tetano
Editor, Senior Moderator
Virology. 2014 Jul 17;464-465C:11-20. doi: 10.1016/j.virol.2014.06.033. [Epub ahead of print]
An important amino acid in nucleoprotein contributes to influenza A virus replication by interacting with polymerase PB2.
Gui X1, Li R2, Zhang X1, Shen C1, Yu H3, Guo X1, Kang Y1, Chen J1, Chen H4, Chen Y5, Xia N6.
Author information
Abstract
The nucleoprotein (NP) of influenza A virus plays a critical role in the formation of viral ribonucleoprotein (vRNP) complex. However, it remains unclear which key residues in NP are associated with the assembly of vRNP and contribute to virus replication. Here, a highly conserved aspartic acid at residue 88 (D88) of NP was identified by molecular docking of NP with the Fv region of a broad-spectrum anti-NP mAb 19C10 and further demonstrated to be an important residue contributes to the RNP activity, virus growth in MDCK cells and replication in lungs of infected mice by comparing recombinant wild-type A/WSN/1933 virus to the mutant virus that contains an alanine instead of aspartic acid at NP residue 88. D88 was also predicted to interact with PB2 by molecular docking and further verified by immunoprecipitation. These findings provide new information for understanding the interaction between NP and other polymerase subunits in virus replication.
Copyright ? 2014 Elsevier Inc. All rights reserved.
KEYWORDS:
Docking; Epitope; Influenza A virus; Interaction; Nucleoprotein; Replication; vRNP complex
PMID:
25043584
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25043584
An important amino acid in nucleoprotein contributes to influenza A virus replication by interacting with polymerase PB2.
Gui X1, Li R2, Zhang X1, Shen C1, Yu H3, Guo X1, Kang Y1, Chen J1, Chen H4, Chen Y5, Xia N6.
Author information
Abstract
The nucleoprotein (NP) of influenza A virus plays a critical role in the formation of viral ribonucleoprotein (vRNP) complex. However, it remains unclear which key residues in NP are associated with the assembly of vRNP and contribute to virus replication. Here, a highly conserved aspartic acid at residue 88 (D88) of NP was identified by molecular docking of NP with the Fv region of a broad-spectrum anti-NP mAb 19C10 and further demonstrated to be an important residue contributes to the RNP activity, virus growth in MDCK cells and replication in lungs of infected mice by comparing recombinant wild-type A/WSN/1933 virus to the mutant virus that contains an alanine instead of aspartic acid at NP residue 88. D88 was also predicted to interact with PB2 by molecular docking and further verified by immunoprecipitation. These findings provide new information for understanding the interaction between NP and other polymerase subunits in virus replication.
Copyright ? 2014 Elsevier Inc. All rights reserved.
KEYWORDS:
Docking; Epitope; Influenza A virus; Interaction; Nucleoprotein; Replication; vRNP complex
PMID:
25043584
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25043584