antibiotic resistant variant atcc 70067  (ATCC)

Journal: bioRxiv

Article Title: Biochemical characterization of naturally occurring mutations in SARS-CoV-2 RNA-dependent RNA polymerase

doi: 10.1101/2024.02.24.581855

Figure Lengend Snippet: (A) Structure of Remdesivir®-triphosphate (RTP). (B) Comparison of fluorescence curves recorded for wt RdRp (black) and for RdRp in the presence of 100µM RTP (red). (C) Calculated residual activity (RA) of wt RdRp in % of RdRp activity for reaction with 100µM RTP (red) compared to uninhibited reaction (gray). (D) Residual RdRp activities in % measured for various nsp7:nsp8:nsp12 combinations in the presence of 100µM RTP. Results represent statistically processed data from at least three independent measurements. Outliers were excluded using a Q-test at a 90 % significance level. The % of RdRp activity was calculated by comparing the area under the curve (AUC) with the AUC of wt RdRp. A paired two-tailed t-test was utilized to compare RAs of various RdRp variants with RA of RdRp composed of wt nsp7, wt nsp8 and nsp12 with indicated p values ( ns = p > 0.05; * = p ≤ 0.05; ** = p ≤ 0.01; *** = p ≤ 0.001). RFU – relative fluorescence units.

Article Snippet: Interestingly, the most Remdesivir®-resistant RdRp variant was a combination of wt nsp12 with nsp8 Q24R, exhibiting nearly double RA compared to that of the wt RdRp.

Techniques: Comparison, Fluorescence, Activity Assay, Two Tailed Test