Three times the charm: ComplexINC’s MultiBac tool enables structure determination of influenza C polymerase

October 29, 2015
Crystal structure of influenza C polymerase in the apo form

Crystal structure of influenza C polymerase in the apo form

The architecture of influenza C polymerase has been reported in Nature. The teams of Ervin Fodor, Jonathan Grimes and David Stuart, University of Oxford UK, have crystallized recombinant influenza C polymerase and determined its structure by X-ray diffraction methods. The crystal structure reveals a new conformation adopted by influenza polymerase in the apo state, complementing earlier crystal structure analyses of influenza A and B polymerases that were determined in the presence of viral RNA substrates. All influenza polymerases crystallized to date were produced by ComplexINC’s MultiBac technology that is at the core of the ComplexINC work programme.

“Influenza remains a major challenge to public health” says Imre Berger, ComplexINC Coordinator, who co-authored an earlier influenza structure report in Nature last year. “Together, these structures provide invaluable insight into the molecular dynamics of the polymerase in RNA bound and unbound states.”

“This impressive series of high impact publications, on a central protein complex of a major human pathogen compellingly underscores the prowess of our MultiBac technology, which has become the leading tool for multiprotein complex production in academic and industrial R&D today” adds Ismail Moarefi, CEO of CreLux and ComplexINC Joint Coordinator.

“Influenza polymerase is a key target for drug discovery to combat the disease” concludes Daniel Fitzgerald, CEO of ComplexINC spin-out Geneva Biotech which commercializes ComplexINC technologies including MultiBac.  “Geneva Biotech is delighted to offer these influenza polymerase reagents and services to the community very soon.”

The research leading to these results has received funding from the European Community's Seventh Framework Programme (FP7/2007-2013) under grant agreement N° 279039.