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: Anna V Cauldwell, Olivier Moncorgé, Wendy S Barclay
• Journal: Journal of virology (J Virol) Vol. 87 Issue 2 Pg. 1278-84 (Jan 2013) ISSN: 1098-5514 [Electronic] United States
• PMID: 23115299 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Mutant Proteins
• PB2 protein, Influenzavirus A
• Ribonucleoproteins
• Viral Proteins
• RNA-Dependent RNA Polymerase

Topics

• Animals
• Birds (virology)
• Cell Line
• Humans
• Influenza A virus (immunology, isolation & purification, physiology)
• Influenza in Birds (virology)
• Mutant Proteins (genetics, metabolism)
• Protein Binding
• RNA-Dependent RNA Polymerase (genetics, metabolism)
• Ribonucleoproteins (metabolism)
• Viral Proteins (genetics, metabolism)
• Virus Replication