Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities.

By J. Stevens, O. Blixt, L. Glaser, J. Taubenberger, P. Palese, J. Paulson, Ian A. Wilson. Journal of Molecular Biology, 2006

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Influenza A viruses: new research developments (2011, background): “The HA proteins of the human seasonal H1 and H3 virus subtypes mainly recognize receptors with terminal α-2,6-SA moieties, which are found on bronchial epithelial cells of the human upper respiratory tract (URT”
Sialic acids in human health and disease (2008, positive): “Such ‘jumps’ require the hemagglutinin component of the virus to undergo specific mutations, switching from preferentially recognizing the α2-3-linkage of sialic acids found in the intestinal epithelium of birds (where the virus resides), to preferentially binding α2-6-linked sialic acids, which are”
Review of Aerosol Transmission of Influenza A Virus (2006, background): “For the influenza A (H1N1) pandemic strain of 1918, this change required only 1 or 2 amino acid substitutions (36).”
Predominant Role of Bacterial Pneumonia as a Cause of Death in Pandemic Influenza: Implications for Pandemic Influenza Preparedness (2008, background): “receptor affinity [80]— creates both a direct pathway for second-”
Influenza Virus Evolution, Host Adaptation and Pandemic Formation (2010, background): “Glycan array and structural analyses (Chandrasekaran et al., 2008; Stevens et al., 2006) showed that the 1918 variant with a Gly at 225 had a blended α2– 3/α2–6 SA binding specificity while those sequences with an aspartic acid at 225 had a α2–6 SA binding specificity, yet there was no appreciable…”