Science Advances

Supplementary Materials

The PDF file includes:

  • Supplementary Methods
  • Table S1. IAV strains used in this work.
  • Fig. S1. Success of the HL-SGM print is further validated by lectin binding after A. ureafaciens NA treatment.
  • Fig. S2. HPLC chromatograms overlaid with the HL-SGM binding profile for Penn indicate that glycan specificity is more important for virus binding than abundance of glycan.
  • Fig. S3. Conditions for NA treatment of the microarrays are confirmed on a defined N-glycan microarray, and those enzymatic conditions are applied to the HL-SGM for an avian and swine strain, revealing the same Sia-independent binding.
  • Fig. S4. MALDI-TOF-MS characterization of additional glycan fractions reveals phosphorylated glycans and sialylated glycans.
  • Fig. S5. Presence of sialylated or phosphorylated glycans within the human lung fractions is confirmed by peak shifts in the HPLC profile after enzymatic treatment due to phosphatase or NA sensitivity.
  • Fig. S6. Phosphatase conditions for the HL-SGM were optimized on a defined mannose phosphate glycan microarray using binding of Fv M6P-1.
  • Fig. S7. Hapten competition studies indicate that binding to sialylated glycans can be inhibited by sialyllactose, but not Fv M6P-1, which binds to the mannose phosphate array while Penn does not.
  • Fig. S8. Proteomics of Penn grown in canine kidney cells identifies the canine MPR protein.

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Other Supplementary Material for this manuscript includes the following:

  • Table S2. Raw glycan microarray data (Excel file).

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