TABLE 3.
Summary of MAb binding to DENV-2 DIII mutants expressed on the surfaces of yeast cells
MAb | MAb binding to mutanta
|
|||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
T303Y | G304Y | K305E | K307N | K307Q | K307I | K307E | K310E | T315G | T315G and S331Y | H317Y | R323E | E327R | D329G | D329R | G330D | S331Y | E338D | T359I | E383G | P384A | P384N | N390H | N390Y | |
Type-specific neutralizing MAbs | ||||||||||||||||||||||||
1F1 | <1 | <1 | 98 | 100 | 81 | 36 | 88 | 48 | 100 | 51 | 96 | 100 | 27 | 37 | 37 | 2 | 100 | 100 | 100 | 3 | <1 | <1 | 100 | 76 |
3H5-1 | 60 | 1 | 93 | 86 | 93 | 43 | 62 | 41 | 96 | 88 | 92 | 100 | 39 | 99 | 48 | 100 | 100 | 84 | 100 | 5 | <1 | <1 | 100 | 60 |
6B6-10 | 33 | 2 | 98 | 80 | 90 | 67 | 85 | 44 | 100 | <1 | 100 | 100 | 26 | <1 | 2 | <1 | <1 | 100 | 100 | 100 | 17 | 31 | 100 | 76 |
9A3D-8 | 88 | 19 | 76 | 89 | 67 | 29 | 5 | 63 | 83 | 67 | 100 | 100 | 17 | 100 | 100 | 87 | 100 | 100 | 100 | 87 | 59 | 60 | 100 | 75 |
M8051122 | 68 | 1 | 67 | 92 | 90 | 67 | 48 | 17 | ND | ND | ND | 42 | 64 | 60 | 54 | 100 | 100 | 100 | 100 | 4 | 3 | 1 | 54 | 90 |
9F16 | 100 | 1 | 100 | 100 | 100 | 100 | 69 | 33 | ND | ND | ND | 59 | 83 | 100 | 80 | 100 | 89 | 100 | 100 | 1 | 2 | 2 | 78 | 59 |
9F11 | 89 | 2 | 100 | 89 | 100 | 60 | 60 | 23 | ND | ND | ND | 82 | 48 | 100 | 66 | 100 | 88 | 89 | 63 | <1 | 1 | <1 | 62 | 100 |
2Q1899 | 80.8 | 2 | 100 | 100 | 100 | 80 | 43 | 25 | 100 | 100 | 100 | 69 | 98 | 93 | 44 | 100 | 56 | 100 | 100 | 1 | 2 | <1 | 43 | 100 |
Subcomplex-specific neutralizing MAbs | ||||||||||||||||||||||||
9D12 | 35 | 9 | 4 | 32 | 32 | 21 | 17 | <1 | 83 | 76 | 100 | 100 | 100 | 45 | 28 | 72 | 58 | 74 | 100 | 74 | 40 | 3 | 66 | 32 |
1A1D-2 | 100 | 4 | <1 | <1 | <1 | <1 | <1 | <1 | 67 | 73 | 100 | 100 | 100 | 100 | 100 | 100 | 100 | 100 | 100 | 90 | 68 | 47 | 100 | 74 |
Nonneutralizing MAbs | ||||||||||||||||||||||||
5A2-7 | 100 | 40 | 100 | 100 | 98 | 62 | 100 | 27 | 29 | 5 | 17 | 100 | 60 | 66 | 86 | 100 | 89 | 78 | 100 | 38 | 100 | 83 | 84 | 89 |
13D4-1 | 74 | 100 | 94 | 99 | 59 | 51 | 100 | 44 | 100 | 3 | 2 | 100 | 67 | 93 | 87 | 100 | 93 | 100 | 8 | 69 | 100 | 76 | 90 | 90 |
WN E111 | 100 | 92 | 61 | 93 | 100 | 70 | 86 | 35 | 100 | <1 | 14 | 61 | 76 | 17 | 85 | 100 | 100 | 74 | 100 | 100 | 93 | 74 | 100 | 86 |
WN E114 | 100 | 2 | 60 | 78 | 61 | 48 | 45 | 4 | 100 | 100 | 100 | 72 | 37 | 47 | 46 | 100 | 91 | 42 | 100 | 90 | 49 | 48 | 75 | 56 |
Values shown were obtained by dividing the total fluorescence product (percent positive population × mean linear fluorescence intensity) for a mutant for each individual antibody by the total fluorescence product for wild-type DIII. Values in bold indicate reductions in MAb binding of >80% for a given mutation. The results are averages for three to five independent experiments for each mutant and each antibody. Since the G304Y mutant had slightly less surface expression on yeast cells, the values for this mutant only were normalized to the strongest binding antibody for that mutant × 100. ND, not determined.