Glycan-binding preferences and genetic evolution of human seasonal influenza A (H3N2) viruses during 1999-2007 in Taiwan

Ya Fang Wang, Chuan Fa Chang, Huey Pin Tsai, Chia Yu Chi, Ih Jen Su, Jen Ren Wang

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9 Citations (Scopus)


It is generally agreed that human influenza virus preferentially binds to α-2,6-linked sialic acid-containing receptors, and mutations that change the binding preference may alter virus infectivity and host tropism. Limited information is available on the glycan-binding specificity of epidemic influenza viruses. In this study, we systemically investigated the glycan-binding preferences of human influenza A(H3N2) viruses isolated from 1999 to 2007 in Taiwan using a high-throughput carbohydrate array. The binding patterns of 37 H3N2 viruses were classified into three groups with significant binding-pattern variations. The results showed that the carbohydrate-binding patterns of H3N2 varied over time. A phylogenetic analysis of the hemagglutinin gene also revealed progressive drift year to year. Of note, the viruses that caused large outbreaks in 1999 and 2003 showed glycan-binding preferences to both α-2,3 and α-2,6 sialylated glycans. Twenty amino acid substitutions were identified primarily at antigenic sites that might contribute to H3N2 virus evolution and the change in the glycan-binding patterns. This study provides not only a systematic analysis of the receptor-binding specificity of influenza clinical isolates but also information that could help to monitor the outbreak potential and virus evolution of influenza viruses.

Original languageEnglish
Article numbere0196727
JournalPloS one
Issue number5
Publication statusPublished - 2018 May

All Science Journal Classification (ASJC) codes

  • General


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