title: Conditional and reversible disruption of essential herpesvirus proteins.
abstract: Elucidating the function of essential proteins of complex pathogenic viruses is impeded by a paucity of complementing systems. By fusing a destabilizing domain of the FK506-binding protein to essential cytomegalovirus proteins, we generated virus mutants in which amounts of fusion proteins and viral growth can be regulated by the synthetic ligand shield-1. This conditional approach will greatly facilitate the analysis of gene functions of herpesviruses and viruses of other families.
authors: Department of Virology, Hannover Medical School, Hannover, Germany.
authors: Mandy
authors: M
authors: Glass
authors: Andreas
authors: A
authors: Busche
authors: Karen
authors: K
authors: Wagner
authors: Martin
authors: M
authors: Messerle
authors: Eva Maria
authors: EM
authors: Borst
mesh_terms: D000818:Animals; D003587:Cytomegalovirus / Q000235:genetics; D005347:Fibroblasts / Q000821:virology; D020043:Genes, Essential; D005814:Genes, Viral; D005816:Genetic Complementation Test; D016679:Genome, Viral; D006564:Herpesviridae / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008024:Ligands; D051379:Mice; D009025:Morpholines / Q000494:pharmacology; D009154:Mutation; D055550:Protein Stability; D011993:Recombinant Fusion Proteins / Q000235:genetics; D014764:Viral Proteins / Q000235:genetics*; D014779:Virus Replication / Q000187:drug effects / Q000235:genetics
chemical_list: D008024:Ligands; D009025:Morpholines; D011993:Recombinant Fusion Proteins; C540198:Shield-1 compound; D014764:Viral Proteins