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Table 1 Specific polymerization activities and AZT resistance of SFVmac PR-RTs and corresponding viruses

From: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase

Enzyme 1 SPAC p-value 2 AZTMP excision (%) 3 Viral titer in %
w/o AZT 5 μM AZT
WT 28.6 (±3.1) - 3.0 (±1.1) 100 <0.1
K211I 7.0 (±4.8) 0.005 2.4 (±1.4) 1.2 (±1.2) <0.1
I224T 22.5 (±10.3) 0.410 3.5 (±1.4) 146.5 (±21.4) 0.1
S345T 28.8 (±8.3) 0.977 10.4 (±1.2) 40.0 (±16.8) 1.1 (±1.0)
E350K 44.7 (±2.1) 0.003 2.8 (±0.7) 31.7 (±8.8) <0.1
mt2a 13.3 (±0.9) 0.009 14.5 (±0.7) <0.1 <0.1
mt2b 8.7 (±2.9) 0.001 7.9 (±0.6) 23.0 (±7.9) <0.1
mt2c 32.6 (±13.8) 0.667 18.7 (±1.2) 20.6 (±5.5) 3.0 (±2.1)
mt3 15.5 (±2.6) 0.005 35.4 (±0.6) 8.6 (±2.7) 2.8 (±1.3)
mt4 21.7 (±3.9) 0.079 37.9 (±1.3) 113.0 (±19.2) 68.8 (±18.8)
  1. 1SPAC, specific activity in U/10 min*μgprotein. One Unit (U) catalyzes the incorporation of 1 nmol TTP in a poly(rA)/oligo(dT)15 in 10 min at 37°C by 1 μg PR-RT. The values are the means and standard deviations of at least three independent experiments. The p-values were calculated using the unpaired t-test in which we compared each variant with the WT. p-values ≤0.05 are considered significant. 2Quantification of AZTMP removal depicted in Figure 2C was achieved by phosphoimaging. The amount of unblocked primer after AZTMP excision (P30) is equivalent to the quantity of excised AZTMP and is given as a percentage of the total amount of primer in the reaction. 3Data taken from [11]. The viral titers in the cell free supernatants of the WT in the absence of AZT were set to 100% ( viral titer of 7 x 104). Titers of mutant viruses are expressed relative to the WT. Standard errors are given in parenthesis.