Proceedings
MU Faculty or unit

Faculty of Science

Description Interactions between biomolecules constitute the core of biological functions. In protein–protein interactions, specificity plays a key role and many proteins have evolved into extraordinarily precise molecular machines. The multistep phosphorylation pathway of the cytokinin signaling in plants is involving promiscuous protein-protein interactions, allowing the plasticity of the plant cell response to environmental and developmental stimuli. We have developed a recombinant antibody which is able to precisely bind to a specific protein from the phosporylation pathway in vivo. Hereinafter this protein is not phosphorylated after the signal perception and therefore the message is not delivered to the nucleus to commit the reaction of the plant. To accomplish a successful selection of the recombinant antibody, we have developed a in vivo selection method. This method allows targeting of recombinant antibodies for a precise activity. Along the way of developing our method, we came to several conclusions. In vivo selection process is important, because the stability of the recombinant antibody in the reducing environment of the plant cell is difficult to predict. Additionally, the uncertainty of the correct form of the antigen produced by heterologous expression is introducing another variable, which might result in the unsuccessful selection of a correct recombinant antibody.
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