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. Author manuscript; available in PMC: 2020 Feb 15.
Published in final edited form as: J Mol Biol. 2018 Dec 29;431(4):842–856. doi: 10.1016/j.jmb.2018.12.014

Figure 7: Presentation of N-glycans capped with α2,3 linked sialic acids on a glass slide lacks complexity for multivalent interaction with an HA trimer.

Figure 7:

The HA binding sites are colored cyan (to indicate multivalent binding) or red (no multivalent binding). (A) Bidentate binding of a HA to an α2–6 capped, branched N-glycan with three LacNAc repeats on each branch. (B) Bidentate binding is not possible between the equivalent glycan capped with α2–3 linked sialic acid and a HA, due to the different orientation of the sialic acid. (C) On a slide surface glycans capped with α2–3 linked sialic acid must be spaced correctly to form multivalent interactions with a HA, and no recruitment of the glycans is possible. (D) Multivalent binding of avian HA to glycans capped with α2–3 linked sialic acid may be possible on a cell surface, due to the higher density of glycans on cell surface glycoproteins (example shown is ICAM-1, with glycans attached to N-glycosylation sites). HA forms a multivalent interaction with glycans present on one ICAM-1 molecule, or between two different ICAM-1 molecules.