Recognition of Sialylated Poly-N-acetyllactosamine Chains on N- and O-Linked Glycans by Human and Avian Influenza A Virus Hemagglutinins


  • We thank the Otsuka Chemical Co., Ltd for the generous gift of N-linked glycans (10 and 22), and the Consortium for Functional Glycomics (GM62116) for providing the linear sialosides used in these studies. This work was supported in part by NIH grants AI058113 (to J.C.P. and I.A.W.), GM62116 (to J.C.P.), a predoctoral fellowship from the Achievement Rewards for College Scientists Foundation (to DCE); grant GM080209 from the NIH Molecular Evolution Training Program (to D.C.E.), and the Skaggs Institute (I.A.W.).


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Human influenza viruses are proposed to recognize sialic acids (pink diamonds) on glycans extended with poly-LacNAc chains (LacNAc=(yellow circle+blue square)). N- and O-linked glycans were extended with different poly-LacNAc chains with α2-3- and α2-6-linked sialic acids recognized by human and avian influenza viruses, respectively. The specificity of recombinant hemagglutinins (receptors in green) was investigated by using glycan microarray technology.