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. 2014 Dec;88(24):14222–14231. doi: 10.1128/JVI.01763-14

FIG 4.

FIG 4

Mapping crucial amino acids for enzymatic activity in OAS3. (A) TLC showing the activity of 2 nM OAS3 WT, 2 nM OAS3 WT without (w/o) poly(I·C), ∼20 nM D816A/D818A, and ∼5 nM R844X. The OAS3 WT was purified to homogeneity, while D816A/D818A and R844X were purified by one-step cation chromatography. ATP and 2-5A species are indicated. The activity is indicated under each lane by a plus sign for active or a minus sign for inactive (less than 1% activity compared to the wild type). (B) A Western blot confirming the presence of OAS3 WT, D816A/D818A, and R844X assessed for activity as described for panel A. (C) TLC showing the activity of homogenous OAS3 and several immunoprecipitated mutants. ATP and 2-5A species are indicated. The activity is indicated under each lane by a plus sign for active or a minus sign for inactive (less than 1% activity compared to the wild type). (D) A Western blot confirming the presence of the immunoprecipitated OAS3 mutants.