Table 6.
CA/p2 processing efficiencies of the HXB2 and PR-2 proteases
| Substrate | Relative substrate conversion | ||
|---|---|---|---|
| HXB2 | PR-2 | Ratio (PR-2/HXB2) |
|
| WT | 1 | 1 | - |
| V362I | 0.87 | 1.3 | 1.49 |
| A364V | 7.6 | 11 | 1.45 |
Comparison of the CA/p2 processing efficiencies of the HXB2 and PR-2 protease enzymes. Three different nonapeptides representing the CA/p2 cleavage site were cleaved with either the HXB2 or the PR-2 protease: 1. wild-type (WT) KARVL↓AEANLe-NH2, 2. (V362I) KARIL↓AEANLe-NH2 and 3. (A364V) KARVL↓VEANLe-NH2. The bevirimat resistance mutations are underlined and the arrow indicates the actual junction. The cleavage efficiency of the WT substrate was set to 1, conversion of substrates with V362I or A364V was measured relative to the conversion of the WT substrate. The test was performed in triplicate.