Aims: The outbreak of highly pathogenic avian influenza H5N1 in poultry and the influenza A pandemic have wreaked havoc on public health. Viruses alter their carbohydrate binding preferences, thereby causing pandemics all over the world. In this study, we tried to investigate the carbohydrate binding specificity of influenza clinical isolates. Materials & methods: Biotin-conjugated polyacrylamide-based glycan epitopes were immobilized on UltraBind™ membranes and used to survey the glycan-binding preference of influenza clinical isolates, including seasonal influenza A, A(H1N1)pdm09 and influenza B viruses. In addition, the DNA sequences of influenza B virus hemagglutinin were analyzed. Results: Human influenza A, especially the A(H1N1)pdm09 viruses, accepted α2,6 and α2,3 sialylated glycans, sulfated glycans and α2,8 sialosides. Although all influenza B clinical isolates bound strongly to NeuAc, 6′-sialyl lactose and sialyl biantennary N-glycan, some viruses also recognized sulfated and α2,3 sialylated glycans. According to the nucleotide sequences of viral hemagglutinin, influenza B viruses that exhibited weak interaction with sulfated and α2,3 sialylated glycans showed fewer charged amino acids. Conclusion: The substrate specificities of influenza clinical isolates were surveyed. Influenza A exhibited more complicated glycan-binding patterns than influenza B viruses. Our findings provided a systematic investigation of receptor-binding specificities for influenza clinical isolates, as well as useful information for exploring viral tropism.
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