Abstract
Mathilde Richard works in the field of virology, more specifically on the evolution and pathogenesis of influenza viruses. In this mSphere of Influence article, she reflects on how the two articles "Structure of Influenza A Polymerase Bound to the Viral RNA Promoter" by A. Pflug, D. Guilligay, S. Reich, and S. Cusack (Nature 516:355-360, 2014, https://doi.org/10.1038/nature14008) and "Structural Insight into Cap-Snatching and RNA Synthesis by Influenza Polymerase" by S. Reich, D. Guilligay, A. Pflug, H. Malet, I. Berger, et al. (Nature 516:361-366, 2014, https://doi.org/10.1038/nature14009) made an impact on her by providing new grounds to study the influenza virus polymerase and its role in virus biology and evolution.
Highlights
In 2014, the Cusack research group described the high-resolution structures of the influenza A virus and influenza B virus polymerases in complex with the viral promoter in two articles published back-to-back in Nature (“Structure of Influenza A Polymerase Bound to the Viral RNA Promoter” [1]; “Structural Insight into CapSnatching and RNA Synthesis by Influenza Polymerase” [2])
To overcome technical difficulties of expressing sufficient and pure amounts of influenza virus RNA-dependent RNA polymerase (RdRp) necessary for crystallization, the Cusack group produced the polymerase subunits as a self-cleaving polyprotein expressed in insect cells from one single open reading frame (ORF) using the ComplexLINK and MultiBac technologies [3]
The genes coding for the different subunits are separated by the cleavage sequence of the NIa protease of the tobacco etch virus (TEV), which is encoded by the ORF
Summary
In 2014, the Cusack research group described the high-resolution structures of the influenza A virus and influenza B virus polymerases in complex with the viral promoter in two articles published back-to-back in Nature (“Structure of Influenza A Polymerase Bound to the Viral RNA Promoter” [1]; “Structural Insight into CapSnatching and RNA Synthesis by Influenza Polymerase” [2]). Until the studies by the Cusack research group, only crystals of fragments of the influenza virus RdRp were available, and how the subunits formed a functional protein complex was unclear.
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