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J Virol. 1990 October; 64(10): 4830-4835
Rotaviruses specifically bind to the neutral glycosphingolipid asialo-GM1.
R E Willoughby,
R H Yolken and
R L Schnaar
Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
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.
J Virol. 1990 October; 64(10): 4830-4835
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Copyright © 1990 by the American Society for Microbiology. All rights reserved.