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. 2023 Oct 24;31:101142. doi: 10.1016/j.omtm.2023.101142

Figure 5.

Figure 5

Characterization of rAAV2-M203V and -M211V

(A) Amino sequence alignment of the VP3 N-terminal region of AAV1-11 and the number of matches with the AAV2 sequence. AAV7 and AAV9 had a the highly conserved sequence with AAV2 for the VP3 N-terminal region. (B) Productivity comparison between rAAV2 wild-type (WT) and rAAV2 variants at 24, 48, and 72 h post-transfection. Productivity assay results are presented as the means of three independent production batches. Error bars represent ± SD of titer in three independent production batches. (C) CGE electropherograms of rAAV2-WT and rAAV2 variants. (D) Deconvoluted mass values of rAAV2-WT and rAAV2 variants for VP3 and VP3 clip. (E) VP stoichiometry of rAAV2-WT and rAAV2 variants. To determine the VP molar stoichiometry, areas of the CGE peaks detected at 214 nm were divided by the molar extinction efficient of VPs at 214 nm, reflecting the UV absorbance of peptide bonds and amino acids under denatured conditions. (F) Thermal unfolding plot of rAAV2-WT and rAAV2 variants.