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Fret detection can identify which host cells are targeted by a pathogen using effector proteins.
Fluorescence resonance energy transfer (FRET) is a potent method for studying molecular interactions inside living cells with improved spatial (angstrom) and temporal (nanosecond) resolution, distance range, and sensitivity as well as a broader range of biological applications thanks to recent developments in fluorescence microscopy and the creation of new fluorescent probes.
An excited molecule fluorophore (the donor) transfers energy non-radiatively to another fluorophore (the acceptor) through an intermolecular long-range dipole-dipole coupling phenomenon known as fluorescence resonance energy transfer (FRET). EGF receptor (EGFR) dimerization and its conformational state are detected via FRET (Gadella and Jovin, 1995). The EGFR existing on cells was made available for binding by fluorescently tagged EGF molecules with fluorescein donor and rhodamine acceptor.
FRET is a very effective tool for spotting possible molecular interactions and is applicable to methods including flow cytometry, immunocytochemistry, immunohistochemistry, and ELISA. Due to its simplicity, sensitivity, and ease of automation, FRET is also perfectly suited for High Throughput Screening (HTS). Detecting interactions between two biomolecules, such as the binding of a ligand to a receptor, is one common application of FRET. A FRET signal can only be seen when the biomolecules are close together as a result of a binding event. The success of FRET depends on the use of superior labelled reagents. These could be proteins, peptides, or antibodies, depending on the experiment setup planned.
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