TABLE 1.
HveA contact residues
| HveA contact residue | No. of interactionsa
|
gD residue(s) contacted | Effect of mutationb on:
|
Cate- gory | ||
|---|---|---|---|---|---|---|
| Side chain | Main chain | gD binding | HSV entry | |||
| K18 | 1 | 1 | A7, T29 | Wild type | Wild type | 1 |
| S20 | 4 | 1 | A7, M11 | Wild type | Wild type | 1 |
| P21 | 1 | P14 | Wild type | Wild type | 1 | |
| G30 | 2 | P32 | Wild type | Wild type | 1 | |
| E31 | 1 | P32 | Wild type | Wild type | 1 | |
| L32 | 3 | P31 | Wild type | Wild type | 1 | |
| T33 | 3 | P31, P32 | Wild type | Wild type | 1 | |
| E38 | 4 | 2 | D26, V24 | Wild type | Wild type | 1 |
| L49 | 1 | A7 | Wild type | Wild type | 1 | |
| R75 | 5 | 6 | P14, N15 | Increased | Wild type | 2 |
| P17 | 1 | 3 | T29, D30 | Reduced | Wild type | 3 |
| K26 | 4 | D26 | Reduced | Wild type | 3 | |
| G34 | 6 | T29, D30, L28 | Reduced | Wild type | 3 | |
| T35 | 1 | 11 | T29, L28, Q27 | Reduced | Wild type | 3 |
| V36 | 2 | Q27 | Reduced | Wild type | 3 | |
| P39 | 4 | V24, L25 | Reduced | Wild type | 3 | |
| S74 | 2 | 5 | N15 | Reduced | Wild type | 3 |
| T76 | 2 | 1 | P14, N15 | Reduced | Wild type | 3 |
| G22 | 1 | P14 | Negative | Negative | 4 | |
| Y23 | 14 | M11, A12, L25 | Negative | Negative | 4 | |
| C37 | 2 | 12 | M11, D26, Q27, T29 | Negative | Negative | 4 |
a
An interaction was defined as an atom on an HveA residue coming within 4 Å of an atom on a gD residue. Side chain interactions were defined as interactions involving atoms on an HveA residue that are directly eliminated by alanine substitution, i.e., atoms downstream from the Cβ of the residue. Main chain interactions were defined as interactions involving atoms not eliminated by alanine substitution, i.e., atoms upstream from and including the Cβ.
b
Each contact residue was replaced with alanine individually, and the mutant proteins were assessed for ability to bind gD and mediate HSV entry.