The receptor preference of influenza viruses
Article first published online: 17 MAR 2010
© 2010 Blackwell Publishing Ltd
Influenza and Other Respiratory Viruses
Volume 4, Issue 3, pages 147–153, May 2010
How to Cite
Meng, B., Marriott, A. C. and Dimmock, N. J. (2010), The receptor preference of influenza viruses. Influenza and Other Respiratory Viruses, 4: 147–153. doi: 10.1111/j.1750-2659.2010.00130.x
- Issue published online: 5 APR 2010
- Article first published online: 17 MAR 2010
- Accepted 5 January 2010. Published Online 17 March 2010.
- Cell receptor;
- influenza virus;
- N-acetyl neuraminic acid;
- surface plasmon resonance
Please cite this paper as: Meng et al. (2010) The receptor preference of influenza viruses. Influenza and Other Respiratory Viruses 4(3), 147–153.
Objectives The cell surface receptor used by an influenza virus to infect that cell is an N-acetyl neuraminic acid (NANA) residue terminally linked by an alpha2,3 or alpha2,6 bond to a carbohydrate moiety of a glycoprotein or glycolipid. Our aim was to determine a quick and technically simple method to determine cell receptor usage by whole influenza A virus particles.
Methods We employed surface plasmon resonance to detect the binding of viruses to fetuin, a naturally occurring glycoprotein that has both alpha2,3- and alpha2,6-linked NANA, and free 3′-sialyllactose or 6′-sialyllactose to compete virus binding. All virus stocks were produced in embryonated chicken’s eggs.
Results The influenza viruses tested bound preferentially to NANAalpha2,3Gal or to NANAalpha2,6Gal, or showed no preference. Two PR8 viruses had different binding preferences. Binding preferences of viruses correlated well with their known biological properties.
Conclusions Our data suggest that it is not easy to predict receptor usage by influenza viruses. However, direct experimental determination as described here can inform experiments concerned with viral pathogenesis, biology and structure. In principle, the methodology can be used for any virus that binds to a terminal NANA residue.