Faculty Collaboration Database

Rotaviruses specifically bind to the neutral glycosphingolipid asialo-GM1. J Virol 1990 Oct;64(10):4830-5

Date

10/01/1990

Pubmed ID

2168971

Pubmed Central ID

PMC247971

DOI

10.1128/JVI.64.10.4830-4835.1990

Scopus ID

2-s2.0-0025066089 (requires institutional sign-in at Scopus site)   55 Citations

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.

Author List

Willoughby RE, Yolken RH, Schnaar RL

Author

Rodney E. Willoughby MD Professor in the Pediatrics department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Animals
Cattle
Cell Line
G(M1) Ganglioside
Glycolipids
Glycosphingolipids
Intestines
Mice
Rotavirus
Species Specificity
Viral Plaque Assay
Virus Replication