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Fig. 1 | Virology Journal

Fig. 1

From: The tyrosine 73 and serine 83 dephosphorylation of H1N1 swine influenza virus NS1 protein attenuates virus replication and induces high levels of beta interferon

Fig. 1

Phosphorylation status analysis of predicted NS1 protein phosphorylation sites in 293 T cells. a 293 T cells transfected with plasmid pCAGGS-NS1 or pCAGGS-NS1 mutant Y73F, S76A, S83A, T151A, S161A, and S195A were lysed 48 h after transfection. Protein samples were separated by SDS-PAGE containing Phos-tag (designated as Phos-tag(+))and general SDS-PAGE (designated as Phos-tag(−)),and analyzed by western blotting with mouse anti-NS1 antibodies. The Phos-tag is a ligand that shifts the mobility of phosphorylated NS1proteins.The bottom band is the NS1 protein in its unphosphorylated form. b The percentage of unphosphorylated NS1 protein in the total NS1 protein. The intensities of the unphosphorylated NS1 and total NS1 protein bands were quantified using ImageJ software. The ratios of unphosphorylated NS1 to total NS1 protein are shown

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Virology Journal

ISSN: 1743-422X