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. Author manuscript; available in PMC: 2020 Mar 4.
Published in final edited form as: Nature. 2019 Sep 4;573(7773):287–290. doi: 10.1038/s41586-019-1530-7

Fig. 2. Mutations at the FluPolA dimer interface inhibit cRNA to vRNA replication.

Fig. 2

a, Scheme of transcription and replication by FluPolA in the context of viral ribonucleoproteins (vRNPs). b, vRNP reconstitution assay with the PA352-356A dimer mutant and complementation with the transcription-deficient PAD108A mutant. Data are mean ± s.e.m., n=3 independent transfections. Two-way ANOVA. P < 0.05 is considered significant. mRNA signals for PA352-356A with and without PAD108A were compared by two-tailed unpaired t-test. P < 0.05 is considered significant. c, Effect of the PA352-356A mutation on in vitro transcription by FluPolA primed with a capped RNA primer. Data are mean ± s.e.m., n=3 independent reactions. One-way ANOVA. P<0.05 is considered significant. d, e, Effect of the PA352-356A mutation on in vitro primer-independent replication by FluPolA on a vRNA (d) and cRNA (e) template. Data are mean ± s.e.m., n=3 independent reactions. One-way ANOVA. P < 0.05 is considered significant. For gel source data, see Supplementary Fig. 2.