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. 2019 Sep 19;10:4272. doi: 10.1038/s41467-019-12080-1

Fig. 1.

Fig. 1

Design and biophysical properties of BG505 SOSIP-I53-50A.1NT1. a Schematic representation of the computational docking protocol used to identify trimeric NP components suitable for fusion to BG505 SOSIP. r and ω were sampled during docking to minimize d while avoiding clashes. The C termini of BG505 SOSIP and N termini of the I53-50A trimer are shown as red and blue spheres, and the dashed line indicates the linker that connects BG505 SOSIP and I53-50A. b Sodium  dodecyl  sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of BG505 SOSIP and BG505 SOSIP-I53-50A.1NT1 under reducing (left) and non-reducing (right) conditions. c SEC chromatogram of BG505 SOSIP-I53-50A.1NT1 with peaks corresponding to aggregates and trimers annotated (left) and blue native (BN)-PAGE of trimer fractions (right). d NS-EM analysis of PGT145/SEC-purified BG505 SOSIP-I53-50A.1NT1 with BG505 SOSIP (light blue) and I53-50A.1NT1 (dark blue) annotated. Shown are 2D-class averages. e Glycan profile of BG505 SOSIP-I53-50A.1NT1 as determined by HILIC-UPLC with complex glycans in pink and oligomannose glycans in green. The pie chart represents the percentage of total complex glycans vs. oligomannose glycans per trimer. The percentages of Man5-9GlcNAc2 glycans (M5–M9) are listed in the table for BG505 SOSIP and BG505 SOSIP-I53-50A.1NT1. Source data are provided as a Source Data file