title: Detection of protein interactions during virus infection by bimolecular fluorescence complementation.
abstract: The bimolecular fluorescence complementation (BiFC) allows not only the investigation of protein interactions but also the visualization of protein complexes in living cells. This method is based on two nonfluorescent fragments of fluorescent proteins (FPs) which can reassemble into a fluorescent complex. The formation of the fluorescent complex requires association of the nonfluorescent fragments which is facilitated by their fusion to two proteins that interact with each other. It is necessary to confirm the specificity of the BiFC signal, e.g., by using proteins with a mutated interaction site. Here, we describe a BiFC protocol adapted for the investigation of protein-protein interactions during herpesvirus infection.
authors.affiliation: Institute of Virology, Ulm University Medical Center, Ulm, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Jens
authors.initials: J
authors.lastname: von Einem
mesh_terms: D003587:Cytomegalovirus / Q000502:physiology*; D015870:Gene Expression; D005822:Genetic Vectors / Q000235:genetics; D006801:Humans; D008163:Luminescent Measurements / Q000379:methods*; D008164:Luminescent Proteins / Q000378:metabolism*; D025941:Protein Interaction Mapping / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D014162:Transfection
chemical_list: D008164:Luminescent Proteins; D011993:Recombinant Fusion Proteins