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. 2009 Mar 4;83(10):4778–4790. doi: 10.1128/JVI.02493-08

FIG. 2.

FIG. 2.

Protein steady-state levels and L4-100K methylation in A549 cells infected with H5pg4100 and H5pm4151 viruses. (A) Cells were infected in the absence (AdOx−) or presence (AdOx+) of AdOx and harvested at the indicated times after infection (h p.i.). Total cell extracts were prepared from noninfected (0) and infected cells, and 25-μg aliquots of lysates were separated by SDS-10% PAGE and analyzed by immunoblotting using L4-100K rat MAb 6B10 or mouse MAb B6-8, recognizing the E2A-72K protein. The same lysates were used for immunoprecipitation (IP) with MAb Asym-24, detecting asymmetrically dimethylated arginine residues (B). The immunocomplexes were separated by SDS-10% PAGE and analyzed by immunoblotting using MAb 6B10. (C) Binding of PRMT1 to L4-100K in infected cells. Whole lysates were prepared as described above and used for immunoblotting with MAb 6B10 (upper panel) and immunoprecipitation with anti-PRMT1 MAb.