title: Unstable polymerase-nucleoprotein interaction is not responsible for avian influenza virus polymerase restriction in human cells.
abstract: Avian-origin influenza virus polymerase activity can be dramatically increased in human cells with the PB2 E627K mutation. Previously, others have proposed that this mutation increases the stability of the viral ribonucleoprotein complex (vRNP) measured by the interaction between PB2 and NP. However, we demonstrate here that a variety of PB2 adaptive mutations, including E627K, do not enhance the stability of the vRNP but rather increase the amount of replicated RNA that results in more PB2-NP coprecipitation.
authors.affiliation: Imperial College London, Faculty of Medicine, Division of Infectious Disease, London, United Kingdom.
authors.forename: Anna V
authors.initials: AV
authors.lastname: Cauldwell
authors.forename: Olivier
authors.initials: O
authors.lastname: Moncorgé
authors.forename: Wendy S
authors.initials: WS
authors.lastname: Barclay
mesh_terms: D000818:Animals; D001717:Birds / Q000821:virology; D002460:Cell Line; D006801:Humans; D009980:Influenza A virus / Q000276:immunology* / Q000302:isolation & purification / Q000502:physiology*; D005585:Influenza in Birds / Q000821:virology; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D012324:RNA-Dependent RNA Polymerase / Q000235:genetics / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D050505:Mutant Proteins; C057027:PB2 protein, Influenzavirus A; D012261:Ribonucleoproteins; D014764:Viral Proteins; D012324:RNA-Dependent RNA Polymerase