Receptor Binding of Recent H3N2 Influenza Viruses
Author Information
Author(s): Kumari Kshama, Gulati Shelly, Smith David F, Gulati Upma, Cummings Richard D, Air Gillian M
Primary Institution: University of Oklahoma Health Sciences Center
Hypothesis
What are the receptor binding specificities of recent human H3N2 influenza viruses?
Conclusion
Recent human H3N2 isolates have not changed their receptor binding specificity to α2-3 sialic acid, and the ability to agglutinate chicken red cells is likely due to increased hemagglutinin density rather than affinity.
Supporting Evidence
- All recent H3N2 viruses bind to a specific subset of α2-6-sialylated oligosaccharides.
- Agglutination of chicken red cells does not correlate with binding to any oligosaccharide on the Glycan Array.
- Infectious progeny viruses were only released from MDCK cells.
Takeaway
This study looked at how recent flu viruses stick to cells. It found that just because a virus can stick to a type of cell doesn't mean it can make more viruses.
Methodology
The study used glycan arrays to analyze the binding of recent H3N2 viruses to various sialylated oligosaccharides.
Limitations
The study did not explore all possible receptor types and focused primarily on α2-6 sialic acids.
Digital Object Identifier (DOI)
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