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. 2006 Feb;55(2):266–274. doi: 10.1136/gut.2005.072231

Table 1 Polyprotein processing and replicative capacity of hepatitis C virus (HCV) replicons carrying mutations within the 1073–1081 epitope.

Replicon In vitro processing* Polyprotein processing† Replicative capacity of HCV replicons‡
GND nd ++ 0.4 (–)
Wt (ET) ++ ++ 1541 (++)
1073C‐A ++ nd 2082 (++)
1074I‐A + 2.2 (–)
1074I‐E nd 16 (–)
1074I‐K 0.6 (–)
1074I‐L ++ nd 1741 (++)
1074I‐M ++ ++ 1278 (++)
1074I‐A1079W‐A 8.5 (–)
1074I‐A1081V‐A + 2.6 (–)
1075N‐A ++ ++ 0.4 (–)
1076G‐A +/– nd 3.0 (–)
1077V‐A ++ nd 4572 (++)
1078C‐A ++ ++ 4085 (++)
1079W‐A + 0.6 (–)
1079W‐A1081V‐A nd ++ 294 (+)
1080T‐A ++ nd 3689 (++)
1081V‐A ++ ++ 1713 (++)
1082Y‐A ++ + 1.0 (–)
1082Y‐F ++ nd 2861 (++)

*Self‐cleavage of the NS3‐4A protein in rabbit reticulocyte lysate, as shown in fig 4.

†Cleavage of the HCV NS3 to 5B polyprotein, as shown in fig 5A.

‡Values represent the ratio of relative light units measured 48 hours and four hours after electroporation. The four hour values, which reflect transfection efficiency, were set to 100%.

++, full processing (comparable with wild‐type); +, incomplete processing with significantly reduced amounts of NS3; −, no cleavage.

Negative control is the NS3/4A protease with a disrupted NS3/4A cleavage site, as previously described.23,24

nd, not done.