Isolate-Specific Differences in the Conformational Dynamics and Antigenicity of HIV-1 gp120

Supplemental material

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  Fig. S1 (SDS- and native-PAGE analysis of purified gp120 proteins.)

  Fig. S2 (SAXS reconstruction, Kratky plot, and Porod-Debye analysis of SAXS data.)

  Fig. S3 to S6 (Pepsin digestion maps for 1084i gp120, 1157ip gp120, HXB2 gp120, and SF162 gp120, respectively.)

  Fig. S7 and S8 (Sequence coverage of all peptides for every isolate and of peptides that are comparable across isolates, respectively.)

  Fig. S9 to S12 (Deuteration plots of all unique 1084i peptides (±) sCD4, 1157ip peptides (±) sCD4, HXB2 peptides (±) sCD4, and SF162 peptides, respectively.)

  Fig. S13 (Heat map summary of HDX-MS data.)

  Fig. S14 and S15 (Deuteration plots for all comparable inner domain peptides and for all comparable outer domain/variable loop/bridging sheet peptides, respectively (unliganded gp120).

  Fig. S16 (Heat map summary of sCD4-bound gp120 deuteration and difference maps.)

  Fig. S17 and S18 (Deuteration plots for all comparable inner domain peptides and all comparable outer domain/variable loop/bridging sheet peptides, respectively (sCD4-bound gp120).

  Fig. S19 (Linear epitope-specific antibody peptide competition ELISA.)

  Fig. S20 (Linear epitope-specific antibody SPR binding curves.)

  Fig. S21 (Conformation-dependent antibody SPR binding curves.)

  Fig. S22 (N5i5 SPR binding curves ± sCD4.)

  Fig. S23 (17b SPR binding curves ± sCD4.)

  Fig. S24 (sCD4-induced stabilization of peptides within 17b and N5i5 epitopes.)

  Table S1 (SPR experimental details.)

  Table S2 (Chi-square error of 1:1 binding vs. fixed dissociation rate fits to CD4i antibody SPR data.)

  Supporting Information (Methods for peptide competition ELISA.)

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