Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells.
The chemical nature of receptors involved in the attachment of simian rotavirus (SA-11) to a monkey kidney cell line (LLC-MK2) was investigated. Enzymic treatment of cells before virus infection indicated that membrane proteins and phospholipids are not involved in virus attachment, whereas sialic acid and galactose participate in the receptor structure to differing extents. Incubation of SA-11 with bovine brain gangliosides before infection strongly reduced its ability to bind to cell membranes. Similar experiments with individual purified gangliosides from bovine brain showed that virus infection was prevented by preincubation with GM1. Moreover, desialylated cells regained susceptibility to virus infection when coated with whole gangliosides or GM1 immediately after Clostridium perfringens neuraminidase treatment. The binding of SA-11 to whole gangliosides or GM1 was quantified by an ELISA procedure. The results suggest that gangliosides, mainly GM1, are part of the receptor structure for SA-11 of susceptible LLC-MK2 cells.
Superti
F
F
Department of Ultrastructures, Istituto Superiore di Sanità, Rome, Italy.
Donelli
G
G
D000818:Animals; D001667:Binding, Competitive; D002460:Cell Line; D010450:Endopeptidases / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D005732:Gangliosides / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism; D008049:Lipase / Q000378:metabolism; D009439:Neuraminidase / Q000378:metabolism; D011991:Receptors, Virus / Q000378:metabolism*; D012401:Rotavirus / Q000378:metabolism* / Q000502:physiology; D014779:Virus Replication
D005732:Gangliosides; D011991:Receptors, Virus; D008049:Lipase; D006026:Glycoside Hydrolases; D009439:Neuraminidase; D010450:Endopeptidases