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. 1998 Apr;72(4):3362–3369. doi: 10.1128/jvi.72.4.3362-3369.1998

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 +
a

In these constructs, the deleted amino acids were replaced by the dipeptide RS. 

b

The sequences that contribute to the two hydrophobic domains are underlined. 

c

In these mutants, there is an N-to-S change at the indicated positions.