TABLE 4.
Neutralization of SF162 expressing deglycosylated Envs.
| Fold change in neutralization sensitivity compared with SF162a |
||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| V1V2b | V3 | V4 | C4V5 | |||||||||||||
| 154 | 186 | 195 | 293 | 299 | 329 | 382 | 388 | 392 | 398 | 401 | 438 | 454 | ||||
| NCSFKVTTSIRNKMQKEYALFYKLDVVPIDNDNTSYKLINCNTS | NCTRPNNNTRKSITIGPGRAFYATGDIIGDIRQAHCNIS | CNSTQLFNSTWNNTIGPNNTNGT | NITGLLLTRDGGKEISNTT | |||||||||||||
| MAb | Epitope | GM154c | GM186 | GM195 | GM293 | GM299 | GM329 | GM382 | GM388 | GM392 | GM398 | GM401 | GM438 | GM454 | ||
| P1H6 | V1 | 30.0 | 15.0 | 150.0 | 3.5 | 106.3 | 229.7 | −2.9 | 2.4 | −14.6 | 4.3 | 1.4 | 1.3 | 2.0 | ||
| P3C8 | V1 | 250.0 | 12.5 | 250.0 | 1.4 | 225.0 | 15.0 | −15.0 | 1.5 | −9.4 | 1.8 | 1.1 | −1.2 | −1.4 | ||
| P3B2 | V1 | 31.0 | 5.2 | 44.3 | 2.0 | 39.0 | 18.0 | −19.0 | −1.0 | −6.0 | 2.6 | −1.2 | 1.1 | 1.5 | ||
| P4D7 | V1 | 20.0 | 2.0 | 10.0 | 1.4 | 31.0 | 13.9 | −36.0 | −1.0 | −16.0 | 1.6 | −1.3 | 1.2 | 1.0 | ||
| P3E1 | V3 | 50.0 | −2.7 | 10.0 | 2.5 | 24000.0 | 120.0 | −2.5 | 3.2 | −5.0 | 4.4 | −1.3 | −1.5 | 1.0 | ||
| P3C5 | V3 | 4.0 | −9.7 | 1.0 | 1.4 | 203.0 | 10.9 | −1.6 | 1.1 | −1.4 | 1.5 | 1.4 | 1.2 | 1.4 | ||
a
Increase in neutralization sensitivity determined at the IC50. Changes greater than 10 fold are shown in bold. Negative numbers indicate a fold decrease in IC50 values.
b
GM154, GM186, and GM195 were replication competent viruses generated in PBMC, and neutralization of these viruses was compared with neutralization of PMBC-produced replication competent SF162 virus. In all other cases, pseudoviruses were used.
c
All GM viruses are named for the position of the N→Q mutation according to SF162 numbering.