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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/NeuAc
3-Gal
) 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
NeuGc
3Gal
is preferred to NeuAc
3Gal
. 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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