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. Author manuscript; available in PMC: 2017 Aug 1.
Published in final edited form as: Cell Rep. 2017 Apr 25;19(4):719–732. doi: 10.1016/j.celrep.2017.04.013

Figure 2. Construction and characteristics of diverse 4-glycan-deleted HIV-1 Env trimers.

Figure 2

(A) Construction of diverse glycan-deleted HIV-1 Env trimers. Chimeric soluble Env trimers of diverse HIV-1 Clade B and C strains were constructed using the gp41, and gp120 N- and C-termini regions of BG505 DS-SOSIP.664 prefusion stabilized molecule. Molecular surface of a model of the chimeric CH505.DS-SOSIP is shown with structural portions from CH505 and BG505 colored light blue and salmon, respectively (middle), the same model is shown with sequence identical to CH505 colored in light blue and sequence identical to BG505 colored in salmon (right).

(B) Overall and CD4-binding site sequence identity between diverse glycan-deleted HIV-1 Env trimers.

(C) Representative purification profiles of 4-glycan-deleted (ΔGly4) HIV Env DS-SOSIP trimers. Gel filtration and SDS-PAGE for clade A BG505 and chimeric clade C CH505 are shown.

(D) Negative stain EM of the purified glycan-deleted HIV-1 Env trimers. The proteins are highly homogenous and 2D particle class-averages are shown.

(E) BG505 (left) and CH505 (right) DS-SOSIP Man-5 models showing relative proportions of oligomannose versus complex glycosylation at each PNGS. Glycans removed in ΔGly4 proteins are indicated and glycans with >30% change in oligomannose content between wild type and ΔGly4 versions are highlighted between BG505 and CH505 SOSIP paired models and oligomannose proportions are shown and colored according to the key. Concealed glycans are indicated with dashed lines.

(F) Antigenic analysis of purified glycan-deleted HIV-1 Env trimers. Antibodies that target different HIV-1 sites of vulnerability and difference conformational states and the CD4-receptor were used to evaluate the antigenicity and conformational states.

See also Figure S2, S3 and Table S2.

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