Researchers Develop Novel Antibody to Knockdown of Protein in Vertebrates
Researchers from Technische Universität Dresden developed a synthetic antibody that improves functional analysis of proteins.
A research led by Dr. Jörg Mansfeld of the Biotechnology Center of the TU Dresden in collaboration with Dr. Caren Norden of the Max Planck Institute for Molecular Cell Biology and Genetics developed a synthetic antibody to knockdown of protein in vertebrates. The synthetic antibody was combined with auxin-inducible protein knockdown to observe fluorescent proteins in living cells along with ability to rapidly remove the proteins in a temporally controlled manner. The research was published in Nature Communications on August 17, 2018.
Proteins perform a wide variety of functions in cells and tissues and are the most important basic component of all cells. The proteins are linked to a green fluorescent protein (GFP) via targeted genetic manipulation in order to clarify the physiological roles of proteins. The GFP are visible under the microscope and the observation allows initial conclusions about the function of the protein. However, an isolated protein is required to determine the exact function and the consequences of a protein in cells, tissues or model organisms. Such isolation is achieved by knockout of the protein on the genetic level. However, the non-viability of the cell or the model organism does not allow to examine the functions of essential proteins. The approach of isolating proteins from cells only at a specific time is required to determine the functionality of proteins. The targeted temporary degradation of proteins is evident in plants that is mediated by the hormone auxin. The underlying mechanism can also be applied to animal and human cells after genetic manipulation.
The researchers developed a synthetic antibody to observe GFP-linked proteins in living cells. Moreover, the antibody rapidly degrades the proteins in a targeted manner for functional analysis. The auxin recognition sequence (AID) linked to a GFP recognizing antibody was responsible for the degradation. The AID is structurally-related to camelid antibodies and allow complete degradation of GFP-linked proteins in human cell culture when auxin are added. The functional analysis is made much easier by the possibility to follow the degradation of the protein ‘live’ under the microscope.
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