Key result
Influenza A and B virus nucleoproteins can be efficiently expressed in E. coli without codon optimization, yielding soluble monomers that react well with specific antibodies.
Why the study?
Influenza viral nucleoprotein is important for diagnostic methods, vaccines, and antiviral drugs, but expressing soluble influenza A and B nucleoproteins in E. coli without codon-optimization had not been established.
Influenza A and B nucleoproteins can be efficiently expressed in E. coli without codon optimization, preserving their native structure and immune reactivity.
May enable NP-based influenza diagnostics and antivirals; leaves open clinical validation.
Viral nucleoprotein (NP) is an abundant essential protein of an influenza virus that has important functional and structural roles. It participates in genomic organization, nuclear trafficking, RNA transcription, and genome replication. From the research point of view, NP is an important protein that is used in the development of new diagnostic methods and vaccination protocols. NP is a promising target for antiviral chemotherapeutic drugs as well. Successful expression of codon-optimized NP genes in E. coli has been reported. In this study, we demonstrated the efficient expression and purification of soluble NPs of influenza A and B viruses in E. coli without the codon-optimization of DNA sequences. This procedure preserves the co-translational protein folding, protein configuration and function. Obtained NPs of influenza A and B viruses were monomers and reacted well with mouse specific antibodies according to Western blot analysis. Our results show that both influenza A and influenza B virus NPs can be efficiently expressed in E. coli without codon-optimization.
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Yolshin et al. (2019) studied this question. Expression of influenza A and B nucleoproteins without codon optimization was evaluated on Expression and purification of soluble nucleoproteins. Influenza A and B virus nucleoproteins can be efficiently expressed in E. coli without codon optimization, yielding soluble monomers that react well with specific antibodies.
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