Science Immunology

Supplementary Materials

Supplementary Material for:

Structural basis for potent antibody-mediated neutralization of human cytomegalovirus

Sumana Chandramouli, Enrico Malito, TuongVi Nguyen, Kate Luisi, Danilo Donnarumma, Yi Xing, Nathalie Norais, Dong Yu, Andrea Carfi*

*Corresponding authors. Email: andrea.carfi{at}

Published 30 June 2017, Sci. Immunol. 2, eaan1457 (2017)
DOI: 10.1126/sciimmunol.aan1457

This PDF file includes:

  • Fig. S1. Comparison of HCMV gH/gL with related herpesvirus gH/gL.
  • Fig. S2. Surface charge distribution on Pentamer.
  • Fig. S3. Sequence conservation in gH and gL of HCMV and EBV.
  • Fig. S4. Sequence conservation in gH and gL among β-herpesviruses.
  • Fig. S5. Superposition of UL128 and ULl30 N-terminal domains with the most structurally similar chemokines, as identified by DALI.
  • Fig. S6. Cavities in the Pentamer structure.
  • Fig. S7. Pepsin digestion coverage of gH, gL, UL128, UL130, and UL131A.
  • Fig. S8. Mapping of neutralizing epitopes by HDX-MS.
  • Fig. S9. Regions of Pentamer stabilized by Fab binding.
  • Fig. S10. Electron density maps of Pentamer complexes with Fabs 8I21 and 9I6.
  • Fig. S11. Binding of soluble Pentamer to cell surfaces.
  • Table S1. Analysis of Pentamer subunit interfaces.
  • Table S2. Analysis of the Pentamer–8I21 Fab interface.
  • Table S3. Molecular determinants of Pentamer–8I21 Fab binding.
  • Table S4. Pentamer epitope mapping by HDX-MS.
  • Legends for movies S1 and S2

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Other Supplementary Material for this manuscript includes the following:

  • Movie S1 (.avi format). Pentamer structure.
  • Movie S2 (.avi format). Pentamer is flexible and adopts different conformations.

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