Supplementary Materials

Supplementary Material for:

Staged induction of HIV-1 glycan–dependent broadly neutralizing antibodies

Mattia Bonsignori,* Edward F. Kreider, Daniela Fera, R. Ryan Meyerhoff, Todd Bradley, Kevin Wiehe, S. Munir Alam, Baptiste Aussedat, William E. Walkowicz, Kwan-Ki Hwang, Kevin O. Saunders, Ruijun Zhang, Morgan A. Gladden, Anthony Monroe, Amit Kumar, Shi-Mao Xia, Melissa Cooper, Mark K. Louder, Krisha McKee, Robert T. Bailer, Brendan W. Pier, Claudia A. Jette, Garnett Kelsoe, Wilton B. Williams, Lynn Morris, John Kappes, Kshitij Wagh, Gift Kamanga, Myron S. Cohen, Peter T. Hraber, David C. Montefiori, Ashley Trama, Hua-Xin Liao, Thomas B. Kepler, M. Anthony Moody, Feng Gao, Samuel J. Danishefsky, John R. Mascola, George M. Shaw, Beatrice H. Hahn, Stephen C. Harrison, Bette T. Korber,* Barton F. Haynes*

*Corresponding author. Email: mattia.bonsignori{at}dm.duke.edu (M.B.); btk{at}lanl.gov (B.T.K.); barton.haynes{at}dm.duke.edu (B.F.H.)

Published 15 March 2017, Sci. Transl. Med. 9, eaai7514 (2017)
DOI: 10.1126/scitranslmed.aai7514

This PDF file includes:

  • Materials and Methods
  • Fig. S1. Characteristics of DH270 lineage mAbs.
  • Fig. S2. DH270 lineage displays an N332-dependent V3-glycan bnAb functional profile.
  • Fig. S3. DH475 and DH272 are strain-specific, N332-glycan–dependent antibodies.
  • Fig. S4. CH848 was infected by a single TF virus.
  • Fig. S5. CH848 was infected by a subtype C virus.
  • Fig. S6. Coevolution of CH848 autologous virus and the N332-dependent V3-glycan antibody lineages DH272, DH475, and DH270.
  • Fig. S7. Mutations in CH848 Env over time.
  • Fig. S8. Accumulation of amino acid mutations in CH848 virus over time.
  • Fig. S9. CH848 virus lineage maximum likelihood phylogenetic tree rooted on the TF sequence.
  • Fig. S10. Inverse correlation between the potency of V3-glycan bnAbs and V1 length shown for the full panel of 207 viruses.
  • Fig. S11. Role of VH1-2*02 intrinsic mutability in determining DH270 lineage antibody somatic hypermutation.
  • Fig. S12. Effect of the G57R mutation on DH270.IA4 and DH270.UCA binding to Env 10.17 gp120.
  • Fig. S13. Virus signature analysis.
  • Fig. S14. Autologous Env V1 length associations with DH270 lineage neutralization and gp120 binding.
  • Fig. S15. Sequence and structural comparison of DH270.UCA1 and DH270.UCA3.
  • Fig. S16. Accumulation of mutation in DH270 lineage antibodies.
  • Fig. S17. Negative-stain EM of DH270 Fab in complex with the 92BR SOSIP.664 trimer.
  • Fig. S18. DH270.1 and other N332 bnAbs bound to the 92BR SOSIP.664 trimer.
  • Fig. S19. DH270.1 binding kinetics to 92BR SOSIP.664 trimers with mutated PNG sites.
  • Fig. S20. DH270.1 binding kinetics to 92BR SOSIP.664 trimer with additional mutations.
  • Fig. S21. Man9-V3 glycopeptide binding of DH270 lineage antibodies.
  • Fig. S22. Example of an immunization regimen derived from studies of virus-bnAb coevolution in CH848.
  • Table S1. N332-dependent CH848 plasma neutralization.
  • Table S2. NGS longitudinal sampling of VH(D)JH rearrangements assigned to the DH270, DH272, and DH475 lineages from memory B cell mRNA.
  • Table S3. CH848 plasma neutralization breadth over time.
  • Table S4. Data collection and refinement statistics.
  • Legends for data set S1 to S4
  • References (3652)

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Other Supplementary Material for this manuscript includes the following:

  • Data set S1 (Microsoft Excel format). DH270 lineage heterologous neutralization (207-virus panel).
  • Data set S2 (Microsoft Excel format). Autologous binding and neutralization of DH270, DH272, and DH475 lineages.
  • Data set S3 (Microsoft Excel format). Heterologous neutralization on a 24-virus panel.
  • Data set S4 (Microsoft Excel format). Virus signatures.

[Download Data sets S1 to S4]