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The TFAMoplex—Conversion of the Mitochondrial Transcription Factor A into a DNA Transfection Agent
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The TFAMoplex—Conversion of the Mitochondrial Transcription Factor A into a DNA Transfection Agent
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Journal Article
The TFAMoplex—Conversion of the Mitochondrial Transcription Factor A into a DNA Transfection Agent
2022
Overview
Non‐viral gene delivery agents, such as cationic lipids, polymers, and peptides, mainly rely on charge‐based and hydrophobic interactions for the condensation of DNA molecules into nanoparticles. The human protein mitochondrial transcription factor A (TFAM), on the other hand, has evolved to form nanoparticles with DNA through highly specific protein‐protein and protein‐DNA interactions. Here, the properties of TFAM are repurposed to create a DNA transfection agent by means of protein engineering. TFAM is covalently fused to Listeria monocytogenes phospholipase C (PLC), an enzyme that lyses lipid membranes under acidic conditions, to enable endosomal escape and human vaccinia‐related kinase 1 (VRK1), which is intended to protect the DNA from cytoplasmic defense mechanisms. The TFAM/DNA complexes (TFAMoplexes) are stabilized by cysteine point mutations introduced rationally in the TFAM homodimerization site, resulting in particles, which show maximal activity when formed in 80% serum and transfect HeLa cells in vitro after 30 min of incubation under challenging cell culture conditions. The herein developed TFAM‐based DNA scaffolds combine interesting characteristics in an easy‐to‐use system and can be readily expanded with further protein factors. This makes the TFAMoplex a promising tool in protein‐based gene delivery. The protein human mitochondrial transcription factor A (TFAM) binds and condenses DNA into nanoparticles. TFAM is used as a scaffold to form so called TFAMoplexes for DNA transfection of mammalian cells. The TFAM protein is coupled to a membranolytic phospholipase and a kinase to overcome important hurdles in the transfection process.
Publisher
John Wiley & Sons, Inc,John Wiley and Sons Inc
