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

FIG 1.

FIG 1

Alignment of pOAS1, hOAS1, and OAS domains 1, 2, and 3 of OAS3 and purification of recombinant OAS3. (A) An alignment displaying residues conserved between hOAS1, pOAS1, and the three OAS domains of OAS3, denoted D1, D2, and D3, respectively. The numbers of amino acids spanned by each OAS domain in the full-length OAS3 are given in parentheses. Asterisks denote the three aspartic acid residues constituting the active sites of pOAS1 and hOAS1. Daggers denote residues crucial for dsRNA binding. A plus sign denotes the conserved lysine at position 212 in pOAS1. (B) A total of 1.5 mg OAS3 was loaded on a HiLoad 16/60 Superdex 200 column. OAS3 eluted in a single peak from the HiLoad 16/60 Superdex 200 column, and fractions D15 to E9 were collected. The chromatograms of the molecular mass markers used to estimate the mass of OAS3 is shown. (C) Coomassie-stained 8% SDS-PAGE. Load, sample loaded onto the HiLoad 16/60 Superdex 200 column; D15 to E9, fractions D15 to E9; Pool, pooled peak fractions; Concentrated, concentrated pool of the peak fractions; Marker, a low-molecular-mass marker (in kDa); pOAS1, the purified pOAS1.