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. 2003 Mar;77(5):2843–2849. doi: 10.1128/JVI.77.5.2843-2849.2003

TABLE 1.

Mutation analysis of the proteinase domain of BYV L-Prolegend

Classa BYV variant Mutation Processing efficiencyb GUS activityb
I A14 R456A 100 ± 8 100 ± 13
A15 E470A 67 ± 3 87 ± 10
A16 Q481A 95 ± 5 95 ± 12
A17 D492A 93 ± 4 125 ± 17
A21 Q521A 99 ± 8 102 ± 15
A23 K543A 95 ± 6 114 ± 13
A24 H556A 72 ± 5 95 ± 10
A25 R559A 81 ± 6 86 ± 10
A27 S578A 104 ± 5 92 ± 11
II A18 R503A 92 ± 7 43 ± 3
A20 C517A 54 ± 4 27 ± 6
A22 D529A 58 ± 4 2 ± 1
A26 D571A 59 ± 3 3 ± 1
III A13 D446A 97 ± 7 <0.001
A19 C509A UDc <0.001
a

The mutant variants are divided into classes according to the levels of GUS activity. These levels are ≥86% for class I, ≤2% for class II, and <0.001% for

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class III.

b

Expressed as percentages of the levels found for the wild type. Means and standard deviations are shown.

c

UD, undetectable.