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. 2015 Jul 28;7(1):28–45. doi: 10.1007/s13238-015-0193-x

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© The Author(s) 2015

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Cellular receptors and receptor-destroying activity of influenza C virus and influenza A and B virus. The structure of cellular receptors for HEF from influenza C virus (N-acetyl-9-O-acetylneuraminic acid) and HA from influenza A and B virus (N-acetylneuraminic acid) are shown. Both neuraminic acid derivatives are the terminal sugars in carbohydrate chains attached to glycolipids or glycoproteins located at the cellular surface. Subtypes of influenza A virus HA discriminate between an α2-6 and α2-3 linkage to the second galactosyl residue, a property that (partially) explains species specificity. HEF of influenza C virus apparently recognizes N-acetyl-9-O-acetylneuraminic acid independent of its linkage to the next sugar. HEF has also esterase activity that cleaves acetyl from the C9 position. In influenza A and B virus the receptor-destroying activity is performed by the NA protein, which hydrolyzes the glycosidic bond between sialic acid and galactosyl residues. The cleaved bonds are indicated by a red line