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Journal of Virology, March 2001, p. 2276-2287, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2276-2287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Cécile Delorme,1,* Harald Brüssow,1,* Josette Sidoti,1 Niamh Roche,2 Karl-Anders Karlsson,2 Jean-Richard Neeser,1 and Susann Teneberg2

Nestlé Research Center, Nestec Ltd., CH-1000 Lausanne 26, Switzerland,1 and Institute of Medical Biochemistry, Göteborg University, SE 405 30 Göteborg, Sweden2

Received 26 June 2000/Accepted 30 November 2000

The glycosphingolipid binding specificities of neuraminidase-sensitive (simian SA11 and bovine NCDV) and neuraminidase-insensitive (bovine UK) rotavirus strains were investigated using the thin-layer chromatogram binding assay. Both triple-layered and double-layered viral particles of SA11, NCDV, and UK bound to nonacid glycosphingolipids, including gangliotetraosylceramide (GA1; also called asialo-GM1) and gangliotriaosylceramide (GA2; also called asialo-GM2). Binding to gangliosides was observed with triple-layered particles but not with double-layered particles. The neuraminidase-sensitive and neuraminidase-insensitive rotavirus strains showed distinct ganglioside binding specificities. All three strains bound to sialylneolactotetraosylceramide and GM2 and GD1a gangliosides. However, NeuAc-GM3 and the GM1 ganglioside were recognized by rotavirus strain UK but not by strains SA11 and NCDV. Conversely, NeuGc-GM3 was bound by rotaviruses SA11 and NCDV but not by rotavirus UK. Thus, neuraminidase-sensitive strains bind to external sialic acid residues in gangliosides, while neuraminidase-insensitive strains recognize gangliosides with internal sialic acids, which are resistant to neuraminidase treatment. By testing a panel of gangliosides with triple-layered particles of SA11 and NCDV, the terminal sequence sialyl-galactose (NeuGc/NeuAcalpha 3-Galbeta ) was identified as the minimal structural element required for the binding of these strains. The binding of triple-layered particles of SA11 and NCDV to NeuGc-GM3, but not to NeuAc-GM3, suggested that the sequence NeuGcalpha 3Galbeta is preferred to NeuAcalpha 3Galbeta . Further dissection of this binding epitope showed that the carboxyl group and glycerol side chain of sialic acid played an important role in the binding of such triple-layered particles.

* Corresponding author. Mailing address: Nestlé Research Center, P.O. Box 44, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Switzerland. Phone: 41 21 785 91 55. Fax: 41 21 785 85 49. E-mail: cecile.delorme{at}rdls.nestle.com and harald.bruessow{at}rdls.nestle.com.

Journal of Virology, March 2001, p. 2276-2287, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2276-2287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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