Rotaviruses specifically bind to the neutral glycosphingolipid asialo-GM1.
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.
Willoughby
R E
RE
Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Yolken
R H
RH
Schnaar
R L
RL
D000818:Animals; D002417:Cattle; D002460:Cell Line; D005677:G(M1) Ganglioside; D006017:Glycolipids / Q000302:isolation & purification / Q000378:metabolism; D006028:Glycosphingolipids / Q000302:isolation & purification / Q000378:metabolism*; D007422:Intestines / Q000032:analysis; D051379:Mice; D012401:Rotavirus / Q000502:physiology*; D013045:Species Specificity; D010948:Viral Plaque Assay; D014779:Virus Replication
D006017:Glycolipids; D006028:Glycosphingolipids; D005677:G(M1) Ganglioside; C018835:asialo GM1 ganglioside