Skip to main content
. Author manuscript; available in PMC: 2020 May 1.
Published in final edited form as: Virology. 2019 Mar 4;531:100–113. doi: 10.1016/j.virol.2019.03.002

Table 3.

Support of replication of HDV genome by mutated forms of AgS a,b.

Mutation mutant:wt ratiod Accumulation of HDV G RNA at day 9 post-transfection, % c
Wild type e N/A 100 ± 3.79
 
U(1221)C 100:0 78.81 ± 10.04
Glu(126)Glu f
 
U(1262)C
Lys(113)Glu 5:95 69.43 ±11.23
10:90 68.04 ± 43.30
20:80 83.94 ± 10.16
40:60 76.53 ±37.75
80:20 52.61 ± 5.22
100:0 12.46 ± 2.19
 
U(1469)A 100:0 109.65 ± 1.19
Ile(44)Leu
a

The tested mutations were found in the HDV genomes recovered from M6593 (see Table 2).

b

The replication capacity was measured using co-transfection of mutation-bearing plasmid pDL444 and unmutated vector pDL542 into Huh7 cells. In these settings, the replication of HDV G RNA that is transcribed from pDL542 and cannot make delta antigen (56) depends on the AgS that is provided from the mutated version of pDL444.

c

The percentage is calculated relatively to the levels of accumulated HDV G RNA, which replication was supported by wild type AgS supplied from unmodified vector pDL444.

d

The combination of wild type (wt) and mutated form of AgS in different ratios was only examined for the change U(1262)C that causes the amino acid substitution Lys(113)Glu. In this case, co-transfection was performed using a ratio of 1:1 of pDL542:(pDL444 mutant + pDL444 wt). The shown in the table ratios of mutant:wt represent the mass ratios between pDL444 mutant and pDL444 wt plasmids.

e

The wild type AgS was supplied from the plasmid pDL444.

f

This silent mutation (in terms of amino acid change) was used as an additional control.