Rotaviruses specifically bind to the neutral glycosphingolipid Asialo-GM1

Rodney E. Willoughby, Robert H Yolken, Ronald Lee Schnaar

Research output: Contribution to journalArticle

Abstract

Rotaviruses are the major etiologic agents of severe diarrhea in children. Many rotaviruses encode a hemagglutinin which binds to sialic acids. We report that rotaviruses specifically recognize the neutral glycosphingolipid gangliotetraosylceramide (asialo-GM1 or GA1). GA1 resolved by thin-layer Chromatography is bound by rotavirus, and binding is blocked by neutralizing rotavirus antiserum. Similar glycosphingolipid structures, such as globoside, gangliotriaosylceramide, and GA1 oxidized with galactose oxidase are ineffective in binding rotavirus. Other enteric viruses also specifically bind GA1. GA1 adsorbed to polystyrene beads inhibits rotavirus replication in vitro (as do anti-GA1 antibodies). The use of orally administered immobilized GA1 or anti-GA1 antibodies may prove useful in preventing or attenuating rotaviral and other enteric viral infections.

Original languageEnglish (US)
Pages (from-to)4830-4835
Number of pages6
JournalJournal of Virology
Volume64
Issue number10
StatePublished - 1990

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Neutral Glycosphingolipids
glycosphingolipids
Rotavirus
Anti-Idiotypic Antibodies
Globosides
Galactose Oxidase
Sialic Acids
Glycosphingolipids
Enterovirus
antibodies
sialic acids
Polystyrenes
polystyrenes
Hemagglutinins
Virus Diseases
hemagglutinins
Thin Layer Chromatography
asialo GM1 ganglioside
thin layer chromatography
neutralization

ASJC Scopus subject areas

  • Immunology

Cite this

Rotaviruses specifically bind to the neutral glycosphingolipid Asialo-GM1. / Willoughby, Rodney E.; Yolken, Robert H; Schnaar, Ronald Lee.

In: Journal of Virology, Vol. 64, No. 10, 1990, p. 4830-4835.

Research output: Contribution to journalArticle

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