TABLE 2.
NS3 mutants used in this study
NS3 mutant | Position of mutated amino acids | Amino acid sequence deletedb | Glycosylation | Transport to Golgi |
---|---|---|---|---|
NS3 | + | + | ||
pGEMHID1a | Δ118–126 | AIIHTTLLV | − | + |
pGEMHID2a | Δ118–136 | AIIHTTLLVA AVVALLTSV | − | + |
pGEMHID3 | Δ127–136 | AAVVALLTSV | − | + |
pGEMHID4 | Δ127–147 | AAVVALLTSV CTLSSDMSAFV | − | + |
pGEMHIID1 | Δ153–162 | KTEVPSWFKS | ± | + |
pGEMHIID2 | Δ153–172 | KTEVPSWFKS LNPMLGVVNL | ± | + |
pGEMHIID3 | Δ153–182 | KTEVPSWFKS LNPMLGVVNLGATFLMMVCA | + | + |
pGEMHIID4a | Δ163–172 | LNPMLGVVNL | + | + |
pGEMHIID5a | Δ163–182 | LNPMLGVVNL GATFLMMVCA | + | + |
pGEMCT | Δ156–229 | VPSWFKSLN PMLGVVNLGA TFLMMVCAKS ERALNQQIDM IKKEVMKKQS YNDAVRMSFT EFSSIPLDGF EM PLT | + | + |
GSIc | 63 | + | + | |
GSIIc | 150 | − | + |
In these constructs, the deleted amino acids were replaced by the dipeptide RS.
The sequences that contribute to the two hydrophobic domains are underlined.
In these mutants, there is an N-to-S change at the indicated positions.