Table 1 Morphology and thermostability of SOSIP-I53-50NPs

From: Enhancing and shaping the immunogenicity of native-like HIV-1 envelope trimers with a two-component protein nanoparticle

 

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

  1. 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
  2. aRh = hydrodynamic radius
  3. bPd = polydispersity, a sample with a Pd < 14% is considered monodisperse
  4. cTm = melting temperature
  5. dValues adopted from ref. 36
  6. eValues adopted from ref. 22
  7. 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
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