Science Immunology

Supplementary Materials

Supplementary Material for:

Potent and broad HIV-neutralizing antibodies in memory B cells and plasma

LaTonya D. Williams, Gilad Ofek, Sebastian Schätzle, Jonathan R. McDaniel, Xiaozhi Lu, Nathan I. Nicely, Liming Wu, Caleb S. Lougheed, Todd Bradley, Mark K. Louder, Krisha McKee, Robert T. Bailer, Sijy O?Dell, Ivelin S. Georgiev, Michael S. Seaman, Robert J. Parks, Dawn J. Marshall, Kara Anasti, Guang Yang, Xiaoyan Nie, Nancy L. Tumba, Kevin Wiehe, Kshitij Wagh, Bette Korber, Thomas B. Kepler, S. Munir Alam, Lynn Morris, Gift Kamanga, Myron S. Cohen, Mattia Bonsignori, Shi-Mao Xia, David C. Montefiori, Garnett Kelsoe, Feng Gao, John R. Mascola, M. Anthony Moody, Kevin O. Saunders, Hua-Xin Liao, Georgia D. Tomaras, George Georgiou,* Barton F. Haynes*

*Corresponding author. Email: barton.haynes{at}dm.duke.edu (B.F.H.); gg{at}che.utexas.edu (G.G.)

Published 27 January 2017, Sci. Immunol. 2, eaal2200 (2017)
DOI: 10.1126/sciimmunol.aal2200

This PDF file includes:

  • Fig. S1. Epitope mapping by alanine scanning mutagenesis of C-terminal MPER residues.
  • Fig. S2. Comparison of DH511.2-MPER662–683 and DH511.2-MPER670–683 complex structures.
  • Fig. S3. Crystal structure of the unliganded DH511 variant DH511.4.
  • Fig. S4. Surface plasmon resonance analysis of binding of the DH511 clonal lineage to MPR.03 peptide.
  • Fig. S5. DH511_UCA reactivity with U1-snRNP components.
  • Fig. S6. Amino acid alignment of U1-snRNP A and B.MN gp41 reveals no regions of sequence similarity.
  • Fig. S7. Capacity for infectious virion capture develops with DH511 lineage affinity maturation.
  • Fig. S8. Capacity for DH511 lineage to bind to GCN4-gp41-inter is acquired with affinity maturation. immunology.sciencemag.org/cgi/content/full/2/7/eaal2200/DC1
  • Table S1. Sequence characteristics of MPER antibodies isolated from memory B cells.
  • Table S2A. Neutralization activity of MPER mAbs against a cross-clade 30-isolate HIV-1 Env pseudovirus panel (IC50 values).
  • Table S2B. Neutralization activity of MPER mAbs against a cross-clade 30-isolate HIV-1 Env pseudovirus panel (IC80 values).
  • Table S3. Neutralization activity of DH511.2 against a cross-clade 208-isolate HIV-1 Env pseudovirus panel.
  • Table S4. Neutralization activity of DH511.2 against a panel of 200 clade C primary HIV-1 isolates.
  • Table S5. Sequence characteristics and pairing of plasma-derived heavy and light chains identified by MS and paired VH/VL NGS.
  • Table S6. Experimental evidence for the proteomically identified bnAbs in CH0210 plasma.
  • Table S7. Neutralization activity of six plasma mAbs against four HIV-1 Env pseudoviruses.
  • Table S8. Neutralization activity of plasma mAbs DH511.11P and DH511.12P against a cross-clade 208-isolate HIV-1 Env pseudovirus panel.
  • Table S9. Neutralization activity of 35 chimeric MPER mAbs against the tier 2 HIV-1 isolate B.BG1168.
  • Table S10. Neutralization activity of chimeric mAb DH511.2_K3 against a cross-clade 208-isolate HIV-1 Env pseudovirus panel.
  • Table S11. Neutralization activity of chimeric mAb DH511.2_K3 against a panel of 100 clade C primary HIV-1 isolates.
  • Table S12. Sequences of alanine-substituted amino acid 656 to 683 MPR.03 peptides.
  • Table S13. Sequences of COT6.15 MPER mutant viruses.
  • Table S14. Neutralization activity against a series of MPER alanine mutant pseudoviruses in the COT6.15 Env background.
  • Table S15. Peptides used in structural cocrystallization studies.
  • Table S16. Crystallographic data collection and refinement statistics.
  • Table S17. Buried surface areas on heavy chain regions and gp41.
  • Table S18. Buried surface areas at the interface between DH511 lineage heavy chains and gp41, by residue.
  • Table S19. Hydrogen bonds and salt bridges.
  • Table S20. Neutralization activity of the DH511 clonal lineage against a global panel of 12 reference strains.
  • Table S21. Polyreactivity and/or autoreactivity of MPER bnAbs.
  • Table S22. Primers and PCR conditions for paired VH/VL NGS.

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