Table 1.
Relative Binding of MAbs to Oligomeric Δ123
| MAb | NAb activitya | Epitope typeb | Residues known to affect bindingc | CD81 blockaded | HMW1e | HMW2e | Dimere |
|---|---|---|---|---|---|---|---|
| HC33.1 | Yes | Lin | L413, G418, W420, | + | 0.83 | 2.00 | 1.50 |
| HC84‐26 | Yes | DC | C429, L441, F442, K446, W616, | + | 0.48 | 1.10 | 1.20 |
| HC‐11 | Yes | DC | S424, T425, A426, L427, N428, C429, T435, G436, W437, L438, F442, Y443, K446,Y527A, W529, G530,D535, V536 | + | <0.11 | 0.37 | 0.67 |
| HC84‐22 | Yes | DC | W420, I422, A426, L427, N428, C429,W437, L441, F442, Y443, G530, D535, W616 | + | 0.13 | 0.42 | 0.77 |
| HC‐1 | Yes | DC | A426, N428, C429, W529, G530, D535 | + | 0.23 | 0.45 | 0.67 |
| CBH‐4D | No | DC | V536, R630‐G635, P612, L615, | – | <0.15 | <0.15 | <0.15 |
| CBH‐4B | No | DC | R630‐G635 | – | <0.02 | 0.03 | 0.34 |
| HC84‐1 | Yes | DC | A439, L441, F442, Y443, K446 | + | 0.77 | 1.30 | 0.67 |
| HC84‐27 | Yes | DC | A439, L441, F442, Y443, Q444, K446, W616 | + | 1.10 | 1.40 | 1.30 |
| CBH‐7 | Yes | DC | N540, W549 | + | 0.36 | 0.71 | 0.91 |
| AR1A | No | DC | T416, N417, P484, Y485, V538, N540, G547, W549 | + | 0.43 | 1.00 | 1.00 |
| AR1B | No | DC | Q412,W420, N423, R483, P484, Y485, G523, P525, T526, G530, T534, N540, P544, P545, G547, W549 | – | 1.00 | 1.00 | 1.00 |
| AR2A | Yes | DC | N540 | – | 1.00 | 1.00 | 1.00 |
| AR3A | Yes | DC | S424, G523, P525, G530, D535, V538, N540 | + | 0.20 | 0.50 | 1.00 |
| AR3B | Yes | DC | Q412, T416, G418, N423, S424, G523, P525, G530, D535, N540 | + | 0.01 | 0.13 | 0.42 |
| AR3C | Yes | DC | I422, T425, L427, C429, N430, E431, S432, L433, G436, L438, A439, L441, F442, Y443, K446, W529 | + | 0.28 | 0.71 | 1.00 |
| AR3D | Yes | DC | Q412, S424, G523, G530, D535 | + | 0.03 | 0.24 | 0.63 |
| HCV1 | Yes | Lin | L413, N415, G418, W420, I422 | + | 1.00 | 1.00 | 1.00 |
| H53 | No | DC | N540, W549 | – | 1.00 | 1.00 | 1.00 |
| H52 | No | Lin | C652 | – | 3.50 | 3.50 | 3.50 |
| MAb24 | Yes | Lin | L413, I414, N415, T416, G418, W420, H421 | + | 1.10 | 1.80 | 1.70 |
| MAb44 | Yes | Lin | G523, P525, N540, W549, Y613 | + | 0.91 | 1.00 | 1.00 |
| MAb26 | No | Lin | N645‐E661 | – | 1.00 | 1.00 | 1.00 |
| MAb6 | No | Lin | Y527, W529, G530, D535 | – | 0.59 | 1.00 | 1.00 |
| MAb13 | No | Lin | Y527, W529, G530 | – | 0.71 | 1.40 | 1.10 |
| MAb25 | No | Lin | Y527, W529, G530. D535 | – | 0.77 | 1.10 | 1.00 |
| MAb14 | No | DC | P525, Y527, W529, G530 | – | 0.56 | 1.00 | 0.91 |
| MAb22 | No | Lin | Y527, W529, G530 | – | 0.50 | 1.00 | 0.91 |
| MAb39 | No | Lin | G523, P525 | + | 0.77 | 0.83 | 0.83 |
Demonstrated ability to neutralize at least homologous virus.
Epitope designated as discontinuous (DC) when binding is dependent on E2 fold or Linear (Lin) when the MAb binds denatured antigen or a synthetic peptide.
Amino acid residues known to affect binding of MAb by at least 50%. References can be found in Supporting Table S2. For MAbs where crystal structures are available (HC84‐1, HC84‐27, HCV1, and AR3C), residues buried by more than 10Å are listed. Bold residue is the site of an N‐linked glycan. Residues implicated in CBH‐4B and CBH‐4D binding are a personal communication from Steven Foung. Epitope for H52 is an unpublished observation (H.E. Drummer).
Capacity of MAb to block interaction between E2 and CD81.
Relative binding of MAbs to oligomeric forms of Δ123 relative to monomeric Δ123. Original data shown in Supporting Fig. S4.