tetano
Editor, Senior Moderator
J Virol. 2012 Oct 31. [Epub ahead of print]
Unstable polymerase-NP interaction is not responsible for avian influenza polymerase restriction in human cells.
Cauldwell AV, Moncorg? O, Barclay WS.
Source
Imperial College London, Faculty of Medicine, Division of Infectious Disease, Norfolk Place, London, W2 1PG, United Kingdom.
Abstract
Avian-origin influenza 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 co-precipitation.
PMID:
23115299
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23115299
Unstable polymerase-NP interaction is not responsible for avian influenza polymerase restriction in human cells.
Cauldwell AV, Moncorg? O, Barclay WS.
Source
Imperial College London, Faculty of Medicine, Division of Infectious Disease, Norfolk Place, London, W2 1PG, United Kingdom.
Abstract
Avian-origin influenza 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 co-precipitation.
PMID:
23115299
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23115299