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Search for additional influenza virus to cell interactions.
E M Rapoport1, L V Mochalova, H-J Gabius
1Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow, Russia.
Glycoconjugate Journal
|April 1, 2006
Summary
Influenza viruses may use a non-sialic acid receptor, potentially a sulfated oligosaccharide, for cell entry. This discovery challenges the long-held belief that sialyl oligosaccharides are the only influenza virus receptors.
Area of Science:
- Virology
- Glycobiology
- Cell Biology
Background:
- Sialyl oligosaccharides are traditionally recognized as the primary receptors for influenza viruses.
- Some influenza virus strains can replicate in sialic acid-deficient host cells, suggesting alternative entry mechanisms.
Purpose of the Study:
- To investigate the potential for a non-sialic acid receptor in influenza virus cell entry.
- To explore the role of host cell lectin recognition of viral carbohydrate ligands.
Main Methods:
- Utilized polyacrylamide neoglycoconjugates and antibodies to test for galactose-, sialic acid-, mannoside-, and sulfo-N-acetyllactosamine-binding lectins on MDCK and Vero cells.
- Probed influenza A and B viruses with neoglycoconjugates to identify specific binding properties.
Main Results:
- MDCK cells exhibited stronger binding to galactoside probes compared to Vero cells.
- Vero cells showed preferential binding to sialoside, mannoside, and various sulfo-oligosaccharide probes.
- Influenza A and B viruses specifically bound to 6'-HSO (3) LacNAc, a sulfated oligosaccharide, with an affinity comparable to sialooligosaccharides, independent of sialooligosaccharide inhibition.
Conclusions:
- A non-sialic acid receptor, specifically involving 6'-HSO (3) LacNAc recognition, likely mediates influenza virus binding and entry.
- This finding expands our understanding of influenza virus tropism and host-cell interactions beyond sialic acid dependence.