A gel-capture assay for characterizing the sialyl-glycan selectivity of influenza viruses

Velkov, T., Thompson, P. E., El-Kabbani, O., Lindh, F., Stambas, J. and Rockman, S. 2011, A gel-capture assay for characterizing the sialyl-glycan selectivity of influenza viruses, Acta virologica, vol. 55, no. 2, pp. 131-137.

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Title A gel-capture assay for characterizing the sialyl-glycan selectivity of influenza viruses
Author(s) Velkov, T.
Thompson, P. E.
El-Kabbani, O.
Lindh, F.
Stambas, J.ORCID iD for Stambas, J. orcid.org/0000-0002-5690-2551
Rockman, S.
Journal name Acta virologica
Volume number 55
Issue number 2
Start page 131
End page 137
Total pages 7
Publisher Slovenska Akademia Vied * Virologicky Ustav
Place of publication Bratislava, Slovakia
Publication date 2011
ISSN 0001-723X
Summary Sialic acids (SA) usually linked to galactose (Gal) in an α2,6- or α2,3-configuration are considered the main cell receptors for influenza viruses, in particular for their hemagglutinins (HA). The typing of influenza virus HA receptor selectivity is relevant for understanding the transmissibility of avian and swine viruses to the human population. In this study we developed a simple and inexpensive gel-capture assay (GCA) of the influenza virus HA receptor-binding selectivity. Its principle is the binding of soluble influenza virus to pentasaccharide analogs, representatives of receptors of human and avian influenza viruses, immobilized on a gel resin. The human and avian analogs consisted of a sialyllactose-N-tetraose c (LSTc) [Neu5Ac(α2,6)Gal(β1-3)GlcNAc(β1-3)Gal(β1-4)Glc] and a sialyllactose-N-tetraose a (LSTa) [Neu5Ac(α2,3)Gal(β1-3)GlcNAc(β1-3)Gal(β1-4)Glc], respectively. Following equilibration, the unbound virus is washed away and the bound one is assayed via HA by densitometry as a function of the analog concentration. Using GCA, the receptor selectivity of three influenza viruses of different HA subtype was investigated. The results showed that the egg-adapted A/California/07/2009 (H1N1) virus exhibited an avian α2,3-linked LSTa selectivity, however, it retained the ability to bind to the α2,6-linked LSTc human receptor analog. Influenza B virus B/Florida/4/2006 showed α2,6-linked LSTc selectivity and a poor α2,3-linked LSTa avidity. The H3N2 virus A/Wisconsin/15/2009 displayed almost comparable avidity for both receptor analogs with a marginally greater α2,3-linked LSTa avidity. The described assay protocol provides a simple and rapid method for the characterization of influenza virus HA receptor binding selectivity. Keywords: influenza virus; hemagglutinin; receptor; sialyllactose-N-tetraose; gel-capture assay.
Language eng
Field of Research 060506 Virology
Socio Economic Objective 920109 Infectious Diseases
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
HERDC collection year 2011
Copyright notice ©2011, Slovenska Akademia Vied * Virologicky Ustav
Persistent URL http://hdl.handle.net/10536/DRO/DU:30035850

Document type: Journal Article
Collections: Faculty of Health
School of Medicine
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