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. 2019 May 15;10:1021. doi: 10.3389/fimmu.2019.01021

Figure 2.

Figure 2

V1/V2 regions of proviral sequences isolated from an elite suppressor (EN3). (A) Alignment of functional proviral sequences isolated from an elite suppressor (EN3). V1 region is defined as amino acids 131–157 and V2 region is defined as amino acids 158–196 using sequence numbering relative to HXB2 reference standard. Arrows above the alignment show the location of four beta strands described in McLellan et al. (13). Black rectangles show the location of canonical cysteines in the V1/V2 region. Green rectangles show aberrant cysteines in functional sequences isolated from EN3. Blue rectangles show potential N-linked glycosylation sites that are part of the 13 or 15 amino acid insertion in V1. Residues circled in red were targeted in mutagenesis experiments. (B) Primary structure of EN3d071 wild type (WT) and mutants. Single point mutations of EN3d07 WT were introduced to create three different mutants of Env (EN3d071 C136A with no extra cysteines in V1, EN3d071 R(134+1)C with two extra cysteines in V1, and K170E with one extra cysteine in V1). Non-canonical cysteines are shown in red. K170E mutation is shown in blue. (C) Homology models of gp120s EN3d071 wild type (WT) and mutants. Homology models of EN3d071 C136A (18 cysteines), EN3d071 WT (19 cysteines), EN3d071 R(134+1)C (20 cysteines), and EN3d071 K170E (19 cysteines) were built using Modeler v9.21 with 5fykG template. V1 regions are shown in cyan. V2 regions are shown in gray. Cysteines located in the V1 region are shown in yellow. Polymorphisms are labeled with A136 shown in green, R(134+1) shown in orange, K170 shown in purple, and E170 shown in magenta.