Science Immunology

Supplementary Materials

Supplementary Material for:

KIR2DS2 recognizes conserved peptides derived from viral helicases in the context of HLA-C

Mohammed M. Naiyer, Sorcha A. Cassidy, Andrea Magri, Vanessa Cowton, Kevin Chen, Salah Mansour, Hariklia Kranidioti, Berenice Mbirbindi, Pauline Rettman, Scott Harris, Liam J. Fanning, Arend Mulder, Franz H. J. Claas, Andrew D. Davidson, Arvind H. Patel, Marco A. Purbhoo, Salim I. Khakoo*

*Corresponding author. Email: s.i.khakoo{at}

Published 15 September 2017, Sci. Immunol. 2, eaal5296 (2017)
DOI: 10.1126/sciimmunol.aal5296

This PDF file includes:

  • Fig. S1. Peptide stabilization of HLA-C*0102 by HCV peptides.
  • Fig. S2. The effect of single-HCV peptides on degranulation of CD158b NK cells.
  • Fig. S3. Cytotoxicity of KIR2DS2+ NK cell clones to peptide-loaded 721.174 cells.
  • Fig. S4. KIR2DS2 tetramer binding to HLA-C*0102 and HCV peptides or VAPWNSLSL peptide derivatives.
  • Fig. S5. Flow cytometry plots comparing binding of KIR2DS2*001, KIR2DS2*007, and KIR2DS2*008 to HLA-C*0102 and peptide.
  • Fig. S6. Analysis of viral RNA and protein production in DENV replicon– containing cells compared with DENV-2–infected cells.
  • Fig. S7. Flow cytometry plots illustrating gating strategy and killing of HEK cells expressing GFP-tagged DENV replicon by NKL-2DS2 cells.
  • Table S1. Summary of HCV peptides identified to bind HLA-C*0102.
  • Table S2. Protein sequence alignment of HCVs.
  • Table S3. Flavivirus NS3 HLA-C*0102–binding peptides as determined by NetMHCpan.
  • Table S4. Accession numbers of Flavivirus sequences used to compile the alignment in Fig. 4.

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Other Supplementary Material for this manuscript includes the following:

  • Data file S1 (Microsoft Excel format). Raw data for Figs. 1 to 5.
  • Data file S2 (.pdf format). Western blot gels for Figs. 1 to 5.

Files in this Data Supplement: