Investigation of the role of glycans for the biological activity of Semliki Forest virus grown in Aedes albopictus cells using inhibitors of asparagine-linked oligosaccharides trimming.
The effects of N-linked-oligosaccharide-processing inhibitors on the formation of Semliki Forest virus (SFV) in C6/36 Aedes albopictus cells were investigated. The glycosidase inhibitors deoxynojirimycin, deoxymannojirimycin and swainsonine prevented the formation of Endo-H resistant structures, but had little effect on virus formation and on the biological activities of the virus. Tunicamycin greatly inhibited virus formation, but had little effect on cell-cell fusion from within and the cleavage of p 62. These results indicate that correct glycosylation is not a prerequisite for biological activities of SFV, whereas glycosylation per se is needed for virus production.
Naim
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Institute for Hygiene and Medical Microbiology, University of Berne, Switzerland.
Koblet
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D017485:1-Deoxynojirimycin; D000330:Aedes; D000470:Alkaloids / Q000494:pharmacology; D000818:Animals; D005936:Glucans / Q000502:physiology; D005944:Glucosamine / Q000031:analogs & derivatives / Q000494:pharmacology; D006023:Glycoproteins / Q000502:physiology*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006031:Glycosylation; D006596:Hexosaminidases / Q000494:pharmacology; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008561:Membrane Fusion; D008970:Molecular Weight; D012672:Semliki forest virus / Q000502:physiology*; D017026:Swainsonine; D014415:Tunicamycin / Q000494:pharmacology; D014759:Viral Envelope Proteins / Q000378:metabolism; D014779:Virus Replication / Q000187:drug effects*
D000470:Alkaloids; D005936:Glucans; D006023:Glycoproteins; D014759:Viral Envelope Proteins; D014415:Tunicamycin; D017485:1-Deoxynojirimycin; D006026:Glycoside Hydrolases; D006596:Hexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D005944:Glucosamine; D017026:Swainsonine