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Virology. 2014 Sep;464-465:11-20. doi: 10.1016/j.virol.2014.06.033. Epub 2014 Jul 18.

An important amino acid in nucleoprotein contributes to influenza A virus replication by interacting with polymerase PB2.

Author information

1
National Institute of Diagnostics and Vaccine Development in Infectiou Diseases, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China.
2
National Institute of Diagnostics and Vaccine Development in Infectiou Diseases, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, Fujian, China.
3
State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, Fujian, China.
4
State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, Fujian, China; State Key Laboratory for Emerging Infectious Diseases, Department of Microbiology, The University of Hong Kong, Hong Kong SAR, China.
5
National Institute of Diagnostics and Vaccine Development in Infectiou Diseases, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, Fujian, China. Electronic address: yxchen2008@xmu.edu.cn.
6
National Institute of Diagnostics and Vaccine Development in Infectiou Diseases, School of Life Sciences, Xiamen University, Xiamen 361102, Fujian, China; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, Fujian, China. Electronic address: nsxia@xmu.edu.cn.

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.

KEYWORDS:

Docking; Epitope; Influenza A virus; Interaction; Nucleoprotein; Replication; vRNP complex

PMID:
25043584
DOI:
10.1016/j.virol.2014.06.033
[Indexed for MEDLINE]
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