Table 1.
Morphology and thermostability of SOSIP-I53-50NPs
| Morphology (DLS) | Thermostability (nanoDSF) | |||
|---|---|---|---|---|
| Rh (nm)a | Pd (%)b | Tm1 (°C)c | Tm2 (°C)c | |
| BG505 SOSIP | 6.7d | 4.4d | 72.4 (±1.3) | – |
| BG505 SOSIP-I53-50A.1NT1 | n.d. | n.d. | 72.6 (±0.6) | – |
| BG505 SOSIP-I53-50NP | 22.6 | 5.2 | 72.5 (±0.2) | 82.0 (±0.2) |
| ConM SOSIP | 6.4e | 12.5e | 65.7 (±0.1) | – |
| ConM SOSIP-I53-50A | n.d. | n.d. | 67.8 (±0.1) | – |
| ConM SOSIP-I53-50NP | 22.6 | 7.1 | 69.1 (±0.1) | 84.4 (±0.2)f |
| ZM197M SOSIP-I53-50NP | 24.6 | 13.8 | 72.1 (±0.1) | 83.9 (±0.6)f |
| AMC011 SOSIP-I53-50NP | 23.8 | 11.0 | 74.0 (±0.4) | 89.0 (±1.3)f |
All samples have been subjected to a freeze–thaw cycle at −80 °C prior to experiments. All SOSIP-I53-50NPs have the expected Rh of an intact NP and are monodisperse after a freeze–thaw cycle at −80 °C. For BG505 and ConM, corresponding SOSIP trimers and SOSIP fusion proteins are included for comparison. The AMC011 SOSIP-I53-50NP solution was mixed 3:1 with Protein Stabilizing Cocktail (ThermoScientific) prior to freezing. NanoDSF experiments were performed three times. Shown are the means of three measurements with SDs between brackets. See also Supplementary Fig. 3. n.d. not determined
aRh = hydrodynamic radius
bPd = polydispersity, a sample with a Pd < 14% is considered monodisperse
cTm = melting temperature
dValues adopted from ref. 36
eValues adopted from ref. 22
fAs the NanoDSF software did not give a clean valley in the first derivative, it was unable to determine the Tm. Therefore, the Tm was determined manually by taking the lowest point in the first derivative